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5-phospho-D-ribosyl diphosphate + H2O
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Substrates: 40.73% activity compared to D-fructose 1,6-bisphosphate
Products: -
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beta-D-glucose 1,6-bisphosphate + H2O
D-glucose 6-phosphate + phosphate
beta-glycerophosphate + H2O
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Substrates: substrate at pH 9.0, no activity at pH 6.5
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
D-fructose 1,6-diphosphate + H2O
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D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
D-fructose 1-phosphate + H2O
D-fructose + phosphate
Substrates: -
Products: -
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D-fructose 6-phosphate + phosphate
D-fructose 1,6-diphosphate + H2O
-
Substrates: -
Products: -
r
D-glucose 1,6-bisphosphate + H2O
D-glucose 6-phosphate + phosphate
Substrates: -
Products: -
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D-glucose 6-phosphate + H2O
D-glucose + phosphate
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Substrates: 23% of the activity found with D-fructose 1,6-bisphosphate
Products: -
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D-glucose-1-phosphate + H2O
D-glucose + phosphate
Substrates: -
Products: -
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glucose 1,6-diphosphate + H2O
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Substrates: about 10% of maximal activity
Products: -
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glyceraldehyde 3-phosphate + H2O
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Substrates: 11.43% of the activity compared to D-fructose 1,6-bisphosphate
Products: -
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glycerol-2-phosphate + H2O
glycerol + phosphate
Substrates: -
Products: -
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GTP + H2O
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Substrates: 22.9% of the activity compared to D-fructose 1,6-bisphosphate
Products: -
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Ikappabeta alpha phosphate + H2O
Ikappabeta alpha + phosphate
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
Substrates: -
Products: -
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phosphoribosyl diphosphate + H2O
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Substrates: 40.73% of the activity compared to D-fructose 1,6-bisphosphate
Products: -
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ribulose 1,5-bisphosphate + H2O
ribulose 5-phosphate + phosphate
Substrates: 15% of activity obtained with D-fructose 1,6-bisphosphate
Products: -
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ribulose 1,5-diphosphate + H2O
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sedoheptulose 1,6-diphosphate + H2O
sedoheptulose 6-phosphate + phosphate
-
Substrates: -
Products: -
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sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
additional information
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beta-D-glucose 1,6-bisphosphate + H2O

D-glucose 6-phosphate + phosphate
-
Substrates: -
Products: -
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beta-D-glucose 1,6-bisphosphate + H2O
D-glucose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O

D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Campylobacter jejuni serotype O:2
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Campylobacter jejuni serotype O:2 ATCC 700819
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Campylobacter jejuni serotype O:2 NCTC 11168
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
E2RAN6
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: Fbp plays a key role in gluconeogenesis that supplies cellular building blocks such as hexose and intermediates of the pentose phosphate pathway for cell growth. Fructose-1,6-bisphosphatase increases its abundance by 2.0-2.7fold on various aromatic compounds. Fbp plays a key role in aromatic assimilation by Coryneacterium glutamicum. The Fbp gene is disrupted and the mutant WTDfbp loses the ability to grow on aromatic compounds. Genetic complementation by the Fbp gene restores this ability
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: best substrate
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: enzyme functions with FBPase I in the centarle pathways of carbohydrate metabolism
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
A0A7T7JA26
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: enzyme is a part of Calvin cycle
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: the the chloroplastic isozyme plays a key role in the Calvin cycle and the cytoplasmic isozyme plays a key role in the sucrose synthesis in cytoplasm
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is highly specific for D-fructose 1,6-bisphosphate. At 1 mM substrate, activity is only 40% of the activity at 0.06 mM substrate
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: gluconeogenic enzyme
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Picosynechococcus sp. PCC 7002 ATCC 27264
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Picosynechococcus sp. PCC 7002 PR-6
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: preferred substrate
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: key enzyme of the gluconeogenic pathway
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: preferred substrate
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: preferred substrate
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: preferred substrate
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis. It catalyses a multi-step reaction by remodelling its active site according to the respective catalytic requirements
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis. It catalyses a multi-step reaction by remodelling its active site according to the respective catalytic requirements
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: regulatory enzyme of glyconeogenesis. FBPase participates in some nuclear processes during development and regeneration of skeletal muscle
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: the coregulation of phosphofructo 1-kinase I and fructose 1,6-bisphosphatase are required for the ability of these cells to respond to glucose and induce metabolic and Ca2+ signals that can be important for sperm development and function
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: best substrate
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: the substrate is bound in its linear, open conformation with the cleavable C1-phosphate positioned deep in the active site
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: one of the key enzymes in gluconeogenesis
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: the bifunctional enzyme also shows activity of EC 4.1.2.13. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions
Products: -
r
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: the bifunctional enzyme also shows activity of EC 4.1.2.13. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions
Products: -
r
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: FBPase contributes to the partitioning of the fixed carbon for ribulose-1,5-bisphosphate regeneration or starch synthesis
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: best substrate
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: the enzyme plays a key role in the Calvin cycle
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
ir
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O

?
-
Substrates: key regulatory enzyme in the control of the Emden-Meyerhof pathway
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: key regulatory enzyme in the control of the Emden-Meyerhof pathway
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: constitutive enzyme
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: the enzyme is involved in the futile cycling of fructose 6-phosphate and fructose 1,6-diphosphate in flight muscle, the net result of which is the hydrolysis of ATP
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: enzyme in gluconeogenic pathway
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: enzyme plays a key regulatory role in the futile cycle of fructose 1,6-diphosphate synthesis and degradation
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: the alkaline isoenzyme may have an important role in vivo in the regulation and control of glycolysis and glyconeogenesis
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: gluconeogenic enzyme
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: regulatory enzyme in gluconeogenesis
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: enzyme is involved in photosynthetic process
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: isoenzyme A is present when the organism is grown under autotrophic conditions but is not synthesized during heterotrophic growth. Isoenzyme B is detected in both autothrophically and heterotrophically grown organisms
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: the enzyme may be involved in the regulation of the Calvin-Bassham carbon reduction cycle
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: key regulatory enzyme in carbohydrate synthesis in both gluconeogenesis and photosynthesis
Products: -
?
D-fructose 1,6-diphosphate + H2O

D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
r
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
170737, 170740, 170741, 170744, 170747, 170762, 170765, 170772, 170776, 170777, 170782, 170806 Substrates: -
Products: -
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D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is a part of Calvin cycle
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
Ikappabeta alpha phosphate + H2O

Ikappabeta alpha + phosphate
Substrates: purified recombinant His-tagged FBP1 proteins. Wild-type FBP1, but not FBP1 ED, dephosphorylated TNFalpha-induced IkappaB pS32/36
Products: -
?
Ikappabeta alpha phosphate + H2O
Ikappabeta alpha + phosphate
Substrates: NF-kappa-B inhibitor alpha = Ikappabeta alpha catalytic mechanism, overview
Products: -
?
ribulose 1,5-diphosphate + H2O

?
-
Substrates: -
Products: -
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ribulose 1,5-diphosphate + H2O
?
-
Substrates: intestinal and muscle enzyme
Products: -
?
ribulose 1,5-diphosphate + H2O
?
-
Substrates: -
Products: -
?
ribulose 1,5-diphosphate + H2O
?
-
Substrates: 23% of the activity with fructose 1,6-diphosphate
Products: -
?
ribulose 1,5-diphosphate + H2O
?
-
Substrates: -
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O

sedoheptulose 7-phosphate + phosphate
-
Substrates: no activity
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
Substrates: -
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
Substrates: -
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
Substrates: intestinal and muscle enzyme
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
Substrates: -
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
Substrates: 81% of the activity with fructose 1,6-diphosphate
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
Substrates: -
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
Substrates: at 22.4% of the activity with fructose 1,6-diphosphate
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
Substrates: about 5% of maximal activity
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
Substrates: no activity
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
Substrates: -
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
Substrates: activity with isoenzyme F-1, no activity with isoenzyme F-II
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
Substrates: -
Products: -
?
sedoheptulose 1,7-bisphosphate + H2O
sedoheptulose 7-phosphate + phosphate
-
Substrates: no activity
Products: -
?
additional information

?
-
-
Substrates: role as a key enzyme in CO2 assimilation and also in coordinating carbon and nitrogen metabolism
Products: -
?
additional information
?
-
-
Substrates: bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
Products: -
?
additional information
?
-
I3DTM3
Substrates: the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
Products: -
?
additional information
?
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Substrates: the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
Products: -
?
additional information
?
-
-
Substrates: the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
Products: -
?
additional information
?
-
I3DTM3
Substrates: the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
Products: -
?
additional information
?
-
Substrates: the chromosome-encoded isoform is the major fructose 1,6-bisphosphatase of Bacillus methanolicus
Products: -
?
additional information
?
-
-
Substrates: bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
Products: -
?
additional information
?
-
-
Substrates: quantification of phosphate by the malachite green assay. Substrate recognition and binding analysis, structure comparisons, overview. The binding of the PO4-6 phosphate is characterized by an Arg-Pro-Arg motif
Products: -
-
additional information
?
-
-
Substrates: enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
Products: -
?
additional information
?
-
-
Substrates: the FBP active site works by stabilizing the FBPase, and the allosteric site impairs the activity of FBPase through its binding of a nonsubstrate molecule. Competitive inhibition of AMP, fructose 1,6-bisphosphate, or fructose 6-phosphate binding to FBPase with fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP)-binding FBPase
Products: -
?
additional information
?
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Substrates: the binding mode of IkappaB pS32/36 with FBP1 is similar to that of F-1,6-BP with FBP1. The dominant residues in FBP1 responsible for its binding with IkappaBalpha pS32/36 are R244, K275, S124, R314, K270, G123, R277, N213, and K208. Among these residues, R244, K275, N213, K270, and K208 directly interact with pS36, which is not located in the Mg2+ catalytic reaction center
Products: -
-
additional information
?
-
-
Substrates: bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
Products: -
?
additional information
?
-
Substrates: the higher Km for D-fructose 1,6-bisphosphate of LmFBPase compared to the Escherichia coli enzyme may be explained by a sequence difference at the active site, with Tyr221 replaced by Asn221 resulting in the loss of a direct hydrogen bond with substrate D-fructose 1,6-bisphosphate. Binding structure analysis of substrate and product, overview
Products: -
?
additional information
?
-
-
Substrates: the higher Km for D-fructose 1,6-bisphosphate of LmFBPase compared to the Escherichia coli enzyme may be explained by a sequence difference at the active site, with Tyr221 replaced by Asn221 resulting in the loss of a direct hydrogen bond with substrate D-fructose 1,6-bisphosphate. Binding structure analysis of substrate and product, overview
Products: -
?
additional information
?
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-
Substrates: in the assay, fructose-1,6-bisphosphatase hydrolyzes fructose-1,6-bisphosphate into fructose-6-phosphate. Fructose-6-phosphate is used in an enzyme-coupled reaction system that measures spectrophotometrically at 450 nm
Products: -
-
additional information
?
-
-
Substrates: no substrate: D-glucose 1-phosphate, D-glucose 6-phosphate, sorbitol 6-phosphate, phosphoenolpyruvate, D-fructose 6-phosphate, 3-glycerate phosphate, dihydroxyacetone
Products: -
?
additional information
?
-
Substrates: substrate binding analysis of wild-type and mutant enzymes by surface plasmon resonance method, substrate affinities, overview
Products: -
?
additional information
?
-
Substrates: quantification of phosphate by the malachite green assay. Substrate recognition and binding analysis, structure comparisons, overview. The binding of the PO4-6 phosphate is characterized by an Arg-Pro-Arg motif
Products: -
-
additional information
?
-
Substrates: substrate binding analysis of wild-type and mutant enzymes by surface plasmon resonance method, substrate affinities, overview
Products: -
?
additional information
?
-
Substrates: substrate binding analysis of wild-type and mutant enzymes by surface plasmon resonance method, substrate affinities, overview
Products: -
?
additional information
?
-
Substrates: purified recombinant Pcal_0111 catalyzes both phosphatase and aldolase reactions with specific activity values of 4 U and 1.3 U, respectively. Although the enzyme can utilize several substrates for dephosphorylation, no phosphatase activity is detected with AMP, UTP, NADP, glucose 6-phosphate, ribose 5-phosphate, riboflavin 5-monophosphate, and pyridoxal 5-phosphate. Varying amounts of phosphatase activity are found when ATP, GTP, ADP, CTP, glyceraldehyde 3-phosphate, fructose 6-phosphate, fructose 1,6-bisphosphate, and phosphoribosyl diphosphate are used as substrates. The highest phosphatase activity is found with fructose 1,6-bisphosphate followed by phosphoribosyl diphosphate. Spectrophotometric coupled enzyme assay as discontinuous assay method, or product phosphate detection by malachite green assay method. Substrate binding residues include Tyr229, Lys232, and Tyr358
Products: -
?
additional information
?
-
Substrates: no phosphatase activity could be detected with AMP, UTP, NADP, glucose 6-phosphate, ribose 5-phosphate, riboflavin 5-monophosphate, and pyridoxal 5-phosphate
Products: -
?
additional information
?
-
-
Substrates: enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
Products: -
?
additional information
?
-
-
Substrates: enzyme influences the connection between DNA damage, aging and oxidative stress
Products: -
?
additional information
?
-
Substrates: purified YK23 exhibits high phosphatase activity against fructose 1,6-bisphosphate, significant hydrolytic activity toward fructose 1-phosphate, and detectable activity with glyceraldehyde 3-phosphate, erythrose 4-phosphate, and ribulose 1,5-diphosphate
Products: -
?
additional information
?
-
-
Substrates: purified YK23 exhibits high phosphatase activity against fructose 1,6-bisphosphate, significant hydrolytic activity toward fructose 1-phosphate, and detectable activity with glyceraldehyde 3-phosphate, erythrose 4-phosphate, and ribulose 1,5-diphosphate
Products: -
?
additional information
?
-
-
Substrates: binding of the first substrate molecule, in one dimer of the enzyme, produces a conformational change at the other dimer, reducing the substrate affinity and catalytic activity of its subunits
Products: -
?
additional information
?
-
Substrates: not: D-fructose 1-phosphate, D-fructose 6-phosphate, D-fructose 2,6-bisphosphate, glycerol 3-phosphate, glycerol 1-phosphate
Products: -
?
additional information
?
-
-
Substrates: not: D-fructose 1-phosphate, D-fructose 6-phosphate, D-fructose 2,6-bisphosphate, glycerol 3-phosphate, glycerol 1-phosphate
Products: -
?
additional information
?
-
-
Substrates: the enzyme TNA1-Fbp has broad substrate specificities for D-fructose-1,6-bisphosphate and its analogues including D-fructose 1-bisphosphate, D-fructose 6-phosphate, D-glucose 1-phosphate, D-glucose 6-phosphate, glycerol 2-phosphate, and phosphoenolpyruvate, as well as AMP, ADP ATP, substrate specificity, overview
Products: -
?
additional information
?
-
Substrates: a dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase) exhibiting activity of EC 3.1.3.37, sedoheptulose 1,7-diphosphatase, and 3.1.3.11, fructose 1,6-bisphosphatase
Products: -
?
additional information
?
-
-
Substrates: optimization of a coupled enzyme assay that uses fluorescence, which is more sensitive than absorbance at 340 nm, to measure NADPH production over time, FBPase enzyme activity can be determined with as little as 125 pg of recombinant enzyme
Products: -
-
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
D-fructose 1,6-diphosphate + H2O
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
Ikappabeta alpha phosphate + H2O
Ikappabeta alpha + phosphate
Substrates: purified recombinant His-tagged FBP1 proteins. Wild-type FBP1, but not FBP1 ED, dephosphorylated TNFalpha-induced IkappaB pS32/36
Products: -
?
additional information
?
-
D-fructose 1,6-bisphosphate + H2O

D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Campylobacter jejuni serotype O:2
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Campylobacter jejuni serotype O:2 ATCC 700819
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Campylobacter jejuni serotype O:2 NCTC 11168
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
E2RAN6
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: Fbp plays a key role in gluconeogenesis that supplies cellular building blocks such as hexose and intermediates of the pentose phosphate pathway for cell growth. Fructose-1,6-bisphosphatase increases its abundance by 2.0-2.7fold on various aromatic compounds. Fbp plays a key role in aromatic assimilation by Coryneacterium glutamicum. The Fbp gene is disrupted and the mutant WTDfbp loses the ability to grow on aromatic compounds. Genetic complementation by the Fbp gene restores this ability
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: enzyme functions with FBPase I in the centarle pathways of carbohydrate metabolism
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
A0A7T7JA26
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: enzyme is a part of Calvin cycle
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: the the chloroplastic isozyme plays a key role in the Calvin cycle and the cytoplasmic isozyme plays a key role in the sucrose synthesis in cytoplasm
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: gluconeogenic enzyme
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Picosynechococcus sp. PCC 7002 ATCC 27264
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Picosynechococcus sp. PCC 7002 PR-6
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: key enzyme of the gluconeogenic pathway
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
Products: -
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D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: the bifunctional, thermostable enzyme (EC 4.1.2.13/EC 3.1.3.11) catalyses two subsequent steps in gluconeogenesis in most archaea and in deeply branching bacterial lineages
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: regulatory enzyme of glyconeogenesis. FBPase participates in some nuclear processes during development and regeneration of skeletal muscle
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: the coregulation of phosphofructo 1-kinase I and fructose 1,6-bisphosphatase are required for the ability of these cells to respond to glucose and induce metabolic and Ca2+ signals that can be important for sperm development and function
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: best substrate
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: one of the key enzymes in gluconeogenesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: FBPase contributes to the partitioning of the fixed carbon for ribulose-1,5-bisphosphate regeneration or starch synthesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: the enzyme plays a key role in the Calvin cycle
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
?
D-fructose 1,6-bisphosphate + H2O
D-fructose 6-phosphate + phosphate
-
Substrates: -
Products: -
ir
D-fructose 1,6-diphosphate + H2O

?
-
Substrates: key regulatory enzyme in the control of the Emden-Meyerhof pathway
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: key regulatory enzyme in the control of the Emden-Meyerhof pathway
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: constitutive enzyme
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: the enzyme is involved in the futile cycling of fructose 6-phosphate and fructose 1,6-diphosphate in flight muscle, the net result of which is the hydrolysis of ATP
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: enzyme in gluconeogenic pathway
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: enzyme plays a key regulatory role in the futile cycle of fructose 1,6-diphosphate synthesis and degradation
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: the alkaline isoenzyme may have an important role in vivo in the regulation and control of glycolysis and glyconeogenesis
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: gluconeogenic enzyme
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: regulatory enzyme in gluconeogenesis
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: enzyme is involved in photosynthetic process
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: isoenzyme A is present when the organism is grown under autotrophic conditions but is not synthesized during heterotrophic growth. Isoenzyme B is detected in both autothrophically and heterotrophically grown organisms
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: the enzyme may be involved in the regulation of the Calvin-Bassham carbon reduction cycle
Products: -
?
D-fructose 1,6-diphosphate + H2O
?
-
Substrates: key regulatory enzyme in carbohydrate synthesis in both gluconeogenesis and photosynthesis
Products: -
?
D-fructose 1,6-diphosphate + H2O

D-fructose 6-phosphate + phosphate
-
Substrates: enzyme is a part of Calvin cycle
Products: -
?
D-fructose 1,6-diphosphate + H2O
D-fructose 6-phosphate + phosphate
Substrates: enzyme is usually regarded as a regulatory enzyme of gluconeogenesis
Products: -
?
additional information

?
-
-
Substrates: role as a key enzyme in CO2 assimilation and also in coordinating carbon and nitrogen metabolism
Products: -
?
additional information
?
-
-
Substrates: bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
Products: -
?
additional information
?
-
-
Substrates: bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
Products: -
?
additional information
?
-
-
Substrates: enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
Products: -
?
additional information
?
-
-
Substrates: bifunctional fructose 1,6-bisphosphate, FBP, aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity
Products: -
?
additional information
?
-
-
Substrates: enzyme together with phosphofructokinase plays a crucial role in metabolism of pancreatic islet cells
Products: -
?
additional information
?
-
-
Substrates: enzyme influences the connection between DNA damage, aging and oxidative stress
Products: -
?
additional information
?
-
Substrates: a dual-function fructose-1,6/sedoheptulose-1,7-bisphosphatase (FBP/SBPase) exhibiting activity of EC 3.1.3.37, sedoheptulose 1,7-diphosphatase, and 3.1.3.11, fructose 1,6-bisphosphatase
Products: -
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(1H-indol-1-yl)(4-(trifluoromethyl)phenyl)methanone
-
-
(2,3-diethoxy-7,8,9,10-tetrahydro-6H-cyclohepta[b]quinolin-11-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
-
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl)methyl dihydrogen phosphate
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl)phosphonic acid
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)methyl dihydrogen phosphate
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)phosphonic acid
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl)methyl dihydrogen phosphate
-
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl)phosphonic acid
-
(2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl)methyl dihydrogen phosphate
-
(2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl)phosphonic acid
-
(2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl)methyl dihydrogen phosphate
-
(2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl)phosphonic acid
-
(2-amino-8H-indeno[1,2-d][1,3]thiazol-5-yl)methyl dihydrogen phosphate
-
(2-amino-8H-indeno[1,2-d][1,3]thiazol-5-yl)phosphonic acid
-
(2-amino-8H-indeno[1,2-d][1,3]thiazol-6-yl)methyl dihydrogen phosphate
-
(2-amino-8H-indeno[1,2-d][1,3]thiazol-6-yl)phosphonic acid
-
(2-aminomethyl-6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]-amine
-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
(3-Bromo-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
-
IC50: 0.0017 mM
(3-Bromo-phenyl)-(6,7-dimethoxy-2-methyl-quinazolin-4-yl)-amine
-
IC50: 0.0045 mM
(3-Bromo-phenyl)-(6,7-dimethoxy-quinazolin-4-yl)-amine
-
IC50: 0.001 mM
(3-Bromo-phenyl)-(7-ethoxy-6-nitro-quinazolin-4-yl)-amine
-
IC50: 0.0039 mM
(3-Bromo-phenyl)-[6-(2-methoxy-ethoxy)-quinazolin-4-yl]-amine
-
IC50: 0.0029 mM
(3-Bromo-phenyl)-[7-methoxy-6-(2-methoxy-ethoxy)-quinazolin-4-yl]-amine
-
IC50: 0.0055 mM
(3-Chloro-4-fluoro-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
-
IC50: 0.00053 mM
(3-Chloro-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
-
IC50: 0.0016 mM
(3-Chloro-phenyl)-(6,7-dimethoxy-quinazolin-4-yl)-amine
-
IC50: 0.0013 mM
(4-(3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl)-thiazol-2-yl)-methanol
an allosteric inhibitor
-
(4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol
(5-[2-amino-5-[(propylsulfanyl)carbonyl]-1,3-thiazol-4-yl]furan-2-yl)phosphonic acid
-
-
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid
(6,7-diethoxy-1,2,3,4-tetrahydroacridin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
-
-
(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
-
-
(6,7-Diethoxy-quinazolin-4-yl)-(3-ethynyl-phenyl)-amine
-
IC50: 0.0024 mM
(6,7-Diethoxy-quinazolin-4-yl)-(3-fluoro-phenyl)-amine
-
IC50: 0.0092 mM
(6,7-Diethoxy-quinazolin-4-yl)-(3-iodo-phenyl)-amine
-
IC50: 0.0021 mM
(6,7-Dimethoxy-quinazolin-4-yl)-(3-ethynyl-phenyl)-amine
-
IC50: 0.0009 mM
1-(cyclopropyl)methyl-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
1-benzyl-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
1-Fluoro-2,4-dinitrobenzene
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate
2,5-anhydromannitol 1,6-diphosphate
-
-
2,5-dichloro-N-(4-methyl-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
2,5-dichloro-N-(5-methyl-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2,5-dichloro-N-(6-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2,5-dichloro-N-(6-methoxy-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2,5-dichloro-N-(6-methyl-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2,5-dichloro-N-[5-(3-furyl)-1,3-benzoxazol-2-yl]benzenesulfonamide
-
-
2,5-dichloro-N-[5-methoxy-7-(4-methoxypyridin-3-yl)-1,3-benzoxazol-2-yl]benzenesulfonamide
-
-
2,5-dichloro-N-[7-(3-hydroxyphenyl)-5-methoxy-1,3-benzoxazol-2-yl]benzenesulfonamide
-
-
2,5-dichloro-N-[7-(4-hydroxyphenyl)-5-methoxy-1,3-benzoxazol-2-yl]benzenesulfonamide
-
-
2-(2-(phenylamino)thiazol-4-yl)phenol
-
2-(2-aminoethyl)-6,7-diethoxy-N-[3-(2-methyl-1,3-thiazol-4-yl)phenyl]quinazolin-4-amine
-
uncompetitive
2-(2-thienyl)-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-(3,4-dihydroxyphenyl)-3,7,8-trihydroxy-4H-1-benzopyran-4-one
-
2-(3,4-dihydroxyphenyl)-3-hydroxy-4H-1-benzopyran-4-one
-
2-(3,4-dihydroxyphenyl)-3-hydroxy-7,8-dimethoxy-4H-1-benzopyran-4-one
-
2-(3,4-dihydroxyphenyl)-4H-1-benzopyran-4-one
-
2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-3-[[(2R,3R,4S,5R,6R)-3,4,5-trihydroxy-6-[[(2R,3S,4S,5R)-3,4,5,6-tetrahydroxyoxan-2-yl]methoxy]oxan-2-yl]oxy]-4H-1-benzopyran-4-one
-
2-(3,4-dihydroxyphenyl)-5-hydroxy-4H-1-benzopyran-4-one
-
2-(3,4-dihydroxyphenyl)-7-hydroxy-4H-1-benzopyran-4-one
-
2-(3,4-dimethoxyphenyl)-3,7,8-trihydroxy-4H-1-benzopyran-4-one
-
2-(3,4-dimethoxyphenyl)-3-hydroxy-4H-1-benzopyran-4-one
-
2-(3,4-dimethoxyphenyl)-3-hydroxy-7,8-diphenoxy-4H-1-benzopyran-4-one
-
2-(3,4-dimethoxyphenyl)-5,7-dihydroxy-4H-1-benzopyran-4-one
-
2-(3,4-diphenoxyphenyl)-3-hydroxy-7,8-dimethoxy-4H-1-benzopyran-4-one
-
2-(3-hydroxyphenyl)-4H-1-benzopyran-4-one
-
2-(3-pyridyl)-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-(4-(4-hydroxyphenyl)thiazol-2-ylamino)phenol
-
2-(4-hydroxyphenyl)-4H-1-benzopyran-4-one
-
2-(4-phenylthiazol-2-ylamino)phenol
-
2-acetamido-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl dihydrogen phosphate
-
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl dihydrogen phosphate
-
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl dihydrogen phosphate
-
2-amino-4-[1-(3-phosphono)phenyl]thiazole
-
-
2-amino-4-[2-(5-(1-(3-bromophenyl)-1,3-propyl)phosphono)-furanyl]-5-isobutyl-thiazole
-
-
2-amino-4-[2-(5-(O-phenyl)-(N-((S)-1-ethoxycarbonyl)ethyl)-phosphonamido)-furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-(5-bis(p-acetoxybenzyl)phosphono)furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-(5-diphenylphosphono)furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-(5-monophenyl-monoamino-phosphono)furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-(5-monophenylphosphono)furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-(5-N,N'-bis((S)-1-(1-ethoxycarbonyl)ethyl)phosphonoamido)furanyl]-5-isobutylthiazole
-
optimization of the diamide prodrugs of phosphonic acid leads to the identification of a new diamide, the first reported orally efficacious FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-ethoxycarbonylthiazole
2-amino-4-[2-(5-phosphono)furanyl]-5-isobutylthiazole
2-amino-4-[2-(5-phosphono)furanyl]-5-phenylthiazole
2-amino-4-[2-(5-phosphono)furanyl]-5-propylsulfanylthiazole
2-amino-4-[2-(6-phosphono)pyridyl]thiazole
-
-
2-amino-4-[2-[5-(1-(4-pyridyl)-1,3-propyl)phosphono]furanyl]-5-isobutylthiazole
-
-
2-amino-4-[2-[5-bis(1-(1-ethoxycarbonyloxy)ethyl)phosphono]-furanyl]-5-isobutyl-thiazole
-
-
2-amino-4-[2-[5-bis(ethoxycarbonyloxymethyl)phosphono]-furanyl]-5-isobutyl-thiazole
-
-
2-amino-4-[2-[5-bis(phenoxycarbonyloxymethyl)phosphono]-furanyl]-5-isobutyl-thiazole
-
-
2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl dihydrogen phosphate
-
2-amino-5-(2,2,2-trifluoroethyl)-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-(2-furanyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(2-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-(2-naphthyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(2-thienyl)-4-[(N-phosphonomethyl)carbamoyl]-thiazole
-
-
2-amino-5-(2-thienyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(3-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-(4-acetylphenyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(4-chlorophenyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(4-fluorophenyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(4-methanesulfonyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(4-methoxycarbonylphenyl)-4-[2-(5-phosphono)-furanyl]thiazole
-
-
2-amino-5-(4-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-(4-methylthiophenyl)-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-(4-phenylphenyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-(4-tert-butylphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-(N-morpholinyl)-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-benzyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-benzyloxycarbonyl-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-bromo-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-chloro-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-cyclobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-cyclohexyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-cyclohexylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-cyclopentyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-cyclopentylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-cyclopropylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-amino-5-ethylthio-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-hydroxymethyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-iodo-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
2-amino-5-isopropyl- 4-[1-(4-methoxy-3-phosphono)phenyl]-thiazole
-
-
2-amino-5-isopropyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-isopropylthio-4-[2-(5-phosphono)furanyl]thiazole hydrobromide
-
-
2-amino-5-methyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-methylsulfanyl-4-[2-(5-diethylphosphono)furanyl]thiazole
2-amino-5-neopentyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-phenyl- 4-[1-(4-fluoro-3-phosphono)phenyl]thiazole
-
-
2-amino-5-phenyl-4-[2-(5-methyl-4-phosphono)oxazolyl]-thiazole
-
-
2-amino-5-phenyl-4-[3-(1-phosphono)pyrrolyl]thiazole
-
-
2-amino-5-phenylthio-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-propyl- 4-[1-(4-methyl-3-phosphono)phenyl]thiazole
-
-
2-amino-5-propyl-4-phosphonomethoxycarbonylthiazole
-
-
2-amino-5-propyl-4-[1-(3-phosphono)phenyl]thiazole
-
-
2-amino-5-propyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-tert-butylthio-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-amino-5-[(4-morpholinyl)methyl]-4-[2-(5-phosphono)furanyl]-thiazole dihydrobromide
-
-
2-amino-5-[(N,N-dimethyl)carbamoyl]-4-[2-(5-phosphono)-furanyl]thiazole
-
-
2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl dihydrogen phosphate
-
2-amino-8H-indeno[1,2-d][1,3]thiazol-5-yl dihydrogen phosphate
-
2-amino-8H-indeno[1,2-d][1,3]thiazol-6-yl dihydrogen phosphate
-
2-bromo-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-bromo-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2-carbamoyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-chloro-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-cyano-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-deoxyribose-5-phosphate
-
-
2-ethyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-hydroxymethyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-methyl-5-isobutyl-4-[2-(5-phosphono)furanyl]-thiazole
-
-
2-methylamino-5-isobutyl-4-[2-(5-hosphono)furanyl]thiazole
-
-
2-methylthio-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-phenyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-phosphoglycerate
Campylobacter jejuni serotype O:2
slight inhibition
2-thiocarbamoyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-vinyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
2-[(3S,11aS)-3-(4-hydroxybenzyl)-1,4-dioxo-1,3,4,6,11,11a-hexahydro-2H-pyrazino[1,2-b]isoquinolin-2-yl]-N-[2-(4-hydroxyphenyl)ethyl]pentanamide
-
uncompetitive
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate
3,4-dihydroxy-N'-[(E)-[4-oxo-6-(propan-2-yl)-4H-chromen-3-yl]methylidene]benzohydrazide
compound potently inhibits both fructose-1,6-bisphoshate aldolase and fructose-1,6-bisphosphatase with IC50 values below 30 microM
3,5-diphenyl-1-(3-(trifluoromethyl) phenyl)-1H-pyrazole
-
-
3,6,8-trichloro-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-1-benzopyran-4-one
-
3,8-dichloro-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-1-benzopyran-4-one
-
3-(2-(ethoxycarbonyl)-7-nitro-1H-indol-3-yl)propanoic acid
-
3-(2-carboxyethyl)-4,6-dichloro-1H-indole-2-carboxylic acid
3-(2-carboxyethyl)-4-(2-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(2-methylpropyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(3-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(3-methoxyanilino)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(3-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(4-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(4-methoxyanilino)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-(4-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-chloro-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-ethyl-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-4-isobutyl-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-(2-methylpropyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-bromo-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-chloro-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-cyclopropyl-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-ethyl-7-methyl-1H-indole-2-carboxylic acid
8.2% inhibition at 0.01 mM
3-(2-carboxyethyl)-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-ethyl-7-nitro-1H-indole-2-carboxylicacid
-
3-(2-carboxyethyl)-5-isobutyl-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-5-phenylamino-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-chloro-5-cyclopropyl-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-chloro-5-ethyl-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-chloro-5-propyl-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(3-methoxyphenylamino)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(3-nitrophenyl)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(4-methoxyphenylamino)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-(4-nitrophenyl)-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-phenyl-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-4-phenylamino-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-5-phenyl-1H-indole-2-carboxylic acid
-
3-(2-carboxyethyl)-7-nitro-5-propyl-1H-indole-2-carboxylic acid
-
3-(3-amino-3-oxopropyl)-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
-
3-(4-(4-hydroxyphenyl)thiazol-2-ylamino)benzenesulfonamide
-
3-(4-(4-hydroxyphenyl)thiazol-2-ylamino)phenol
-
3-(4-phenylthiazol-2-ylamino)benzenesulfonamide
-
3-(4-phenylthiazol-2-ylamino)phenol
-
3-chloro-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-1-benzopyran-4-one
-
3-chloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
3-chloro-N-[(3,5-dichlorophenyl)carbamoyl]benzenesulfonamide
3-ethyl-5-isobutyl-7-nitro-1H-indole-2-carboxylic acid
-
molecular modeling of binding mode. The key hydrogen bonding interactions are observed between the carboxylate and residues Thr 27, Lys 112 and Arg 140, which are also recognized by the phosphate group in AMP. This hydrogen bonding network may make crucial contributions to the binding affinity. The indole ring is situated in a hydrophobic pocket involved in residues Leu30 and Leu34. The 7-nitro group interacted with the hydroxyl group of Thr31 via a hydrogen bond
3-hydroxy-7-methoxy-2-(3-methoxyphenyl)-4H-1-benzopyran-4-one
-
3-hydroxy-7-methoxy-2-(4-methoxyphenyl)-4H-1-benzopyran-4-one
-
3-phosphoglycerate
Campylobacter jejuni serotype O:2
slight inhibition
3-[3-[(3-chlorobenzene-1-sulfonyl)amino]-3-oxopropyl]-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
-
3-[3-[(benzenesulfonyl)amino]-3-oxopropyl]-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
-
3-[3-[(cyclopropanesulfonyl)amino]-3-oxopropyl]-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
-
3-[3-[(ethanesulfonyl)amino]-3-oxopropyl]-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
-
4-(2-(2-hydroxyphenylamino)thiazol-4-yl)benzene-1,3-diol
-
4-(2-(3-hydroxyphenylamino)thiazol-4-yl)benzene-1,3-diol
-
4-(2-(3-nitrophenylamino)thiazol-4-yl)phenol
-
4-(2-(4-hydroxyphenylamino)thiazol-4-yl)benzene-1,3-diol
-
4-(2-(4-nitrophenylamino)thiazol-4-yl)phenol
-
4-(2-(phenylamino)thiazol-4-yl)benzene-1,3-diol
-
4-(4-(2,4-dihydroxyphenyl)thiazol-2-ylamino)benzenesulfonamide
-
4-(4-(4-hydroxyphenyl)thiazol-2-ylamino)benzenesulfonamide
-
4-(4-(4-hydroxyphenyl)thiazol-2-ylamino)phenol
-
4-(4-phenylthiazol-2-ylamino)benzenesulfonamide
-
4-(4-phenylthiazol-2-ylamino)phenol
-
4-anilino-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
4-anilinoquinazoline
-
low molecular weight inhibitors of enzyme that are not substrate mimics or AMP analogues
4-chloromercuribenzoate
-
-
4-tert-butyl-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
4-[[(2R,4S)-4-(3-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2R,4S)-4-(3-methoxyphenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2R,4S)-4-(4-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2S,4S)-4-(3-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2S,4S)-4-(3-methoxyphenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
4-[[(2S,4S)-4-(4-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
5,6,7-trimethoxy-2-phenyl-4H-1-benzopyran-4-one
-
5,6-dihydroxy-7-methoxy-2-phenyl-4H-1-benzopyran-4-one
-
5,7-dihydroxy-2-(3-hydroxyphenyl)-4H-1-benzopyran-4-one
-
5-(1H-tetrazol-5-yl)-N-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenyl)pentanamide
-
-
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide
5-anilino-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
5-bromo-3-(2-carboxyethyl)-7-chloro-1H-indole-2-carboxylic acid
36.4% inhibition at 0.01 mM
5-bromo-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
-
5-chloro-2-(N-(2,5-dichlorobenzenesulfonamido))-benzoxazole
-
-
5-ethyl-7-nitro-3-[3-oxo-3-[(propane-2-sulfonyl)amino]propyl]-1H-indole-2-carboxylic acid
-
5-ethyl-7-nitro-3-[3-oxo-3-[(thiophene-2-sulfonyl)amino]propyl]-1H-indole-2-carboxylic acid
-
5-hydroxy-2-(3-hydroxyphenyl)-4H-1-benzopyran-4-one
-
5-hydroxy-2-(4-hydroxyphenyl)-4H-1-benzopyran-4-one
-
5-hydroxy-2-phenyl-4H-1-benzopyran-4-one
-
5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
-
6,7-diethoxy-N-[3-(2-methyl-1,3-thiazol-4-yl)phenyl]quinazolin-4-amine
-
-
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-2-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-3-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-4-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6,7-dimethyl-4-[[(2R,4S)-4-(2-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6,7-dimethyl-4-[[(2R,4S)-4-(6-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
-
-
6-chloro-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-1-benzopyran-4-one
-
6-hydroxy-N-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenyl)hexanamide
-
-
6-oxo-6-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenylamino)hexanoic acid
-
-
7-amino-3-(2-carboxyethyl)-1H-indole-2-carboxylic acid
-
7-bromo-3-(2-carboxyethyl)-5-ethyl-1H-indole-2-carboxylic acid
44.4% inhibition at 0.01 mM
7-hydroxy-2-(3-hydroxyphenyl)-4H-1-benzopyran-4-one
-
7-hydroxy-2-(4-hydroxyphenyl)-3-methyl-4H-1-benzopyran-4-one
-
7-hydroxy-2-(4-hydroxyphenyl)-4H-1-benzopyran-4-one
-
7-hydroxy-2-phenyl-4H-1-benzopyran-4-one
-
7-hydroxy-3-methyl-2-(3-methylphenyl)-4H-1-benzopyran-4-one
-
8-chloro-2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-1-benzopyran-4-one
-
aminoimidazole carboxamide ribotide
-
inhibition of fructose-1,6-bisphosphatase by aminoimidazole carboxamide ribotide prevents growth of Salmonella enterica purH mutants on glycerol
ammonium sulfate
-
10 mM, 127% of initial activity, 50 mM, no residual activity
D-fructose 1,6-bisphosphate
D-fructose 2,6-bisphosphate
D-fructose 6-phosphate
-
mixed-type. AMP, D-fructose 6-phosphate, D-fructose 1,6-bisphosphate interact in a synergistic way to inhibit the enzyme activity
D-fructose-1-phosphate
-
-
D-fructose-2,6-bisphosphate
dehydroascorbate
-
deactivates the enzyme activated by reduced thioredoxin f
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
diethyl [5-(4-amino-1-benzyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
diethyl [5-(4-amino-1-ethyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
diethyl [5-(4-amino-1-methyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
diethyl [5-(4-amino-1-propyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
diphenyl [5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonate
-
non-competitive
ethyl (2S,6S)-4-[5-(2-amino-5-isobutyl-1,3-thiazol-4-yl)-2-furyl]-2,6-dimethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide
i.e. CS917
-
ethyl (2S,6S)-4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-2,6-dimethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide
-
-
ethyl (2S,6S)-4-[[(6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazol-4-yl)oxy]methyl]-2,6-dimethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide
-
-
ethyl 2-[((5-[2-amino-5-(2,2-dimethylpropanoyl)-1,3-thiazol-4-yl]furan-2-yl)[(1-ethoxy-2-methyl-1-oxopropan-2-yl)amino]phosphoryl)amino]-2-methylpropanoate
MB07803
ethyl 3,3,3-trifluoro-2-hydroxy-2-(1-methyl-1H-indol-3-yl)propanoate
-
-
ethyl 3-(3,5-dimethyl-1H-pyrrol-2-yl)-4,4,4-trifluoro-3-hydroxybutanoate
-
-
ethyl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-2,2,6,6-tetramethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide (non-preferred name)
-
-
ethyl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-2,6-dimethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide (non-preferred name)
-
-
ethyl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide (non-preferred name)
-
-
fructose 2,6-bisphosphate
fructose 6-phosphate
-
product inhibitor
fructose-1,6-bisphosphate
at higher concentrations
fructose-2,6-bisphosphate
gossypetinidin chloride
-
herbacetin
most potent flavonoid inhibitor, herbacetin binding is stabilized by a strong interaction with the Glu30 side chain and the Thr24 backbone of FBPase
Hg2+
-
0.1 mM, no residual activity
L-alanine, N,N'-[[5-[2-amino-5-(2-methylpropyl)-4-thiazolyl]-2-furanyl] phosphinylidene]bis-, diethyl ester
-
effect of gluconeogenesis inhibition on postprandial hyperglycemia is investigated using the inhibitor CS-917 in meal-loaded diabetic Goto-Kakizaki rats. CS-917 suppresses plasma glucose elevation after meal loading in a dose-dependent manner at doses ranging from 10 to 40 mg/kg. In an overnight-fasted state, CS-917 decreases the plasma glucose levels dose-dependently at doses ranging from 2.5 to 40 mg/kg. Glucose-lowering is associated with an accumulation of hepatic D-fructose 1,6-bisphosphate and a reduction in hepatic D-fructose 6-phosphate. Chronic treatment of CS-917 decreases plasma glucose significantly, and no significant increase in plasma lactate and no profound elevation in plasma triglycerides are observed by both acute and chronic treatment of CS-917 in Goto-Kakizaki rats
N'-[(E)-(6-ethyl-4-oxo-4H-chromen-3-yl)methylidene]-3,4-dihydroxybenzohydrazide
compound potently inhibits both fructose-1,6-bisphoshate aldolase and fructose-1,6-bisphosphatase with IC50 values below 30 microM
N'-[(E)-(6-tert-butyl-4-oxo-4H-chromen-3-yl)methylidene]-3,4-dihydroxybenzohydrazide
compound potently inhibits both fructose-1,6-bisphoshate aldolase and fructose-1,6-bisphosphatase with IC50 values below 30 microM
N,4-diphenylthiazol-2-amine
-
N,N'-bis(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)pentane-1,5-diamine
-
uncompetitive
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)butan-1,4-diamine
-
0.03 mM, 20% inhibition
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)hexan-1,6-diamine
-
-
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)pentan-1,5-diamine
-
-
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)propan-1,3-diamine
-
-
N-(5-bromo-1,3-benzoxazol-2-yl)-2,5-dichlorobenzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-1-methyl-1H-imidazole-4-sulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-2-(1H-imidazol-1-yl)benzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-2-cyanobenzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-3-nitrobenzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-4-(3-furyl)benzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-4-(trifluoromethoxy)benzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-4-fluorobenzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)-4-methylbenzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)anthracene-2-sulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)biphenyl-2-sulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)biphenyl-3-sulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)biphenyl-4-sulfonamide
-
-
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfamide
-
excellent bioavailability and a good pharmacokinetic profile in rats
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfonamide
N-(5-chloro-1,3-benzoxazol-2-yl)thiophene-2-sulfonamide
-
-
N-(5-tert-butyl-1,3-benzoxazol-2-yl)-2,5-dichlorobenzenesulfonamide
-
-
N-(6,7-diethoxy-9-[3-(2-methylthiazol-4-yl)phenylamino]-2,3-dihydro-1H-cyclopenta[b]quinolin-1-yl)-acetamide
-
-
N-(6,7-diethoxy-9-[3-(2-methylthiazol-4-yl)phenylamino]-2,3-dihydro-1H-cyclopenta[b]quinolin-2-yl)acetamide
-
-
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-chlorobenzenesulfonamide
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[(6-bromo-1H-indol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[4-[[(5-chloro-1,3-benzoxazol-2-yl)amino]sulfonyl]phenyl]butanamide
-
-
N-[6-(4-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
-
non-competitive
N-[7-(3-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
-
-
N-[7-(4-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
-
-
N-[7-[3-(aminomethyl)phenyl]-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
-
-
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
N4-(3-Bromo-phenyl)-7-chloro-quinazoline-4,6-diamine
-
IC50: 0.0119 mM
NaCl
-
in vivo: The presence of 100 mM NaCl in the growth medium only marginally alters the cytosolic and chloroplastic enzyme activities of salt-tolerant varieties whereas both the activities decline appreciably in salt-sensitive varieties tested. in vitro: comparison of inhibition of chloroplastic enzyme in a salt-sensitive and a salt-tolerant enzyme, protection against inhibition in salt-sensitve rice by mannitol, inositol, pinitol, sorbitol, trehalose, sucrose and proline
NADH
-
20% inhibition of isoenzyme A, 83% inhibition of isoenzyme B
nagarse
-
stimulates 2fold to 3fold at pH 9.0, loss of activity at pH 6.5
-
NEM
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
oxidized glutathione
-
deactivates the enzyme activated by reduced thioredoxin f
p-mercuribenzoate
-
up to 90% inhibition at pH 6.5-7.0, slight increase at pH 9.0 when Mg2+ is the metal cofactor. 3fold increase of activity at alkaline pH, less activation at neutral pH when Mn2+ is the metal cofactor
papain
-
stimulates 2fold to 3fold at pH 9.0, loss of activity at pH 6.5
-
Pronase
-
stimulates 2fold to 3fold at pH 9.0, loss of activity at pH 6.5
-
propan-2-yl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-9-methyl-7-oxo-3,5,8-trioxa-4-phosphadecan-1-oate 4-oxide
-
-
pseudo-tetrapeptide OC252
-
the inhibition is synergistic with both AMP and fructose 2,6-bisphosphate, noncompetitive with respect to Mg2+ and, uncompetitive with respect to fructose 1,6-bisphosphate
Ribulose 1,5-diphosphate
-
1 mM, 48% inhibition of isoenzyme A, 3% inhibition of isoenzyme B
S-nitrosoglutathione
GSNO, the chloroplast FBPase isoform cFBP1 is efficiently S-nitrosylated in vitro. GSNO inhibits the FBPase activity in the mutant C173S/C178S but not in mutant C153S. 0.02 mM GSNO produces a 75% activity inhibition in the mutant C173S/C178S, compared with the nontreated protein, S-nitrosylation of FBPase mutants in the Cys of the redox regulatory domain
sedoheptulose 1,7-diphosphate
-
competitive inhibition of activity with fructose 1,6-diphosphate
tert-butyl 4-[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]-9,9-dimethyl-7-oxo-3,5,8-trioxa-4-phosphadecan-1-oate 4-oxide
-
-
TNP-AMP
-
a fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP), is used as a fluorescent probe as it is able to competitively inhibit AMP binding to the AMP allosteric site. AMP and fructose 1,6-bisphosphate both can reduce the fluorescence from the bound TNP-AMP through competition for FBPase, suggesting that TNP-AMP binds not only to the AMP allosteric site but also to the FBP active site. The residue K274 is very important for TNP-AMP to bind to the active site of FBPase. When the residue K274 is mutated to L274, TNP-AMP cannot bind to the active site, but can bind to the allosteric site
[(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)(difluoro)methyl]phosphonic acid
-
[(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)methyl]phosphonic acid
-
[(2R,3S,4R,5R)-5-[4-(aminocarbonyl)-1H-imidazol-1-yl]-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen phosphate
-
-
[2-[(6-amino-8,9-dihydro-7H-purin-8-yl)amino]ethyl]phosphonate
-
[2-[[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]amino]ethyl]phosphonate
-
[3-[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]propyl]phosphonate
-
[5-(1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(2-amino-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
[5-(2-amino-5-isobutyl-1,3-oxazol-4-yl)-2-furyl]phosphonic acid
[5-(2-amino-5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
non-competitive
[5-(2-amino-5-isobutyl-1H-imidazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)furan-2-yl]phosphonic acid
-
-
[5-(2-amino-5-propyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(2-amino-5-propyl-1,3-thiazol-4-yl)thiophen-2-yl]phosphonic acid
-
-
[5-(4-amino-1-tert-butyl-2,3-dihydro-1H-benzimidazol-2-yl)-2-furyl]phosphonate
-
[5-(4-amino-1-tert-butyl-7-ethyl-5-fluoro-2,3-dihydro-1H-benzimidazol-2-yl)-2-furyl]phosphonate
-
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid
[5-(5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
[5-(6-amino-3-phenylpyridin-2-yl)-2-furyl]phosphonic acid
[5-(6-amino-9-tert-butyl-8,9-dihydro-7H-purin-8-yl)-2-furyl]phosphonate
-
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
[5-[2-amino-5-(ethoxycarbonyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
-
-
[5-[2-amino-5-(propylsulfanyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-bromo-6,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
[5-[5-(2-methylpropyl)-2-phenyl-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
-
-
[5-[6-amino-9-(2,2-dimethylpropyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
-
[5-[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
-
[5-[6-amino-9-(2-phenylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one

-
-
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
-
-
(4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol

i.e. PFE, allosteric inhibitor
(4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol
i.e. PFE, allosteric inhibitor, residue L56 coordinates the (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol (PFE) inhibitor ligand, as does residue L73, both of which exhibit hydrophobic interactions with the ligand in the PFE-binding site. In addition, L73 and L56 are part of a network that leads from the allosteric binding site to the active site of the enzyme. This hydrophobic network, also involving residues V48 and L120 may stabilize previously described hydrogen bonding networks including residues R49, S169, and D127, shown in the network, leading to the active site where the metal binds D121, D118, and E280. The M177 and Y164 interfacial residues are positioned between the AMP-binding site and active sites
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid

-
-
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid
-
-
2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate

wild-type muscle enzyme, 50% inhibition at 0.00022 mM, wild-type liver enzyme, 50% inhibition at 0.0046 mM
2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate
-
able to bind not only to the AMP allosteric site but also to the fructose-1,6-bisphosphate active site
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide

-
50% inhibition at 0.0034 mM
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
-
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
-
non-competitive
2-amino-4-[2-(5-phosphono)furanyl]-5-ethoxycarbonylthiazole

-
potent FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-ethoxycarbonylthiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-amino-4-[2-(5-phosphono)furanyl]-5-isobutylthiazole

-
potent FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-isobutylthiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-amino-4-[2-(5-phosphono)furanyl]-5-phenylthiazole

-
potent FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-phenylthiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-amino-4-[2-(5-phosphono)furanyl]-5-propylsulfanylthiazole

-
potent FBPase inhibitor
2-amino-4-[2-(5-phosphono)furanyl]-5-propylsulfanylthiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole

-
poor oral bioavailability
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
-
poor oral bioavailability
2-amino-5-methylsulfanyl-4-[2-(5-diethylphosphono)furanyl]thiazole

-
potent FBPase inhibitor
2-amino-5-methylsulfanyl-4-[2-(5-diethylphosphono)furanyl]thiazole
-
potent FBPase inhibitor: when administerd intravenously it lowers plasma glucose levels in 18 h fasted normal Sprague-Dawley rats above 50% at doses below 10 mg/kg
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate

-
-
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate
-
-
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate

-
-
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate
-
-
3-(2-carboxyethyl)-4,6-dichloro-1H-indole-2-carboxylic acid

-
non-competitive
3-(2-carboxyethyl)-4,6-dichloro-1H-indole-2-carboxylic acid
MDL-29951
3-chloro-N-[(3,5-dichlorophenyl)carbamoyl]benzenesulfonamide

-
-
3-chloro-N-[(3,5-dichlorophenyl)carbamoyl]benzenesulfonamide
-
-
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide

-
-
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide

-
-
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide

-
-
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide

-
-
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
-
-
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide

-
-
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide
-
-
ADP

33% inhibition; 38% inhibition
ADP
1.5 mM, 30% decrease in activity; 30% inhibition at 1.5 mM
AMP

-
-
AMP
inhibitory below 0.2 mM
AMP
-
50% inhibition at 0.015 mM
AMP
-
transformation of enzyme to inactive T-state, inhibition shows quarternary transition and cooperativity
AMP
FBPase undergoes a quaternary transition from the canonical R-state to a T-like state in response to AMP. Glc-6-P and AMP are synergistic inhibitors
AMP
AMP and D-fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase
AMP
-
at pH 7.4, 0.0004 mM, complete inhibition
AMP
-
susceptibility of enzyme decreases in complex with aldolase
AMP
50% inhibition at 0.00016 mM
AMP
-
no significant inhibition
AMP
lung enzyme is significantly less inhibited than the muscle enzyme
AMP
-
muscle enzyme is more strongly inhibited than the liver isoenzyme
AMP
wild-type muscle enzyme, 50% inhibition at 0.0001 mM, Hill coefficient 1.78, wild-type liver enzyme, 50% inhibition at 0.0044 mM, Hill coefficient 2.08
AMP
-
113Tyr and 31Thr play an mportant role, each via two hydrogen bonds affecting the binding affinity of inhibitor AMP to FBPase
AMP
inactive, AMP-associated T state of the enzyme, AMP binding results in improved thermal stability of muscle FBPase
AMP
-
allosteric inhibition. The fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP), is used as a fluorescent probe as it is able to competitively inhibit AMP binding to the AMP allosteric site
AMP
has a negative regulator role
AMP
negative allosteric regulation by AMP. This allosteric regulation requires information transmission between the AMP binding site and the active site of the enzyme. Two residues in the AMP binding site (Lys112 and Tyr113) are involved in initiating the message between the two sites. Binding structure analysis
AMP
non-competitive inhibition
AMP
AMP binds to an effector site about 30 A distant from the active site and acts as an allosteric inhibitor, the crystal structure of LmFBPase complexed with its allosteric inhibitor AMP shows an inactive form of the tetramer, in which the dimer pairs are rotated by 18° relative to each other, revealing an allosteric mechanism in which AMP binding triggers a rearrangement of hydrogen bonds across the large and small interfaces. Retraction of the effector loop required for AMP binding releases the side chain of His23 from the dimer-dimer interface. This is coupled with a flip of the side chain of Arg48 which ties down the key catalytic dynamic loop in a disengaged conformation and also locks the tetramer in an inactive rotated T-state. AMP inhibits the catalytic activity of LmFBPase without eliminating the substrate binding; allosteric inhibitor. AMP binding triggers a rearrangement of hydrogen bonds across the large and small interfaces. Retraction of the effector loop required for AMP binding releases the side chain of His23 from the dimer-dimer interface. This is coupled with a flip of the side chain of Arg48 which ties down the key catalytic dynamic loop in a disengaged conformation and also locks the tetramer in an inactive rotated T-state
AMP
-
non-competitive. AMP, D-fructose 6-phosphate, D-fructose 1,6-bisphosphate interact in a synergistic way to inhibit the enzyme activity
AMP
-
binding of AMP, and presumably NAD+, stabilizes an inactive, T-state of FBPase
AMP
-
sensitivity decreases greatly with increasing pH or temperature. Inhibition of Zn2+ and AMP is synergistic
AMP
-
sensitivity to AMP is decreased with increase in pH, temperature and Mg2+ concentration
AMP
-
0.073 mM, 50% inhibition
AMP
-
non-competitive inhibition of cytosolic enzyme, the chloroplastic enzyme is AMP-insensitive
AMP
-
non-competitive inhibition of cytosolic enzyme, the chloroplatic enzyme is AMP-insensitive
AMP
-
acts synergistically with fructose-2,6-bisphosphate on the frog muscle FBPase
AMP
-
the AMP binding is mainly located in the N-terminal region
AMP
-
muscle enzyme: 50% inhibition at 0.00054 mM, liver enzyme: 50% inhibition at 0.085 mM
AMP
-
0.1 mM, 9% inhibition of isoenzyme A, complete inhibition of isoenzyme B
AMP
-
mixed linear inhibitor
AMP
-
the phosphoenzyme is about 3fold more sensitive than the dephosphoenzyme
AMP
-
inhibits cytoplasmic enzyme, no inhibition of chloroplastic enzyme
AMP
-
no inhibition of the enzyme from chloroplast
AMP
-
structural aspects of the allosteric inhibition
AMP
-
uptake of 1 M of NEM per mol of subunit is accompanied by a loss of sensitivity towards AMP. K+ induces a conformational change on the enzyme derivative which hinders AMP interaction with the protein
AMP
-
comparison of inhibition of homotetramer and hybrid tetramers
AMP
-
study of allosteric inhibition, two classes of binding sites with two distinct affinities for AMP are possible
AMP
wild-type, 50% inhibition at 0.0016 mM, mutant E97A, 50% inhibition at 0.0038 mM, mutant D118A, 50% inhibition at 0.0069 mM, mutant D121A, 50% inhibition at 0.0074 mM
AMP
-
isoenzyme F-I is inhibited, isoenzyme F-II is not inhibited
AMP
a regulatory inhibitor, AMP-binding loop structure analysis
AMP
-
the cFBPase functional site residues of AMP binding are Arg30, Asp32, and Phe33. Asp32 plays a key role in maintaining the AMP binding conformation. Residues of the binding site are Leu20, Gln23, Arg30, Asp32, Phe33, Thr34, Lys115, and Tyr116 forming a pocket surface structure. Docking analysis of enzyme mutant R30T/D32E/F33L shows that the replaced Thr30 forms a hydrogen bond with AMP
ATP

50% inhibition; 56% inhibition
ATP
1 mM, reduces activity by 40%
ATP
-
activates the microsomal and mitochondrial enzyme, inhibits the cytosoli enzyme
ATP
1.5 mM, 90% decrease in activity; 90% inhibition at 1.5 mM
Ca2+

-
Ca2+
-
inhibition is potentiated by Li+
Ca2+
-
wild type and mutant enzyme
Ca2+
unique divalent metal ion inhibitor
Ca2+
-
Ca2+ affects conformation of the catalytic loop 52-72 of muscle FBPase and inhibits its activity by competing with activatory divalent cations, e.g. Mg2+ and Zn2+. Aldolase associates with FBPase in its active form, i.e. with loop 52-72 in the engaged conformation, while Ca2+ stabilizes the disengaged-like form of the loop
Ca2+
similar inhibition constant as Mn2+
Ca2+
-
0.05 mM, 41% residual activity
Ca2+
-
slight inhibition of isozyme FBP1. Presence of glutamic acid at position 69 ensures strong binding of Ca2+ to the muscle FBPase, which in turn disrupts the proper interaction of catalytic divalent cations (e.g. Mg2+) with the substrate in the catalytic site. Ectothermal vertebrates FBP2 is significantly less sensitive to Ca2+ than warm-blooded animals being still more sensitive to the cation than FBP1; strong inhibition
Ca2+
-
50% inhibition at 59 nM, muscle enzyme. At elevated Ca2+ concentration, enzyme dissociates from Z-line
Ca2+
-
Glu 69 is essential for the high sensitivity of muscle fructose-1,6-bisphosphatase inhibition by calcium ions
Ca2+
-
competitive with respect to Mg2+
Ca2+
-
chloroplastic enzyme
Ca2+
-
at high concentration depending on the concentration of Mg2+
citrate

-
-
citrate
-
mixed type of inhibition with a change from a hyperbolic velocity curve in absence of citrate to a sigmoidal one in its presence
Cu2+

-
-
Cu2+
-
1 mM, no residual activity
D-fructose 1,6-bisphosphate

-
D-fructose 1,6-bisphosphate
substrate inhibition at high concentrations
D-fructose 1,6-bisphosphate
-
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
-
D-fructose 1,6-bisphosphate
-
competitive, changes substrate saturation curve from hyperbolic to sigmoidal. AMP, D-fructose 6-phosphate, D-fructose 1,6-bisphosphate interact in a synergistic way to inhibit the enzyme activity
D-fructose 1,6-bisphosphate
-
substrate inhibition at higher concentrations
D-fructose 2,6-bisphosphate

-
-
D-fructose 2,6-bisphosphate
AMP and fructose 2,6-bisphosphate are not synergistic inhibitors of the type I FBPase
D-fructose 2,6-bisphosphate
the Lys residue, which is known to be essential for inhibiting Fru 2,6-P2 in gluconeogenic FBPases, is also conserved in EgFBPaseIII at Lys408
D-fructose 2,6-bisphosphate
-
D-fructose 2,6-bisphosphate
a natural heterotropic inhibitor
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
-
D-fructose 2,6-bisphosphate
-
-
D-fructose 2,6-bisphosphate
-
D-fructose 2,6-bisphosphate
-
the binding of fructose 1,6-bisphosphate induces the appearance of catalytic sites with lower affinity for substrate and lower catalytic activity. The inhibitor, fructose 1,6-bisphosphate, competes with the substrate for the high-affinity sites. Binding of substrate to the low-affinity sites acts as a stapler that prevents dissociation of the tetramer and hence exchange of subunits, and results in substrate inhibition
D-fructose 2,6-bisphosphate
a natural heterotropic inhibitor
D-fructose-2,6-bisphosphate

-
-
D-fructose-2,6-bisphosphate
-
-
D-fructose-2,6-bisphosphate
competitive inhibition
D-fructose-2,6-bisphosphate
-
-
D-fructose-2,6-bisphosphate
-
acts synergistically with AMP on the frog muscle FBPase
D-fructose-2,6-bisphosphate
competitive inhibition
D-fructose-2,6-bisphosphate
kinetic mechanism
D-fructose-2,6-bisphosphate
-
two pathways of allosteric inhibition are possible
D-fructose-2,6-bisphosphate
-
-
D-fructose-2,6-bisphosphate
-
D-glucose 6-phosphate

allosteric inhibition. FBPase undergoes a quaternary transition from the canonical R-state to a T-like state in response to glucose 6-phosphate. Glc-6-P and AMP are synergistic inhibitors
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate

-
-
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate

-
-
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate

-
-
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate

-
-
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
-
-
diethyl [5-(4-amino-1-benzyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate

-
-
diethyl [5-(4-amino-1-benzyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
-
-
diethyl [5-(4-amino-1-ethyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate

-
-
diethyl [5-(4-amino-1-ethyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
-
-
diethyl [5-(4-amino-1-methyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate

-
-
diethyl [5-(4-amino-1-methyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
-
-
diethyl [5-(4-amino-1-propyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate

-
-
diethyl [5-(4-amino-1-propyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

-
-
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

-
-
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

-
-
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

-
-
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

-
-
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

-
-
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

-
-
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

-
-
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

-
-
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
-
-
EDTA

at an equimolar concentration to the bivalent metal ions, almost complete loss of activity; at an equimolar concentration to the bivalent metal ions, almost complete loss of activity
EDTA
5 mM, complete inhibition of phosphatase activity; complete inhibition of phosphatase activity by 5 mM EDTA
EDTA
-
0.1 mM, complete inhibition
fructose 1,6-diphosphate

-
at high concentrations
fructose 1,6-diphosphate
-
above 0.1 mM
fructose 1,6-diphosphate
-
substrate inhibition above 0.05 M
fructose 1,6-diphosphate
-
-
fructose 1,6-diphosphate
-
above 0.015 mM
fructose 1,6-diphosphate
-
concentration required for 50% inhibition is 0.045 mM for the muscle enzyme, 0.060 mM for the intestinal enzyme and 0.065 mM for the liver enzyme
fructose 1,6-diphosphate
-
at high concentrations
fructose 1,6-diphosphate
-
the substrate is unable to bind to the free enzyme as an inhibitor
fructose 1,6-diphosphate
-
no inhibition up to 1 mM
fructose 1,6-diphosphate
-
above 4 mM
fructose 1,6-diphosphate
-
0.4 mM, 58% loss of maximal activity
fructose 1,6-diphosphate
-
at high concentrations
fructose 2,6-bisphosphate

competitive inhibition. Fructose-2,6-bisphosphate binding reduces the concentration of AMP required for a given level of inhibition. It also induces positive co-operativity in the kinetics of the forward reaction, converting a hyperbolic (Michaelis-Menten) relationship between substrate concentration and rate into a sigmoidal one
fructose 2,6-bisphosphate
competitive inhibitor
fructose 2,6-bisphosphate
-
-
fructose 2,6-bisphosphate
global conformational change in porcine FBPase induced by fructose 2,6-bisphosphate in the absence of AMP
fructose 2,6-bisphosphate
-
-
fructose 2,6-diphosphate

-
competitive
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
lung enzyme is slightly more sensitive to inhibition than the liver enzyme. Synergistic effect of AMP and fructose 2,6-diphosphate on lung and liver enzyme
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
muscle enzyme: 50% inhibition at 0.0063 mM, liver enzyme: 50% inhibition at 0.0015 mM
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
the phosphoenzyme is about 3fold more sensitive than the dephosphoenzyme
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
-
fructose 2,6-diphosphate
-
-
fructose-2,6-bisphosphate

-
-
fructose-2,6-bisphosphate
fructose 2,6-bisphosphate binds at the active site, and shows a synergistic inhibitory effect with AMP
fructose-2,6-bisphosphate
-
fructose-2,6-bisphosphate
50% inhibition in the presence of 0.2 mM fructose-1,6-bisphosphate
H2O2

isozyme EgFBPaseI is inhibited by 1 mM H2O2 and recovers when incubated with DTT
H2O2
the activity of EgFBPaseIII is partially inhibited by the H2O2 treatment, but is not reactivated when incubated with DTT, indicating that EgFBPaseIII is nonspecifically oxidized at amino acid residues, but not specifically at Cys residues
K+

-
inhibitory in the cytosol, activating in mitochondria and microsomes, depedent on the presence of Mg2+ or Mn2+, overview
K+
-
at 5 mM Mg2+, increasing K+ up to 140 mM are progressively inhibitory for neutral and alkaline isoenzyme from liver, muscle neutral isoenzyme is activated, 10% at 5 mM Mg2+ but inhibited at 1 mM Mg2+
KCl

50 mM, residual activity 20%
KCl
-
in vitro: at higher concentration KCl inhibits the salt-sensitive rice, but the salt-tolerant rice remains unaffected
Li+

-
Li+
1 mM, 50% residual activity; 1 mM, 50% residual activity
Li+
50% inhibition at 1.1 mM
Li+
-
linear competitive inhibitor
MB06322

-
-
MB06322
-
oral administration of the prodrug, MB06322, to Zucker Diabetic Fatty rats leads to dose-dependent inhibition of gluconeogenesis and endogenous glucose production and consequently to significant blood glucose reduction
MB07803

-
-
MB07803
a prodrug of MB07729
-
Mg2+

inhibitory above 10 mM
Mg2+
-
complete inhibition at 1-50 mM. Mg2+ is inhibitory at any concentration regardless of KCl absence or presence
Mg2+
-
inhibits above the optimal concentration of 1-1.5 mM
Mg2+
-
inhibition at nonphysiological high concentrations
Mg2+
-
inhibitory at higher concentration on free enzyme. Not inhibitory for enzyme in complex with aldolase. Mg2+ at physiological concentration increases the affinity of enzyme to aldolase, at higher concentration decreases the concentration of the complex
Mn2+

thermostability of LmFBPase is increased by more than 9°C in the presence of Mn2+
Mn2+
-
inhibits above the optimal concentration of 0.05-0.07 mM
Mn2+
highly activating at up to 3 mM, inhibitory above
Mn2+
-
inhibition above 0.5 mM
Mn2+
-
inhibitory above 3 mM
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfonamide

-
-
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfonamide
-
non-competitive
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

-
-
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

-
-
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-chlorobenzenesulfonamide

-
-
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-chlorobenzenesulfonamide
-
-
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

-
-
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

-
-
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide

-
-
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
-
-
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

-
-
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[(6-bromo-1H-indol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide

-
-
N-[(6-bromo-1H-indol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
-
-
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

-
-
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

-
-
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

-
-
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide

-
-
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide
-
-
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

-
-
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
-
-
Na+

-
-
NAD+

-
-
NAD+
-
binding of AMP, and presumably NAD+, stabilizes an inactive, T-state of FBPase
NAD+
-
no inhibition of isoenzyme A, 67% inhibition of isoenzyme B
NaF

-
-
NH4+

-
-
NH4+
-
0.01-0.02 mM, slight activation of neutral and alkaline isoenzyme, progressive inhibition at increasing concentration
p-hydroxymercuribenzoate

-
strong
p-hydroxymercuribenzoate
-
-
phosphate

-
-
phosphate
-
product inhibitor
phosphoenolpyruvate

Campylobacter jejuni serotype O:2
weak inhibition, noncompetitive inhibition, the reaction's kcat is decreased while Km remains barely changed
UDP

-
-
Zn2+

-
-
Zn2+
-
0.001-0.010 mM has no significant effect, with 0.002-0.0035 mM Zn2+, in absence of EDTA, 50% inhibition, 80% inhibition by 0.01 mM Zn2+
Zn2+
-
pH 7.5, 0.0015 mM, 92% inhibition. Inhibition of Zn2+ and AMP is synergistic
Zn2+
-
strong inhibitor at low concentrations, activator at high concentrations
Zn2+
-
due to binding to a noncatalytic divalent metal binding site
Zn2+
-
inhibitory above 3 mM
Zn2+
-
the enzyme activity is completely inhibited at concentrations higher than 1 mM in presence of 10 mM Mg2+
[5-(2-amino-1,3-thiazol-4-yl)-2-furyl]phosphonic acid

-
-
[5-(2-amino-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(2-amino-5-isobutyl-1,3-oxazol-4-yl)-2-furyl]phosphonic acid

-
-
[5-(2-amino-5-isobutyl-1,3-oxazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid

-
-
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid

-
-
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid
-
-
[5-(5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid

-
-
[5-(5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
-
-
[5-(6-amino-3-phenylpyridin-2-yl)-2-furyl]phosphonic acid

-
-
[5-(6-amino-3-phenylpyridin-2-yl)-2-furyl]phosphonic acid
-
-
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid

-
-
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid
-
-
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid

-
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-bromo-6,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5-bromo-6,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-7-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

-
-
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
-
-
additional information

-
AMP, ADP or glucose have no effect on enzyme activity
-
additional information
I3DTM3
not inhibitory: AMP, phosphoenolpyruvate, D-fructose 1-phosphate, D-fructose 6-phosphate, and D-fructose 2,6-bisphosphate up to 5 mM; not inhibitory: AMP, phosphoenolpyruvate, D-fructose 1-phosphate, D-fructose 6-phosphate, and D-fructose 2,6-bisphosphate up to 5 mM
-
additional information
not inhibitory: AMP, phosphoenolpyruvate, D-fructose 1-phosphate, D-fructose 6-phosphate, and D-fructose 2,6-bisphosphate up to 5 mM; not inhibitory: AMP, phosphoenolpyruvate, D-fructose 1-phosphate, D-fructose 6-phosphate, and D-fructose 2,6-bisphosphate up to 5 mM
-
additional information
-
not inhibitory: AMP, phosphoenolpyruvate, D-fructose 1-phosphate, D-fructose 6-phosphate, and D-fructose 2,6-bisphosphate up to 5 mM; not inhibitory: AMP, phosphoenolpyruvate, D-fructose 1-phosphate, D-fructose 6-phosphate, and D-fructose 2,6-bisphosphate up to 5 mM
-
additional information
Campylobacter jejuni serotype O:2
Campylobacter jejuni FBPase is not inhibitred by AMP. The enzyme also shows limited sensitivity to other glycolytic and gluconeogenic intermediates. The allosteric cooperative control of the enzyme's activity found in type I FBPases appears to have been lost
-
additional information
-
AMP, ADP or glucose have no effect on enzyme activity
-
additional information
-
cytosolic Fru-1,6-P2ase is inhibited by the effects of 15 months of elevated CO2 concentration. 37.2% decrease of activity
-
additional information
not: AMP
-
additional information
-
not: AMP
-
additional information
activity of FBPase diminishes upon dilution into assay buffers. Relative activity falls to about 70% after 2 min and reaches a threshold of about 35% after 1 h
-
additional information
-
activity of FBPase diminishes upon dilution into assay buffers. Relative activity falls to about 70% after 2 min and reaches a threshold of about 35% after 1 h
-
additional information
isozyme EgFBPaseII is resistant to H2O2 up to concentrations of 1 mM; not inhibited by concentrations of AMP up to 1 mM; not inhibited by concentrations of AMP up to 1 mM
-
additional information
isozyme EgFBPaseII is resistant to H2O2 up to concentrations of 1 mM; not inhibited by concentrations of AMP up to 1 mM; not inhibited by concentrations of AMP up to 1 mM
-
additional information
-
isozyme EgFBPaseII is resistant to H2O2 up to concentrations of 1 mM; not inhibited by concentrations of AMP up to 1 mM; not inhibited by concentrations of AMP up to 1 mM
-
additional information
no inhibition but slight activation by AMP
-
additional information
-
no inhibition but slight activation by AMP
-
additional information
-
cytosolic Fru-1,6-P2ase is inhibited by the effects of 15 months of elevated CO2 concentration. 13.3% decrease of activity
-
additional information
-
cytosolic Fru-1,6-P2ase is inhibited by the effects of 15 months of elevated CO2 concentration. 56.7% decrease of activity
-
additional information
-
inhibitor design, synthesis and molecular modeling, overview
-
additional information
-
design, synthesis, and structure-activity relationship of a series of phosphonic acid containing benzimidazoles that function as fructose-1,6-bisphosphatase inhibitors and AMP mimics
-
additional information
-
synthesis and evaluation of a series of phosphonic acid-containing thiazoles as enzyme inhibitors, structure-guided drug design approach, optimization of both the thiazole FBPase inhibitors and their prodrugs, overview
-
additional information
mammalian muscle FBPase is about 100times more susceptible to the allosteric inhibitors AMP and NAD+ and about 1000times more sensitive to inhibition by Ca2+ than the liver isozyme
-
additional information
-
mammalian muscle FBPase is about 100times more susceptible to the allosteric inhibitors AMP and NAD+ and about 1000times more sensitive to inhibition by Ca2+ than the liver isozyme
-
additional information
the FBPase pig kidney tetramer overlay of human and pig kidney (PDB IDs 1FTA and 1KZ8, respectively) show nearly identical orientation and conformation in the active site, AMP allosteric binding site, and inhibitor (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol allosteric binding site architecture
-
additional information
-
the FBPase pig kidney tetramer overlay of human and pig kidney (PDB IDs 1FTA and 1KZ8, respectively) show nearly identical orientation and conformation in the active site, AMP allosteric binding site, and inhibitor (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol allosteric binding site architecture
-
additional information
-
a series of novel indole derivatives is designed and synthesized as inhibitors of fructose-1,6-bisphosphatase (FBPase), structure-activity relationships, molecular docking, overview. No inhibition by 3-(2-carboxyethyl)-4-nitro-1H-indole-2-carboxylic acid and 3-(2-carboxyethyl)-6-nitro-1H-indole-2-carboxylic acid
-
additional information
a series of novel indole derivatives is designed and synthesized as inhibitors of fructose-1,6-bisphosphatase (FBPase), structure-activity relationships, molecular docking, overview. No inhibition by 3-(2-carboxyethyl)-4-nitro-1H-indole-2-carboxylic acid and 3-(2-carboxyethyl)-6-nitro-1H-indole-2-carboxylic acid
-
additional information
-
the FBP active site works by stabilizing the FBPase, and the allosteric site impairs the activity of FBPase through its binding of a nonsubstrate molecule. Competitive inhibition of AMP, fructose 1,6-bisphosphate, or fructose 6-phosphate binding to FBPase with fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP)-binding FBPase
-
additional information
indole derivatives as fructose-1,6-bisphosphatase inhibitors, structures analysis, structure-activity relationships of indole-2-carboxylic acid derivatives, overview. FBPase inhibitors bearing N-acylsulfonamide moiety on the 3-position of the indole-2-carboxylic acid scaffold are identified with IC50s at the submicromolar levels. Each subunit of the homotetrameric enzyme binds one inhibitor in the AMP allosteric site and one fructose-1,6-bisphosphate in the substrate site. No inhibition by 7-acetamido-3-(2-carboxyethyl)-5-ethyl-1H-indole-2-carboxylic acid. The indole scaffold is situated in the purine pocket and interacts with Glu20, Ala24, and Leu30 via hydrophobic interactions. The 2-COOH constructs the extensive hydrogen bond interactions with Thr27, Gly28, and Thr31 via partly mimicking the phosphate group of AMP and contributes significantly to the binding affinity. The indole NH forms an H-bond with the side chain OH group of Thr31, and this H-bond is critical as well, as the corresponding benzofuran analogue lost activity completely. In addition, the 7-NO2 is able to form a hydrogen bond with Thr31, while the 7-Cl is trapped in a hydrophobic cavity lined with Val17, Leu30, Leu34, and Met177. Detailed noncovalent interactions of receptor-ligand and binding pose comparison
-
additional information
the reaction catalyzed by fructose 1,6-bisphosphatase (FBPase) occurs in the cytoplasm, with its intracellular activity regulated by the competitive inhibitor fructose 2,6-bisphoshate and the allosteric inhibitor AMP. Molecular determinants of flavonoid binding to human liver FBPase isozyme, structural specificity of flavonoids in the inhibition of human fructose 1,6-bisphosphatase, overview
-
additional information
-
AMP, ADP or glucose have no effect on enzyme activity
-
additional information
-
rapid regulation of frucose-1,6-diphosphatase following glucose addition is controlled mainly by enzyme inhibitors
-
additional information
cFBP1 is quite sensitive to higher oxidant concentrations
-
additional information
-
FBPase is suppressed, and gluconeogenesis is inhibited during freezing
-
additional information
-
fluoroquinolones inhibit fructose 1,6-bisphosphatase leading to suppression of hepatic gluconeogenesis (the cells are exposed to fluoroquinolones at 1 mM with either 10 mM phosphoenolpyruvate and fructose-1,6-bisphosphate, or 10 mM fructose-6-phosphate in the presence or absence of 10 mM sodium lactate and 1 mM sodium pyruvate). Gene expression levels of rate-limiting enzymes involved in hepatic gluconeogenesis are measured. In the glucose production assay and gene expression analysis, moxifloxacin and gatifloxacin show similar inhibitory effects, but moxifloxacin shows apparent effects with less variation, metabolome analysis, overview. Moxifloxacin and gatifloxacin at a concentration of 1 mM do not suppress the upregulated phosphoenolpyruvate carboxykinase 1 and glucose 6-phosphatase with gluconeogenic substrates. Instead, they upregulate or tend to upregulate these genes. In addition, fluoroquinolone does not affect the expression of other gluconeogenic genes including mitochondrial isoform phosphoenolpyruvate carboxykinase 2, fructose 1,6-bisphosphatase, and glycolytic genes like pyruvate dehydrogenase 2 or pyruvate kinase. Involvement of fructose 1,6-bisphosphatase in gluconeogenesis suppression by moxifloxacin and gatifloxacin in monkey hepatocytes, overview
-
additional information
-
sorbitol increases the susceptibility of the enzyme to inhibition by high concentrations of D-fructose 1,6-bisphosphate
-
additional information
-
while the inactive T-states of FBP1 and FBP2 are similar, the active R-state of FBP2 adopts the cruciform structure while in the liver enzyme FBP1, the R-state is planar. Distinct sensitivity of the two isozymes towards effectors; while the inactive T-states of FBP1 and FBP2 are similar, the active R-state of FBP2 adopts the cruciform structure, while in the liver enzyme FBP1, the R-state is planar. Distinct sensitivity of the two isozymes towards effectors
-
additional information
-
not inhibited by AMP
-
additional information
-
inhibitor design, synthesis and molecular modeling, overview
-
additional information
phosphoenolpyruvate, AMP, ADP, citrate, not inhibitory up to 1 mM
-
additional information
-
phosphoenolpyruvate, AMP, ADP, citrate, not inhibitory up to 1 mM
-
additional information
no inhibition by isocitrate
-
additional information
no inhibition by isocitrate
-
additional information
-
no inhibition by isocitrate
-
additional information
enzyme mutant T84S can be used to trap reaction intermediates, through crystallographic methods, facilitating the design of potent inhibitors via structure-based drug design
-
additional information
-
2,3-dihydro-1H-cyclopenta[b]quinoline moiety may represent a suitable scaffold for the synthesis of potent F16BPase inhibitors endowed with significantly lower epidermal growth factor receptor tyrosine kinase inhibitory activity
-
additional information
-
not: NaCl, KCl, NH4Cl
-
additional information
-
not: NH4CL
-
additional information
no inhibition by AMP; no significant effect of AMP on the phosphatase activity
-
additional information
Na+, K+, phosphoenolpyruvate
-
additional information
-
Na+, K+, phosphoenolpyruvate
-
additional information
-
not: AMP
-
additional information
-
design, synthesis, and structure-activity relationship of a series of phosphonic acid containing benzimidazoles that function as fructose-1,6-bisphosphatase inhibitors and AMP mimics
-
additional information
-
rapid inactivation in vivo by addition of glucose is caused by phosphorylation of the enzyme
-
additional information
-
cytosolic Fru-1,6-P2ase is inhibited by the effects of 15 months of elevated CO2 concentration. 30.8% decrease of activity
-
additional information
-
repression of chloroplastic enzyme in tomato fruits, using of antisence technique, does not influence metabolite levels as greatly as it does in leaves, probably because any alterations are buffered by the ability of the fruit to import sugars
-
additional information
the FBPase pig kidney tetramer overlay of human and pig kidney (PDB IDs 1FTA and 1KZ8, respectively) show nearly identical orientation and conformation in the active site, AMP allosteric binding site, and inhibitor (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol allosteric binding site architecture
-
additional information
not: AMP
-
additional information
-
not: AMP
-
additional information
-
no inhibition by AMP
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.0026 - 0.17
beta-D-glucose 1,6-bisphosphate
0.0001 - 3.2
D-fructose 1,6-bisphosphate
0.0111 - 99.98
D-fructose 1,6-diphosphate
1
D-Fructose 1-phosphate
pH 7.7
0.0018 - 0.035
D-fructose-1,6-bisphosphate
0.1 - 0.45
fructose 1,6-bisphosphate
0.00054 - 0.057
fructose 1,6-diphosphate
0.0031 - 0.021
Ribulose 1,5-diphosphate
0.016
sedoheptulose 1,6-diphosphate
-
-
0.0026 - 1.4
sedoheptulose 1,7-diphosphate
0.118
sedoheptulose-1,7-diphosphate
-
-
additional information
additional information
-
0.0026
beta-D-glucose 1,6-bisphosphate

-
wild type enzyme, in 50 mM K+HEPES pH 7.0 at 25°C
0.0048
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme T16P, in 50 mM K+HEPES pH 7.0 at 25°C
0.031
beta-D-glucose 1,6-bisphosphate
-
wild type enzyme, in 50 mM K+HEPES pH 7.0 at 25°C
0.041
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme H20A, in 50 mM K+HEPES pH 7.0 at 25°C
0.045
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme H20Q, in 50 mM K+HEPES pH 7.0 at 25°C
0.066
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme K76A, in 50 mM K+HEPES pH 7.0 at 25°C
0.17
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme H20N, in 50 mM K+HEPES pH 7.0 at 25°C
0.0001
D-fructose 1,6-bisphosphate

-
pH 7.5, 30°C, wild-type enzyme
0.00011
D-fructose 1,6-bisphosphate
-
pH 7.5, 30°C, recombinant enzyme
0.00014
D-fructose 1,6-bisphosphate
-
pH 7.5, 30°C, chimeric enzyme
0.00094
D-fructose 1,6-bisphosphate
-
mutant L54A, 22°C, pH 7.5
0.0011
D-fructose 1,6-bisphosphate
mutant D121A, E-tagged, pH 7.5
0.0012
D-fructose 1,6-bisphosphate
-
wild-type, 22°C, pH 7.5
0.00125
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant M248D
0.0013
D-fructose 1,6-bisphosphate
pH 7.5, mutant K50P/Y57W
0.0013
D-fructose 1,6-bisphosphate
wild-type muscle enzyme, pH 7.5, 37°C
0.0013
D-fructose 1,6-bisphosphate
mutant D118A, E-tagged, pH 7.5
0.0014
D-fructose 1,6-bisphosphate
pH 7.5, 30°C
0.0014
D-fructose 1,6-bisphosphate
22°C, pH 7.5, assay mixtures contains 1 mM phosphoenolpyruvate. Enzyme was incubated for 1 h in assay mixture. The reaction was initiated by the addition of Mg2+
0.0014
D-fructose 1,6-bisphosphate
-
mutant DELTA8
0.0014
D-fructose 1,6-bisphosphate
-
mutant DELTA6
0.0015
D-fructose 1,6-bisphosphate
muscle enzyme mutant T177M/Q179C, pH 7.5, 37°C
0.0015
D-fructose 1,6-bisphosphate
liver enzyme mutant E20K/M177T/C179Q, pH 7.5, 37°C
0.0015
D-fructose 1,6-bisphosphate
-
mutant DELTA5
0.0017
D-fructose 1,6-bisphosphate
muscle enzyme mutant K20E/T177M/Q179C, pH 7.5, 37°C
0.0017
D-fructose 1,6-bisphosphate
22°C, pH 7.5, assay is initiated by the addition of enzyme
0.0017
D-fructose 1,6-bisphosphate
-
wild-type enzyme
0.0017
D-fructose 1,6-bisphosphate
-
wild-type muscle isoenzyme enzyme
0.00175
D-fructose 1,6-bisphosphate
pH 7.5, wild-type enzyme
0.0018
D-fructose 1,6-bisphosphate
wild-type, pH 7.5
0.0018
D-fructose 1,6-bisphosphate
mutant E97A, E-tagged, pH 7.5
0.0019
D-fructose 1,6-bisphosphate
muscle enzyme mutant K20E, pH 7.5, 37°C
0.0019
D-fructose 1,6-bisphosphate
liver enzyme mutant M177T/C179Q, pH 7.5, 37°C
0.0019
D-fructose 1,6-bisphosphate
-
mutant DELTA10
0.002
D-fructose 1,6-bisphosphate
-
mutant DELTA3
0.0021
D-fructose 1,6-bisphosphate
pH 7.5, mutant K50P
0.0021
D-fructose 1,6-bisphosphate
wild-type liver enzyme, pH 7.5, 37°C
0.0021
D-fructose 1,6-bisphosphate
-
native rabbit muscle FBPase
0.0021
D-fructose 1,6-bisphosphate
-
mutant DELTA7
0.0021
D-fructose 1,6-bisphosphate
-
mutant DELTA4
0.0022
D-fructose 1,6-bisphosphate
wild-type, E-tagged, pH 7.5
0.0022
D-fructose 1,6-bisphosphate
-
wild-type liver isoenzyme enzyme
0.0023
D-fructose 1,6-bisphosphate
liver enzyme mutant E20K, pH 7.5, 37°C
0.0025
D-fructose 1,6-bisphosphate
pH 6.6, 25°C, native enzyme
0.0025
D-fructose 1,6-bisphosphate
pH 7.5, mutant A51P
0.0025
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant Y113A
0.0028
D-fructose 1,6-bisphosphate
-
mutant Y116F
0.0031
D-fructose 1,6-bisphosphate
-
-
0.0031
D-fructose 1,6-bisphosphate
-
mutant E69Q of rabbit muscle FBPase
0.00325
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant K112A
0.0037
D-fructose 1,6-bisphosphate
pH 8.0, 22°C, recombinant wild-type enzyme
0.004
D-fructose 1,6-bisphosphate
A0A7T7JA26
recombinant mutant T89S, pH and temperature not specified in the publication
0.0042 - 0.0048
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant M177A
0.0043
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F89W
0.0046
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F232W
0.0048
D-fructose 1,6-bisphosphate
30°C, pH 7.5, recombinant wild-type enzyme
0.0048
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant wild-type enzyme
0.005
D-fructose 1,6-bisphosphate
pH 6.6, 25°C, Trombin treated enzyme
0.005
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F16W
0.0051
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant L73A
0.0052
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant L56A
0.0053
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant Y164A
0.0057
D-fructose 1,6-bisphosphate
pH 8.0, 22°C, recombinant mutant T84S
0.0059
D-fructose 1,6-bisphosphate
30°C, pH 7.5, nonrecombinant enzyme
0.006
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F219W
0.0085
D-fructose 1,6-bisphosphate
-
pH 7.5, mutant enzyme T23I
0.0095
D-fructose 1,6-bisphosphate
-
pH 7.5, mutant enzyme T19I
0.01
D-fructose 1,6-bisphosphate
pH 6.6, 25°C, recombinant enzyme
0.0107
D-fructose 1,6-bisphosphate
-
mutant K115Q
0.0108
D-fructose 1,6-bisphosphate
-
pH 7.5, wild-type enzyme
0.0108
D-fructose 1,6-bisphosphate
-
wild-type
0.014
D-fructose 1,6-bisphosphate
pH 7.7, 50°
0.015
D-fructose 1,6-bisphosphate
37°C
0.0154
D-fructose 1,6-bisphosphate
-
pH 7.5, 30°C
0.016
D-fructose 1,6-bisphosphate
22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+
0.0165
D-fructose 1,6-bisphosphate
pH 8.0, temperature not specified in the publication, recombinant enzyme
0.0165
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
0.017
D-fructose 1,6-bisphosphate
A0A7T7JA26
recombinant wild-type enzyme, pH and temperature not specified in the publication
0.018
D-fructose 1,6-bisphosphate
-
pH 7.4, temperature not specified in the publication, wild-type enzyme
0.0198
D-fructose 1,6-bisphosphate
pH 8.0, 37°C
0.0201
D-fructose 1,6-bisphosphate
-
pH 7.5, mutant enzyme G20D
0.0269
D-fructose 1,6-bisphosphate
-
enzyme from healthy liver, pH 7.2, 22°C
0.027
D-fructose 1,6-bisphosphate
pH 7.8, 48°C, wild-type enzyme
0.027
D-fructose 1,6-bisphosphate
pH 7.8, 48°C, mutant enzyme Y229F
0.03
D-fructose 1,6-bisphosphate
-
0.036
D-fructose 1,6-bisphosphate
pH 7.8, 48°C, mutant enzyme Y348F
0.04
D-fructose 1,6-bisphosphate
-
pH not specified in the publication, 40°C
0.04
D-fructose 1,6-bisphosphate
-
pH 7.5, 60°C, purified recombinant enzyme
0.04
D-fructose 1,6-bisphosphate
-
pH 7.4, temperature not specified in the publication, mutant enzyme K274L
0.0419
D-fructose 1,6-bisphosphate
pH 7.5, 37°C
0.044
D-fructose 1,6-bisphosphate
-
pH 7.7, 30°C
0.05
D-fructose 1,6-bisphosphate
Campylobacter jejuni serotype O:2
pH 7.5, 25°C, recombinant enzyme
0.059
D-fructose 1,6-bisphosphate
recombinant enzyme, pH 8.0, 55°C
0.0598
D-fructose 1,6-bisphosphate
-
enzyme from anoxic liver, pH 7.2, 22°C
0.06
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant K29A
0.06
D-fructose 1,6-bisphosphate
pH 8.0, 25°C
0.066
D-fructose 1,6-bisphosphate
-
pH 7.5, 37°C, chloroplastic enzyme
0.07
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, wild-type
0.076
D-fructose 1,6-bisphosphate
-
pH 7.5, 37°C, chloroplastic enzyme
0.08
D-fructose 1,6-bisphosphate
wild-type, Hill coefficient 1.9, pH 8.0, 28°C
0.08
D-fructose 1,6-bisphosphate
mutant N213A, Hill coefficient 1.8, pH 8.0, 28°C
0.08
D-fructose 1,6-bisphosphate
mutant R314A, Hill coefficient 1.8, pH 8.0, 28°C
0.1
D-fructose 1,6-bisphosphate
95°C
0.1
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant E59A
0.1
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant K239A
0.1
D-fructose 1,6-bisphosphate
mutant H215A, Hill coefficient 1.4, pH 8.0, 28°C
0.1
D-fructose 1,6-bisphosphate
mutant T102A, Hill coefficient 2.5, pH 8.0, 28°C
0.11
D-fructose 1,6-bisphosphate
mutant R164A, Hill coefficient 2.1, pH 8.0, 28°C
0.11
D-fructose 1,6-bisphosphate
pH 8.0, 26-27°C, recombinant nontreated mutant C173S/C178S
0.12
D-fructose 1,6-bisphosphate
-
pH 7.5, 80°C, purified recombinant enzyme
0.121
D-fructose 1,6-bisphosphate
-
pH 8.8, 25°C, recombinant enzyme
0.15
D-fructose 1,6-bisphosphate
-
55°C
0.15
D-fructose 1,6-bisphosphate
-
70°C
0.15
D-fructose 1,6-bisphosphate
mutant K29A, Hill coefficient 2.0, pH 8.0, 28°C
0.165
D-fructose 1,6-bisphosphate
isozyme EgFBPaseI, pH 8.0, temperature not specified in the publication
0.165
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
0.17
D-fructose 1,6-bisphosphate
mutant D198H, Hill coefficient 1.9, pH 8.0, 28°C
0.2
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant D186A
0.2
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant R235A
0.2
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, wild-type enzyme
0.21
D-fructose 1,6-bisphosphate
mutant F309A, Hill coefficient 1.8, pH 8.0, 28°C
0.24
D-fructose 1,6-bisphosphate
mutant R307A, Hill coefficient 1.6, pH 8.0, 28°C
0.26
D-fructose 1,6-bisphosphate
mutant Y131A, Hill coefficient 1.6, pH 8.0, 28°C
0.3
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant R69A
0.3
D-fructose 1,6-bisphosphate
pH 8.0, 26-27°C, recombinant S-nitrosoglutathione-treated mutant C173S/C178S
0.31
D-fructose 1,6-bisphosphate
pH 8.0, 50°C
0.32
D-fructose 1,6-bisphosphate
pH 8.0, 22°C
0.43
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
0.43
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
0.44
D-fructose 1,6-bisphosphate
pH 7.7, 50°
0.5
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant H268A
0.5
D-fructose 1,6-bisphosphate
mutant K134A, Hill coefficient 2.2, pH 8.0, 28°C
0.6
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant Y24A
0.61
D-fructose 1,6-bisphosphate
mutant R178A, Hill coefficient 1.1, pH 8.0, 28°C
0.7
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant S19A
0.73
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
0.9
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant S65A
0.9
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant W131A
1.32
D-fructose 1,6-bisphosphate
mutant D200A, Hill coefficient 1.4, pH 8.0, 28°C
1.4
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant R181A
1.5
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant H178A
2.2
D-fructose 1,6-bisphosphate
isozyme EgFBPaseII, pH 8.0, temperature not specified in the publication
2.2
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
2.3
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant H244A
3.2
D-fructose 1,6-bisphosphate
mutant R176A, Hill coefficient 1.2, pH 8.0, 28°C
0.0111
D-fructose 1,6-diphosphate

pH 8.0, 23°C
99.98
D-fructose 1,6-diphosphate
-
-
0.0018
D-fructose-1,6-bisphosphate

-
pH 7.5, 22°C, wild-type enzyme
0.014
D-fructose-1,6-bisphosphate
-
pH 7.7, 30°C
0.035
D-fructose-1,6-bisphosphate
pH 7.7
0.1
fructose 1,6-bisphosphate

wild-type
0.45
fructose 1,6-bisphosphate
-
37°C, pH 10.0
0.00054
fructose 1,6-diphosphate

-
-
0.00077
fructose 1,6-diphosphate
-
-
0.0008
fructose 1,6-diphosphate
-
-
0.00084
fructose 1,6-diphosphate
mutant enzyme G191A
0.001
fructose 1,6-diphosphate
-
at 10 mM Mg2+
0.00103
fructose 1,6-diphosphate
-
mutant enzyme D74E, pH 8.5
0.0013
fructose 1,6-diphosphate
-
-
0.00131
fructose 1,6-diphosphate
-
mutant enzyme D68E, pH 7.5
0.00142
fructose 1,6-diphosphate
-
mutant enzyme N64A, pH 8.5
0.00142
fructose 1,6-diphosphate
mutant enzyme Q32L
0.0015
fructose 1,6-diphosphate
-
-
0.00153
fructose 1,6-diphosphate
mutant enzyme K42T
0.0016
fructose 1,6-diphosphate
-
mutant enzyme K71M/K72M, pH 7.5
0.00167
fructose 1,6-diphosphate
mutant enzyme K42E
0.0017
fructose 1,6-diphosphate
-
-
0.0017
fructose 1,6-diphosphate
-
mutant enzyme N64E, pH 8.5
0.00172
fructose 1,6-diphosphate
-
-
0.00181
fructose 1,6-diphosphate
mutant enzyme I190T
0.002
fructose 1,6-diphosphate
-
-
0.002
fructose 1,6-diphosphate
-
-
0.002
fructose 1,6-diphosphate
-
alkaline isoenzyme
0.0022
fructose 1,6-diphosphate
-
wild type enzyme, pH 8.5
0.0025
fructose 1,6-diphosphate
-
-
0.0028
fructose 1,6-diphosphate
-
wild type enzyme, pH 7.5
0.0028
fructose 1,6-diphosphate
-
mutant enzyme K71A, pH 7.5
0.003
fructose 1,6-diphosphate
-
activated by Mg2+ or Mn2+, at 9°C
0.0034
fructose 1,6-diphosphate
-
neutral isoenzyme
0.00344
fructose 1,6-diphosphate
-
mutant enzyme R49L
0.00351
fructose 1,6-diphosphate
wild type enzyme
0.00351
fructose 1,6-diphosphate
-
wild type enzyme
0.004
fructose 1,6-diphosphate
-
activated by Mg2+, at 17°C
0.00402
fructose 1,6-diphosphate
-
mutant enzyme K50M
0.00407
fructose 1,6-diphosphate
-
mutant enzyme R49C
0.00442
fructose 1,6-diphosphate
-
mutant enzyme R49D
0.005
fructose 1,6-diphosphate
-
-
0.005
fructose 1,6-diphosphate
-
activated by Mg2+, at 22°C or activated by Mn2+ at 17°C
0.006
fructose 1,6-diphosphate
-
without phosphoenolpyruvate
0.008
fructose 1,6-diphosphate
-
-
0.008
fructose 1,6-diphosphate
-
activated by Mn2+ at 35°C or at 22°C
0.008
fructose 1,6-diphosphate
-
activated by Mn2+
0.0083
fructose 1,6-diphosphate
-
-
0.01
fructose 1,6-diphosphate
-
at 2 mM Mg2+
0.01
fructose 1,6-diphosphate
-
activated by Mg2+, at 27°C or activated by Mn2+ at 31°C
0.011
fructose 1,6-diphosphate
-
activated by Mg2+, at 31°C or at 35°C
0.011
fructose 1,6-diphosphate
-
activated by Mg2+
0.013
fructose 1,6-diphosphate
-
in presence of 0.01 mM phosphoenolpyruvate
0.017
fructose 1,6-diphosphate
-
isoenzyme A and B
0.022
fructose 1,6-diphosphate
-
enzyme from ethanol-grown cells
0.025
fructose 1,6-diphosphate
-
isoenzyme F-II
0.029
fructose 1,6-diphosphate
-
enzyme from methanol-grown cells
0.045
fructose 1,6-diphosphate
-
-
0.052
fructose 1,6-diphosphate
-
isoenzyme F-I
0.057
fructose 1,6-diphosphate
-
isoenzyme F-I
0.0031
Ribulose 1,5-diphosphate

-
-
0.021
Ribulose 1,5-diphosphate
-
-
0.0026
sedoheptulose 1,7-diphosphate

-
-
0.008
sedoheptulose 1,7-diphosphate
-
-
0.015
sedoheptulose 1,7-diphosphate
-
isoenzyme A and B
0.03
sedoheptulose 1,7-diphosphate
-
-
0.18
sedoheptulose 1,7-diphosphate
-
isoenzyme F-I
0.3
sedoheptulose 1,7-diphosphate
-
-
1
sedoheptulose 1,7-diphosphate
-
in presence of 5 mM Mg2+
1.4
sedoheptulose 1,7-diphosphate
-
in presence of 5 mM Mn2+
additional information
additional information

-
-
-
additional information
additional information
-
illumination of the chloroplast causes a decrease in Km
-
additional information
additional information
-
comparison of KM of wild-type and hybrid enzymes
-
additional information
additional information
enzyme shows a mechanism of cooperativity that arises from within a single subunit
-
additional information
additional information
-
enzyme shows a mechanism of cooperativity that arises from within a single subunit
-
additional information
additional information
-
enzyme shows unusual temperature dependence for its main substrate di-myo-inositol 1,1-phosphate
-
additional information
additional information
the Km of FBPase reaches its highest significant value in January. In March, May and June, the Km-value remains constant, and lower than January. In October the value increases again significantly with regard to the previous months, although it does not reach the peak attained in January. The lowest significant value is reached in Novemer
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
with all natural substrates, YK23 shows classical hyperbolic saturation kinetics
-
additional information
additional information
-
with all natural substrates, YK23 shows classical hyperbolic saturation kinetics
-
additional information
additional information
activity assays show that the substrate D-fructose 1,6-bisphosphate binds to the enzyme with positive cooperativity, Michaelis-Menten plot
-
additional information
additional information
-
activity assays show that the substrate D-fructose 1,6-bisphosphate binds to the enzyme with positive cooperativity, Michaelis-Menten plot
-
additional information
additional information
kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics, from Arrhenius plots, activation energies for phosphatase and aldolase reactions are calculated 46.5 and 75.62 kJ/mol, respectively
-
additional information
additional information
Campylobacter jejuni serotype O:2
hyperbolic Michaelis-Menten kinetics
-
additional information
additional information
-
enzyme kinetic analysis, the purified enzyme shows a significant decrease in sensitivity to its substrate fructose-1,6-bisphosphate in the liver of frozen frogs as compared with controls
-
additional information
additional information
A0A7T7JA26
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.026 - 175
beta-D-glucose 1,6-bisphosphate
0.0014 - 212
D-fructose 1,6-bisphosphate
3.2 - 22
D-fructose-1,6-bisphosphate
2.5
fructose 1,6-bisphosphate
wild-type
0.0004 - 34
fructose 1,6-diphosphate
additional information
additional information
-
0.026
beta-D-glucose 1,6-bisphosphate

-
mutant enzyme T16P, in 50 mM K+HEPES pH 7.0 at 25°C
0.026
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme H20A, in 50 mM K+HEPES pH 7.0 at 25°C
0.62
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme H20N, in 50 mM K+HEPES pH 7.0 at 25°C
1.56
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme K76A, in 50 mM K+HEPES pH 7.0 at 25°C
20
beta-D-glucose 1,6-bisphosphate
-
wild type enzyme, in 50 mM K+HEPES pH 7.0 at 25°C
21.9
beta-D-glucose 1,6-bisphosphate
-
mutant enzyme H20Q, in 50 mM K+HEPES pH 7.0 at 25°C
175
beta-D-glucose 1,6-bisphosphate
-
wild type enzyme, in 50 mM K+HEPES pH 7.0 at 25°C
0.0014
D-fructose 1,6-bisphosphate

-
mutant DELTA8
0.0014
D-fructose 1,6-bisphosphate
-
mutant DELTA6
0.0015
D-fructose 1,6-bisphosphate
-
mutant DELTA5
0.0019
D-fructose 1,6-bisphosphate
-
mutant DELTA10
0.002
D-fructose 1,6-bisphosphate
-
mutant DELTA3
0.0021
D-fructose 1,6-bisphosphate
-
mutant DELTA7
0.0021
D-fructose 1,6-bisphosphate
-
mutant DELTA4
0.12
D-fructose 1,6-bisphosphate
A0A7T7JA26
recombinant mutant T89S, pH and temperature not specified in the publication
0.17
D-fructose 1,6-bisphosphate
isozyme EgFBPaseI, pH 8.0, temperature not specified in the publication
0.17
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
0.22
D-fructose 1,6-bisphosphate
pH 8.0, 22°C, recombinant mutant T84S
0.26
D-fructose 1,6-bisphosphate
pH 7.8, 48°C, mutant enzyme Y348F
0.3
D-fructose 1,6-bisphosphate
pH 8.0, 50°C
0.3
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant S65A
0.5
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant H178A
0.55
D-fructose 1,6-bisphosphate
-
pH 7.5, lung
0.55
D-fructose 1,6-bisphosphate
A0A7T7JA26
recombinant wild-type enzyme, pH and temperature not specified in the publication
0.62
D-fructose 1,6-bisphosphate
pH 7.8, 48°C, wild-type enzyme
0.63
D-fructose 1,6-bisphosphate
mutant D200A, Hill coefficient 1.4, pH 8.0, 28°C
0.66
D-fructose 1,6-bisphosphate
pH 7.8, 48°C, mutant enzyme Y229F
0.7
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant Y24A
0.7
D-fructose 1,6-bisphosphate
mutant R176A, Hill coefficient 1.2, pH 8.0, 28°C
0.7
D-fructose 1,6-bisphosphate
mutant T102A, Hill coefficient 2.5, pH 8.0, 28°C
0.84
D-fructose 1,6-bisphosphate
mutant D198H, Hill coefficient 1.9, pH 8.0, 28°C
1.08
D-fructose 1,6-bisphosphate
isozyme EgFBPaseII, pH 8.0, temperature not specified in the publication
1.08
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
1.1
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant E59A
1.2
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant D186A
1.2
D-fructose 1,6-bisphosphate
pH 7.7, 50°
1.2
D-fructose 1,6-bisphosphate
mutant H215A, Hill coefficient 1.4, pH 8.0, 28°C
1.2
D-fructose 1,6-bisphosphate
mutant Y131A, Hill coefficient 1.6, pH 8.0, 28°C
1.6
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant R181A
1.8
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant R69A
1.8
D-fructose 1,6-bisphosphate
mutant K134A, Hill coefficient 2.2, pH 8.0, 28°C
1.9
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant W131A
2.1
D-fructose 1,6-bisphosphate
pH 8.0, 22°C, recombinant wild-type enzyme
2.3
D-fructose 1,6-bisphosphate
mutant R164A, Hill coefficient 2.1, pH 8.0, 28°C
2.6
D-fructose 1,6-bisphosphate
mutant R314A, Hill coefficient 1.8, pH 8.0, 28°C
2.8
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant H244A
2.9
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant S19A
3.9
D-fructose 1,6-bisphosphate
mutant D118A, E-tagged, pH 7.5
3.9
D-fructose 1,6-bisphosphate
pH 7.7, 50°
4.6
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, mutant H268A
4.9
D-fructose 1,6-bisphosphate
pH 7.5, 30°C, wild-type enzyme
5.2
D-fructose 1,6-bisphosphate
mutant N213A, Hill coefficient 1.8, pH 8.0, 28°C
5.2
D-fructose 1,6-bisphosphate
mutant R307A, Hill coefficient 1.6, pH 8.0, 28°C
5.2
D-fructose 1,6-bisphosphate
mutant F309A, Hill coefficient 1.8, pH 8.0, 28°C
5.3
D-fructose 1,6-bisphosphate
mutant E97A, E-tagged, pH 7.5
5.4
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant R235A
5.7
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, wild-type
5.8
D-fructose 1,6-bisphosphate
mutant D121A, E-tagged, pH 7.5
6.7
D-fructose 1,6-bisphosphate
pH 7.5, mutant K50P
7.1
D-fructose 1,6-bisphosphate
mutant R178A, Hill coefficient 1.1, pH 8.0, 28°C
7.5
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant K239A
8
D-fructose 1,6-bisphosphate
22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+
8
D-fructose 1,6-bisphosphate
pH 8.0, 37°C
8.4
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
8.57
D-fructose 1,6-bisphosphate
-
pH 7.5, 60°C, purified recombinant enzyme
9.2
D-fructose 1,6-bisphosphate
pH 7.5, mutant K50P/Y57W
10.5
D-fructose 1,6-bisphosphate
wild-type, Hill coefficient 1.9, pH 8.0, 28°C
11.3
D-fructose 1,6-bisphosphate
-
mutant L54A, 22°C, pH 7.5
11.5 - 12.8
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant M177A
12.4
D-fructose 1,6-bisphosphate
pH 7.5, mutant A51P
13.5
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant Y164A
14
D-fructose 1,6-bisphosphate
pH 9.0, 37°C, mutant K29A
14.2
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F232W
14.6
D-fructose 1,6-bisphosphate
-
pH 7.5, 30°C
14.8
D-fructose 1,6-bisphosphate
-
pH 7.5, lung
15
D-fructose 1,6-bisphosphate
-
pH 7.5, mutant enzyme G20D
16.1
D-fructose 1,6-bisphosphate
-
pH 7.5, lung
16.7
D-fructose 1,6-bisphosphate
-
wild-type liver isoenzyme enzyme
17
D-fructose 1,6-bisphosphate
95°C
17.6
D-fructose 1,6-bisphosphate
muscle enzyme mutant K20E/T177M/Q179C, pH 7.5, 37°C
18
D-fructose 1,6-bisphosphate
pH 8.0, 22°C
18.1
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F16W
18.4
D-fructose 1,6-bisphosphate
liver enzyme mutant M177T/C179Q, pH 7.5, 37°C
18.6
D-fructose 1,6-bisphosphate
liver enzyme mutant E20K, pH 7.5, 37°C
18.7
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F219W
19.2
D-fructose 1,6-bisphosphate
30°C, pH 7.5, mutant enzyme F89W
19.7
D-fructose 1,6-bisphosphate
30°C, pH 7.5, recombinant wild-type enzyme
19.9
D-fructose 1,6-bisphosphate
muscle enzyme mutant T177M/Q179C, pH 7.5, 37°C
20
D-fructose 1,6-bisphosphate
-
wild-type, 22°C, pH 7.5
20.4
D-fructose 1,6-bisphosphate
-
pH 7.5, mutant enzyme T23I
20.5
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant wild-type enzyme
20.7
D-fructose 1,6-bisphosphate
30°C, pH 7.5, nonrecombinant enzyme
20.8
D-fructose 1,6-bisphosphate
wild-type liver enzyme, pH 7.5, 37°C
21
D-fructose 1,6-bisphosphate
pH 7.5, 30°C
21.1
D-fructose 1,6-bisphosphate
muscle enzyme mutant K20E, pH 7.5, 37°C
21.3
D-fructose 1,6-bisphosphate
mutant K29A, Hill coefficient 2.0, pH 8.0, 28°C
21.7
D-fructose 1,6-bisphosphate
liver enzyme mutant E20K/M177T/C179Q, pH 7.5, 37°C
21.7
D-fructose 1,6-bisphosphate
-
wild-type, pH 7.0, 37°C
22
D-fructose 1,6-bisphosphate
-
pH 7.5
22
D-fructose 1,6-bisphosphate
pH 7.5, wild-type enzyme
22
D-fructose 1,6-bisphosphate
wild-type, pH 7.5
22.5
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant L73A
22.9
D-fructose 1,6-bisphosphate
-
pH 8.8, 25°C, recombinant enzyme
23
D-fructose 1,6-bisphosphate
wild-type, E-tagged, pH 7.5
23.4
D-fructose 1,6-bisphosphate
wild-type muscle enzyme, pH 7.5, 37°C
23.5
D-fructose 1,6-bisphosphate
-
wild-type muscle isoenzyme enzyme
24
D-fructose 1,6-bisphosphate
22°C, pH 7.5, assay is initiated by the addition of enzyme
24.3
D-fructose 1,6-bisphosphate
-
pH 7.5, wild-type enzyme
24.7
D-fructose 1,6-bisphosphate
-
mutant Y57W, pH 7.0, 37°C
25.6
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant L56A
26
D-fructose 1,6-bisphosphate
22°C, pH 7.5, assay mixtures contains 1 mM phosphoenolpyruvate. Enzyme was incubated for 1 h in assay mixture. The reaction was initiated by the addition of Mg2+
26.4
D-fructose 1,6-bisphosphate
pH 8.0, temperature not specified in the publication, recombinant enzyme
26.4
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
26.8
D-fructose 1,6-bisphosphate
-
pH 7.5, mutant enzyme T19I
26.8
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant K112A
27.2
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant Y113A
30.5
D-fructose 1,6-bisphosphate
pH 7.5, 37°C, recombinant mutant M248D
58.7
D-fructose 1,6-bisphosphate
-
pH 7.5, 80°C, purified recombinant enzyme
212
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
212
D-fructose 1,6-bisphosphate
pH and temperature not specified in the publication
3.2
D-fructose-1,6-bisphosphate

-
pH 7.7, 30°C
22
D-fructose-1,6-bisphosphate
-
pH 7.5, 22°C, wild-type enzyme
0.0004
fructose 1,6-diphosphate

-
mutant enzyme D74A, pH 8.5
0.01
fructose 1,6-diphosphate
-
mutant enzyme D74N, pH 8.5
1.2
fructose 1,6-diphosphate
-
mutant enzyme D74E, pH 8.5
2.3
fructose 1,6-diphosphate
mutant enzyme G191A
5.4
fructose 1,6-diphosphate
-
mutant enzyme N64E, pH 8.5
6.4
fructose 1,6-diphosphate
-
mutant enzyme D68E, pH 7.5
7.1
fructose 1,6-diphosphate
-
mutant enzyme N64A, pH 8.5
9.1
fructose 1,6-diphosphate
-
wild type enzyme, pH 8.5
16
fructose 1,6-diphosphate
-
mutant enzyme K71A, pH 7.5
18
fructose 1,6-diphosphate
wild type enzyme
18
fructose 1,6-diphosphate
-
wild type enzyme
18.3
fructose 1,6-diphosphate
mutant enzyme K42T
19.3
fructose 1,6-diphosphate
mutant enzyme K42E
20.1
fructose 1,6-diphosphate
-
mutant enzyme R49D
21
fructose 1,6-diphosphate
-
wild type enzyme, pH 7.5
21.1
fructose 1,6-diphosphate
mutant enzyme I190T
22.4
fructose 1,6-diphosphate
-
mutant enzyme K50M
23.6
fructose 1,6-diphosphate
-
mutant enzyme R49L and R49C
32.1
fructose 1,6-diphosphate
mutant enzyme Q32L
34
fructose 1,6-diphosphate
-
mutant enzyme K71M/K72M, pH 7.5
additional information
additional information

-
-
additional information
additional information
-
-
-
additional information
additional information
-
comparison of kcat of wild-type and hybrid enzymes
-
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0.0031
(1H-indol-1-yl)(4-(trifluoromethyl)phenyl)methanone
Mus musculus
-
pH 7.5, 37°C
0.01091
(2,3-diethoxy-7,8,9,10-tetrahydro-6H-cyclohepta[b]quinolin-11-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
Oryctolagus cuniculus
-
37°C
0.0164
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.354
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl)phosphonic acid
Homo sapiens
-
0.0191
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.00932
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)phosphonic acid
Homo sapiens
-
0.0215
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.354
(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl)phosphonic acid
Homo sapiens
-
0.0417
(2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.000169
(2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl)phosphonic acid
Homo sapiens
-
0.000124
(2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.0284
(2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl)phosphonic acid
Homo sapiens
-
0.112
(2-amino-8H-indeno[1,2-d][1,3]thiazol-5-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.0187
(2-amino-8H-indeno[1,2-d][1,3]thiazol-5-yl)phosphonic acid
Homo sapiens
-
0.112
(2-amino-8H-indeno[1,2-d][1,3]thiazol-6-yl)methyl dihydrogen phosphate
Homo sapiens
-
0.0919
(2-amino-8H-indeno[1,2-d][1,3]thiazol-6-yl)phosphonic acid
Homo sapiens
-
0.02171
(2-aminomethyl-6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]-amine
Oryctolagus cuniculus
-
37°C
0.00029 - 0.0045
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
0.0017
(3-Bromo-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.0017 mM
0.0045
(3-Bromo-phenyl)-(6,7-dimethoxy-2-methyl-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.0045 mM
0.001
(3-Bromo-phenyl)-(6,7-dimethoxy-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.001 mM
0.0039
(3-Bromo-phenyl)-(7-ethoxy-6-nitro-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.0039 mM
0.0029
(3-Bromo-phenyl)-[6-(2-methoxy-ethoxy)-quinazolin-4-yl]-amine
Homo sapiens
-
IC50: 0.0029 mM
0.0055
(3-Bromo-phenyl)-[7-methoxy-6-(2-methoxy-ethoxy)-quinazolin-4-yl]-amine
Homo sapiens
-
IC50: 0.0055 mM
0.00053
(3-Chloro-4-fluoro-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.00053 mM
0.0016
(3-Chloro-phenyl)-(6,7-diethoxy-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.0016 mM
0.0013
(3-Chloro-phenyl)-(6,7-dimethoxy-quinazolin-4-yl)-amine
Homo sapiens
-
IC50: 0.0013 mM
0.000858
(5-[2-amino-5-[(propylsulfanyl)carbonyl]-1,3-thiazol-4-yl]furan-2-yl)phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000055 - 0.0004
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid
0.0026
(6,7-diethoxy-1,2,3,4-tetrahydroacridin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
Oryctolagus cuniculus
-
37°C
0.0041
(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)[3-(2-methylthiazol-4-yl)phenyl]amine
Oryctolagus cuniculus
-
37°C
0.0024
(6,7-Diethoxy-quinazolin-4-yl)-(3-ethynyl-phenyl)-amine
Homo sapiens
-
IC50: 0.0024 mM
0.0092
(6,7-Diethoxy-quinazolin-4-yl)-(3-fluoro-phenyl)-amine
Homo sapiens
-
IC50: 0.0092 mM
0.0021
(6,7-Diethoxy-quinazolin-4-yl)-(3-iodo-phenyl)-amine
Homo sapiens
-
IC50: 0.0021 mM
0.0009
(6,7-Dimethoxy-quinazolin-4-yl)-(3-ethynyl-phenyl)-amine
Homo sapiens
-
IC50: 0.0009 mM
0.05
1-(cyclopropyl)methyl-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
0.05
1-benzyl-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
0.055
2,5-dichloro-N-(4-methyl-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.0034
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
0.0064
2,5-dichloro-N-(5-methyl-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.0081
2,5-dichloro-N-(6-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.008
2,5-dichloro-N-(6-methoxy-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.01
2,5-dichloro-N-(6-methyl-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.004
2,5-dichloro-N-[5-(3-furyl)-1,3-benzoxazol-2-yl]benzenesulfonamide
Homo sapiens
-
-
0.0035
2,5-dichloro-N-[5-methoxy-7-(4-methoxypyridin-3-yl)-1,3-benzoxazol-2-yl]benzenesulfonamide
Homo sapiens
-
-
0.0017
2,5-dichloro-N-[7-(3-hydroxyphenyl)-5-methoxy-1,3-benzoxazol-2-yl]benzenesulfonamide
Homo sapiens
-
-
0.0018
2,5-dichloro-N-[7-(4-hydroxyphenyl)-5-methoxy-1,3-benzoxazol-2-yl]benzenesulfonamide
Homo sapiens
-
-
0.119
2-(2-(phenylamino)thiazol-4-yl)phenol
Sus scrofa
-
0.00022
2-(2-aminoethyl)-6,7-diethoxy-N-[3-(2-methyl-1,3-thiazol-4-yl)phenyl]quinazolin-4-amine
Homo sapiens
-
uncompetitive
0.008
2-(2-thienyl)-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.005
2-(3-pyridyl)-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.015
2-(4-(4-hydroxyphenyl)thiazol-2-ylamino)phenol
Sus scrofa
-
0.27
2-(4-phenylthiazol-2-ylamino)phenol
Sus scrofa
-
0.01
2-acetamido-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.112
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-7-yl dihydrogen phosphate
Homo sapiens
-
0.000013
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl dihydrogen phosphate
Homo sapiens
-
0.335
2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-9-yl dihydrogen phosphate
Homo sapiens
-
0.0013
2-amino-4-[1-(3-phosphono)phenyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
2-amino-4-[2-(6-phosphono)pyridyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000022
2-amino-5,6-dihydro-4H-benzo[6,7]cyclohepta[1,2-d][1,3]thiazol-9-yl dihydrogen phosphate
Homo sapiens
-
0.000028
2-amino-5-(2,2,2-trifluoroethyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00004
2-amino-5-(2-furanyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000043
2-amino-5-(2-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000012
2-amino-5-(2-naphthyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.95
2-amino-5-(2-thienyl)-4-[(N-phosphonomethyl)carbamoyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000044
2-amino-5-(2-thienyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000021
2-amino-5-(3-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000032
2-amino-5-(4-acetylphenyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000013
2-amino-5-(4-chlorophenyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000016
2-amino-5-(4-fluorophenyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000041
2-amino-5-(4-methanesulfonyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000014
2-amino-5-(4-methoxycarbonylphenyl)-4-[2-(5-phosphono)-furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000022
2-amino-5-(4-methoxyphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000021
2-amino-5-(4-methylthiophenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000034
2-amino-5-(4-phenylphenyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000088
2-amino-5-(4-tert-butylphenyl)-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000016
2-amino-5-(N-morpholinyl)-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000059
2-amino-5-benzyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000015
2-amino-5-benzyloxycarbonyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00005
2-amino-5-bromo-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00007
2-amino-5-chloro-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000012
2-amino-5-cyclobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000021
2-amino-5-cyclohexyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000018
2-amino-5-cyclohexylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000019
2-amino-5-cyclopentyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00002
2-amino-5-cyclopentylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00001
2-amino-5-cyclopropylmethyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000033
2-amino-5-ethylthio-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00012
2-amino-5-hydroxymethyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
2-amino-5-iodo-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.016 - 0.061
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
0.21
2-amino-5-isopropyl- 4-[1-(4-methoxy-3-phosphono)phenyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00003
2-amino-5-isopropyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000024
2-amino-5-isopropylthio-4-[2-(5-phosphono)furanyl]thiazole hydrobromide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00045
2-amino-5-methyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000057
2-amino-5-neopentyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.08
2-amino-5-phenyl- 4-[1-(4-fluoro-3-phosphono)phenyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.01
2-amino-5-phenyl-4-[2-(5-methyl-4-phosphono)oxazolyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.01
2-amino-5-phenyl-4-[3-(1-phosphono)pyrrolyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0003
2-amino-5-phenylthio-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.135
2-amino-5-propyl- 4-[1-(4-methyl-3-phosphono)phenyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.05
2-amino-5-propyl-4-phosphonomethoxycarbonylthiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.25
2-amino-5-propyl-4-[1-(3-phosphono)phenyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0005
2-amino-5-propyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000024
2-amino-5-tert-butylthio-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00015
2-amino-5-[(4-morpholinyl)methyl]-4-[2-(5-phosphono)furanyl]-thiazole dihydrobromide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0017
2-amino-5-[(N,N-dimethyl)carbamoyl]-4-[2-(5-phosphono)-furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00007
2-amino-8H-indeno[1,2-d][1,3]thiazol-4-yl dihydrogen phosphate
Homo sapiens
-
0.307
2-amino-8H-indeno[1,2-d][1,3]thiazol-5-yl dihydrogen phosphate
Homo sapiens
-
0.146
2-amino-8H-indeno[1,2-d][1,3]thiazol-6-yl dihydrogen phosphate
Homo sapiens
-
0.00008
2-bromo-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0065
2-bromo-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.00275
2-carbamoyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00018
2-chloro-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
2-cyano-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0004
2-ethyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00022
2-hydroxymethyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001
2-methyl-5-isobutyl-4-[2-(5-phosphono)furanyl]-thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.001
2-methylamino-5-isobutyl-4-[2-(5-hosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00089
2-methylthio-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
3.1
2-oxoglutarate
Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
0.0135
2-phenyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0005
2-thiocarbamoyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0012
2-vinyl-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00187
2-[(3S,11aS)-3-(4-hydroxybenzyl)-1,4-dioxo-1,3,4,6,11,11a-hexahydro-2H-pyrazino[1,2-b]isoquinolin-2-yl]-N-[2-(4-hydroxyphenyl)ethyl]pentanamide
Homo sapiens
-
uncompetitive
0.00052 - 0.0073
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate
0.00067 - 0.0035
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate
0.0147
3,4-dihydroxy-N'-[(E)-[4-oxo-6-(propan-2-yl)-4H-chromen-3-yl]methylidene]benzohydrazide
Synechocystis sp.
pH 7.5, temperature not specified in the publication
0.0061
3,5-diphenyl-1-(3-(trifluoromethyl) phenyl)-1H-pyrazole
Mus musculus
-
pH 7.5, 37°C
0.05
3-(2-(ethoxycarbonyl)-7-nitro-1H-indol-3-yl)propanoic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
0.0025
3-(2-carboxyethyl)-4,6-dichloro-1H-indole-2-carboxylic acid
Homo sapiens
-
non-competitive
0.0024
3-(2-carboxyethyl)-4-(2-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
0.00069
3-(2-carboxyethyl)-4-(2-methylpropyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00527
3-(2-carboxyethyl)-4-(3-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
0.00131
3-(2-carboxyethyl)-4-(3-methoxyanilino)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00522
3-(2-carboxyethyl)-4-(3-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
0.0024
3-(2-carboxyethyl)-4-(4-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
0.0017
3-(2-carboxyethyl)-4-(4-methoxyanilino)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0018
3-(2-carboxyethyl)-4-(4-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
0.00088
3-(2-carboxyethyl)-4-chloro-7-nitro-1H-indole-2-carboxylic acid
0.00276
3-(2-carboxyethyl)-4-ethyl-7-nitro-1H-indole-2-carboxylic acid
0.00069
3-(2-carboxyethyl)-4-isobutyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00045
3-(2-carboxyethyl)-5-(2-methylpropyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00129
3-(2-carboxyethyl)-5-bromo-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00207
3-(2-carboxyethyl)-5-chloro-7-nitro-1H-indole-2-carboxylic acid
0.00047
3-(2-carboxyethyl)-5-cyclopropyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.0001
3-(2-carboxyethyl)-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0001
3-(2-carboxyethyl)-5-ethyl-7-nitro-1H-indole-2-carboxylicacid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00045
3-(2-carboxyethyl)-5-isobutyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.05
3-(2-carboxyethyl)-5-nitro-1H-indole-2-carboxylic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
0.0016
3-(2-carboxyethyl)-5-phenylamino-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0014
3-(2-carboxyethyl)-7-chloro-5-cyclopropyl-1H-indole-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.0019
3-(2-carboxyethyl)-7-chloro-5-ethyl-1H-indole-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.0013
3-(2-carboxyethyl)-7-chloro-5-propyl-1H-indole-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.00517
3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
0.00131
3-(2-carboxyethyl)-7-nitro-4-(3-methoxyphenylamino)-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0011
3-(2-carboxyethyl)-7-nitro-4-(3-nitrophenyl)-1H-indole-2-carboxylic acid
0.0017
3-(2-carboxyethyl)-7-nitro-4-(4-methoxyphenylamino)-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.002
3-(2-carboxyethyl)-7-nitro-4-(4-nitrophenyl)-1H-indole-2-carboxylic acid
0.0014
3-(2-carboxyethyl)-7-nitro-4-phenyl-1H-indole-2-carboxylic acid
0.00069
3-(2-carboxyethyl)-7-nitro-4-phenylamino-1H-indole-2-carboxylic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00643
3-(2-carboxyethyl)-7-nitro-5-phenyl-1H-indole-2-carboxylic acid
0.00042
3-(2-carboxyethyl)-7-nitro-5-propyl-1H-indole-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.00195 - 0.00594
3-(3-amino-3-oxopropyl)-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
0.05
3-(4-(4-hydroxyphenyl)thiazol-2-ylamino)benzenesulfonamide
Sus scrofa
-
0.013
3-(4-(4-hydroxyphenyl)thiazol-2-ylamino)phenol
Sus scrofa
-
0.104
3-(4-phenylthiazol-2-ylamino)benzenesulfonamide
Sus scrofa
-
0.035
3-(4-phenylthiazol-2-ylamino)phenol
Sus scrofa
-
0.0013
3-chloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.00064 - 0.012
3-chloro-N-[(3,5-dichlorophenyl)carbamoyl]benzenesulfonamide
0.00099
3-ethyl-5-isobutyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
-
pH 7.5, 37°C
0.00186
3-[3-[(3-chlorobenzene-1-sulfonyl)amino]-3-oxopropyl]-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.00066
3-[3-[(benzenesulfonyl)amino]-3-oxopropyl]-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.00131
3-[3-[(cyclopropanesulfonyl)amino]-3-oxopropyl]-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.0011
3-[3-[(ethanesulfonyl)amino]-3-oxopropyl]-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.02
4-(2-(2-hydroxyphenylamino)thiazol-4-yl)benzene-1,3-diol
Sus scrofa
-
0.006
4-(2-(3-hydroxyphenylamino)thiazol-4-yl)benzene-1,3-diol
Sus scrofa
-
0.048
4-(2-(3-nitrophenylamino)thiazol-4-yl)phenol
Sus scrofa
-
0.011
4-(2-(4-hydroxyphenylamino)thiazol-4-yl)benzene-1,3-diol
Sus scrofa
-
0.246
4-(2-(4-nitrophenylamino)thiazol-4-yl)phenol
Sus scrofa
-
0.343
4-(2-(phenylamino)thiazol-4-yl)benzene-1,3-diol
Sus scrofa
-
0.055
4-(4-(2,4-dihydroxyphenyl)thiazol-2-ylamino)benzenesulfonamide
Sus scrofa
-
0.032
4-(4-(4-hydroxyphenyl)thiazol-2-ylamino)benzenesulfonamide
Sus scrofa
-
0.048
4-(4-(4-hydroxyphenyl)thiazol-2-ylamino)phenol
Sus scrofa
-
0.145
4-(4-phenylthiazol-2-ylamino)benzenesulfonamide
Sus scrofa
-
0.124
4-(4-phenylthiazol-2-ylamino)phenol
Sus scrofa
-
0.00069
4-anilino-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.024
4-tert-butyl-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.015
4-[[(2R,4S)-4-(3-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
-
0.1
4-[[(2R,4S)-4-(3-methoxyphenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
value above
0.066
4-[[(2R,4S)-4-(4-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
-
0.1
4-[[(2S,4S)-4-(3-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
value above
0.1
4-[[(2S,4S)-4-(3-methoxyphenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
value above
0.1
4-[[(2S,4S)-4-(4-chlorophenyl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
value above
0.00298
5-(1H-tetrazol-5-yl)-N-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenyl)pentanamide
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.00035 - 0.004
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
0.00017 - 0.0016
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide
0.0017 - 0.0083
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
0.00053 - 0.007
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
0.00022 - 0.0026
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide
0.0016
5-anilino-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00129
5-bromo-3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00092
5-ethyl-7-nitro-3-[3-oxo-3-[(propane-2-sulfonyl)amino]propyl]-1H-indole-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.00042 - 0.0005
5-ethyl-7-nitro-3-[3-oxo-3-[(thiophene-2-sulfonyl)amino]propyl]-1H-indole-2-carboxylic acid
0.0005
5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0041
6,7-diethoxy-N-[3-(2-methyl-1,3-thiazol-4-yl)phenyl]quinazolin-4-amine
Oryctolagus cuniculus
-
-
0.022
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-2-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
-
0.0088
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-3-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
-
0.041
6,7-dimethyl-4-[[(2R,4S)-2-oxido-4-(pyridin-4-yl)-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
-
0.004 - 0.011
6,7-dimethyl-4-[[(2R,4S)-4-(2-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
0.1
6,7-dimethyl-4-[[(2R,4S)-4-(6-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
value above
0.00132
6-hydroxy-N-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenyl)hexanamide
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.00532
6-oxo-6-(3-(5-p-tolyl-1,3,4-oxadiazol-2-yl)phenylamino)hexanoic acid
Homo sapiens
-
pH 7.5, temperature not specified in the publication
0.05
7-amino-3-(2-carboxyethyl)-1H-indole-2-carboxylic acid
Homo sapiens
above, pH 7.5, 37°C, recombinant His-tagged enzyme
3.1
alpha-ketoglutarate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.055
D-fructose 1,6-bisphosphate
Pelophylax lessonae
-
pH 7.5, 25°C
0.00062 - 0.0105
D-fructose 2,6-bisphosphate
0.002
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
0.004 - 0.02
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
0.0042 - 0.02
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
0.007 - 0.02
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
0.005 - 0.02
diethyl [5-(4-amino-1-benzyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
0.00225 - 0.04
diethyl [5-(4-amino-1-ethyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
0.006 - 0.02
diethyl [5-(4-amino-1-methyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
0.0011 - 0.002
diethyl [5-(4-amino-1-propyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
0.0015 - 0.004
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.00185 - 0.02
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.0095 - 0.02
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.0025 - 0.02
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.0008 - 0.002
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.00325 - 0.02
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.002 - 0.0025
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.0015 - 0.002
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.0008 - 0.2
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
0.0068
ethyl (2S,6S)-4-[[(6,7-dimethyl-8H-indeno[1,2-d][1,3]thiazol-4-yl)oxy]methyl]-2,6-dimethyl-7-oxo-8-oxa-3,5-diaza-4-phosphadecan-1-oate 4-oxide
Hominoidea
-
-
0.0119
ethyl 3,3,3-trifluoro-2-hydroxy-2-(1-methyl-1H-indol-3-yl)propanoate
Mus musculus
-
pH 7.5, 37°C
0.0048
ethyl 3-(3,5-dimethyl-1H-pyrrol-2-yl)-4,4,4-trifluoro-3-hydroxybutanoate
Mus musculus
-
pH 7.5, 37°C
0.000044
MB05032
Homo sapiens
pH and temperature not specified in the publication
-
0.019
N'-[(E)-(6-ethyl-4-oxo-4H-chromen-3-yl)methylidene]-3,4-dihydroxybenzohydrazide
Synechocystis sp.
pH 7.5, temperature not specified in the publication
0.0141
N'-[(E)-(6-tert-butyl-4-oxo-4H-chromen-3-yl)methylidene]-3,4-dihydroxybenzohydrazide
Synechocystis sp.
pH 7.5, temperature not specified in the publication
0.318 - 2.5
N,4-diphenylthiazol-2-amine
0.0026
N,N'-bis(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)pentane-1,5-diamine
Homo sapiens
-
uncompetitive
0.0031
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)hexan-1,6-diamine
Oryctolagus cuniculus
-
37°C
0.0295
N,N'-bis-(6,7-diethoxy-2,3-dihydro-1H-cyclopenta[b]quinolin-9-yl)propan-1,3-diamine
Oryctolagus cuniculus
-
37°C
0.0019
N-(5-bromo-1,3-benzoxazol-2-yl)-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
-
0.0094
N-(5-chloro-1,3-benzoxazol-2-yl)-1-methyl-1H-imidazole-4-sulfonamide
Homo sapiens
-
-
0.023
N-(5-chloro-1,3-benzoxazol-2-yl)-2-(1H-imidazol-1-yl)benzenesulfonamide
Homo sapiens
-
-
0.006
N-(5-chloro-1,3-benzoxazol-2-yl)-2-cyanobenzenesulfonamide
Homo sapiens
-
-
0.0018
N-(5-chloro-1,3-benzoxazol-2-yl)-3-nitrobenzenesulfonamide
Homo sapiens
-
-
0.0067
N-(5-chloro-1,3-benzoxazol-2-yl)-4-(3-furyl)benzenesulfonamide
Homo sapiens
-
-
0.0078
N-(5-chloro-1,3-benzoxazol-2-yl)-4-(trifluoromethoxy)benzenesulfonamide
Homo sapiens
-
-
0.0028
N-(5-chloro-1,3-benzoxazol-2-yl)-4-fluorobenzenesulfonamide
Homo sapiens
-
-
0.0062
N-(5-chloro-1,3-benzoxazol-2-yl)-4-methylbenzenesulfonamide
Homo sapiens
-
-
0.0034
N-(5-chloro-1,3-benzoxazol-2-yl)anthracene-2-sulfonamide
Homo sapiens
-
-
0.0077
N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.0038
N-(5-chloro-1,3-benzoxazol-2-yl)biphenyl-2-sulfonamide
Homo sapiens
-
-
0.0098
N-(5-chloro-1,3-benzoxazol-2-yl)biphenyl-3-sulfonamide
Homo sapiens
-
-
0.004
N-(5-chloro-1,3-benzoxazol-2-yl)biphenyl-4-sulfonamide
Homo sapiens
-
-
0.0025
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfonamide
0.013
N-(5-chloro-1,3-benzoxazol-2-yl)thiophene-2-sulfonamide
Homo sapiens
-
-
0.032
N-(5-tert-butyl-1,3-benzoxazol-2-yl)-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
-
0.00851
N-(6,7-diethoxy-9-[3-(2-methylthiazol-4-yl)phenylamino]-2,3-dihydro-1H-cyclopenta[b]quinolin-1-yl)-acetamide
Oryctolagus cuniculus
-
37°C
0.0002 - 0.0037
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.00008 - 0.001
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.00033 - 0.0058
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-chlorobenzenesulfonamide
0.00013 - 0.0015
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.0004 - 0.03
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.00033 - 0.0033
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
0.00014 - 0.0017
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.00035 - 0.005
N-[(6-bromo-1H-indol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
0.00082 - 0.008
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.012
N-[4-[[(5-chloro-1,3-benzoxazol-2-yl)amino]sulfonyl]phenyl]butanamide
Homo sapiens
-
-
0.00057
N-[6-(4-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
non-competitive
0.00057
N-[7-(3-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
-
0.0013
N-[7-(4-aminophenyl)-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
-
0.0026
N-[7-[3-(aminomethyl)phenyl]-5-methoxy-1,3-benzoxazol-2-yl]-2,5-dichlorobenzenesulfonamide
Homo sapiens
-
-
0.0018 - 0.009
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.00076 - 0.006
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.00042 - 0.004
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide
0.0006 - 0.0035
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
0.0119
N4-(3-Bromo-phenyl)-7-chloro-quinazoline-4,6-diamine
Homo sapiens
-
IC50: 0.0119 mM
0.000047
[(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)(difluoro)methyl]phosphonic acid
Homo sapiens
-
0.00084
[(2-amino-4,5-dihydronaphtho[1,2-d][1,3]thiazol-8-yl)methyl]phosphonic acid
Homo sapiens
-
0.012
[(2R,3S,4R,5R)-5-[4-(aminocarbonyl)-1H-imidazol-1-yl]-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen phosphate
Homo sapiens
-
-
0.5
[2-[(6-amino-8,9-dihydro-7H-purin-8-yl)amino]ethyl]phosphonate
Homo sapiens
-
0.097
[2-[[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]amino]ethyl]phosphonate
Homo sapiens
-
0.026
[3-[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]propyl]phosphonate
Homo sapiens
-
0.005
[5-(1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Homo sapiens
-
-
0.00045 - 0.013
[5-(2-amino-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
0.00012 - 0.002
[5-(2-amino-5-isobutyl-1,3-oxazol-4-yl)-2-furyl]phosphonic acid
0.000016
[5-(2-amino-5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Homo sapiens
-
non-competitive
0.005
[5-(2-amino-5-isobutyl-1H-imidazol-4-yl)-2-furyl]phosphonic acid
Homo sapiens
-
-
0.000014 - 0.0005
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
0.000014
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00003
[5-(2-amino-5-propyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Homo sapiens
-
-
0.01
[5-(2-amino-5-propyl-1,3-thiazol-4-yl)thiophen-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0016
[5-(4-amino-1-tert-butyl-2,3-dihydro-1H-benzimidazol-2-yl)-2-furyl]phosphonate
Homo sapiens
-
0.00009
[5-(4-amino-1-tert-butyl-7-ethyl-5-fluoro-2,3-dihydro-1H-benzimidazol-2-yl)-2-furyl]phosphonate
Homo sapiens
-
0.000055 - 0.00218
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid
0.0005 - 0.0035
[5-(5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
0.000042 - 0.0016
[5-(6-amino-3-phenylpyridin-2-yl)-2-furyl]phosphonic acid
0.0022
[5-(6-amino-9-tert-butyl-8,9-dihydro-7H-purin-8-yl)-2-furyl]phosphonate
Homo sapiens
-
0.000039 - 0.00015
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid
0.000001 - 0.000025
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
0.000014
[5-[2-amino-5-(ethoxycarbonyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.000016
[5-[2-amino-5-(propylsulfanyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00015 - 0.00085
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.001 - 0.002
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00045 - 0.002
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0004 - 0.002
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.01
[5-[4-amino-5-bromo-6,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0002 - 0.002
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0025 - 0.02
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0001 - 0.00225
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00009 - 0.0009
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0001 - 0.00065
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00085 - 0.00215
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00008 - 0.00045
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0001 - 0.0021
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00018 - 0.0013
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0005 - 0.02
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0007 - 0.02
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.000225 - 0.002
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00021 - 0.0016
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00009 - 0.002
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00007 - 0.0005
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0004 - 0.002
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00013 - 0.00209
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.0009
[5-[4-amino-7-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0001 - 0.002
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00006 - 0.00035
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00028 - 0.0009
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.000055 - 0.00055
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
0.00056
[5-[5-(2-methylpropyl)-2-phenyl-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0011
[5-[6-amino-9-(2,2-dimethylpropyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
Homo sapiens
-
0.0012
[5-[6-amino-9-(2-cyclohexylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
Homo sapiens
-
0.005 - 0.015
[5-[6-amino-9-(2-phenylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
0.00029
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0045
(2E)-3-(5-bromo-4-hydroxy-2-methoxyphenyl)-1-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-en-1-one
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.000055
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0004
(5-[4-amino-7-[3-(dimethylamino)propyl]-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl)phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0034
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide

Homo sapiens
-
non-competitive
0.0034
2,5-dichloro-N-(5-chloro-1,3-benzoxazol-2-yl)benzenesulfonamide
Homo sapiens
-
-
0.016
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole

Homo sapiens
-
-
0.061
2-amino-5-isobutyl-4-[2-(5-phosphono)furanyl]thiazole
Rattus norvegicus
-
-
0.00052
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0073
2-[3-methyl-5-([[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)thiophen-2-yl]ethyl acetate
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00067
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0035
2-[5-([[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]sulfamoyl)-3-methylthiophen-2-yl]ethyl acetate
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.0024
3-(2-carboxyethyl)-4-(2-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid

Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0024
3-(2-carboxyethyl)-4-(2-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00527
3-(2-carboxyethyl)-4-(3-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid

Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00527
3-(2-carboxyethyl)-4-(3-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00522
3-(2-carboxyethyl)-4-(3-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid

Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00522
3-(2-carboxyethyl)-4-(3-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0024
3-(2-carboxyethyl)-4-(4-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid

Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0024
3-(2-carboxyethyl)-4-(4-fluorophenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0018
3-(2-carboxyethyl)-4-(4-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid

Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0018
3-(2-carboxyethyl)-4-(4-methoxyphenyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00088
3-(2-carboxyethyl)-4-chloro-7-nitro-1H-indole-2-carboxylic acid

Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00088
3-(2-carboxyethyl)-4-chloro-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00276
3-(2-carboxyethyl)-4-ethyl-7-nitro-1H-indole-2-carboxylic acid

Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00276
3-(2-carboxyethyl)-4-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00207
3-(2-carboxyethyl)-5-chloro-7-nitro-1H-indole-2-carboxylic acid

Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00207
3-(2-carboxyethyl)-5-chloro-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00517
3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid

Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00517
3-(2-carboxyethyl)-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0011
3-(2-carboxyethyl)-7-nitro-4-(3-nitrophenyl)-1H-indole-2-carboxylic acid

Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0011
3-(2-carboxyethyl)-7-nitro-4-(3-nitrophenyl)-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.002
3-(2-carboxyethyl)-7-nitro-4-(4-nitrophenyl)-1H-indole-2-carboxylic acid

Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.002
3-(2-carboxyethyl)-7-nitro-4-(4-nitrophenyl)-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.0014
3-(2-carboxyethyl)-7-nitro-4-phenyl-1H-indole-2-carboxylic acid

Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.0014
3-(2-carboxyethyl)-7-nitro-4-phenyl-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00643
3-(2-carboxyethyl)-7-nitro-5-phenyl-1H-indole-2-carboxylic acid

Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme
0.00643
3-(2-carboxyethyl)-7-nitro-5-phenyl-1H-indole-2-carboxylic acid
Homo sapiens
37°C, pH 7.5
0.00195
3-(3-amino-3-oxopropyl)-5-ethyl-7-nitro-1H-indole-2-carboxylic acid

Homo sapiens
pH and temperature not specified in the publication
0.00304
3-(3-amino-3-oxopropyl)-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.00594
3-(3-amino-3-oxopropyl)-5-ethyl-7-nitro-1H-indole-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.00064
3-chloro-N-[(3,5-dichlorophenyl)carbamoyl]benzenesulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.012
3-chloro-N-[(3,5-dichlorophenyl)carbamoyl]benzenesulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00035
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.004
5-(2-hydroxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00017
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0016
5-(2-methoxyethyl)-4-methyl-N-([6-[(methylcarbamoyl)amino]-4-(methylsulfanyl)pyridin-2-yl]carbamoyl)thiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.0017
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0083
5-(2-methoxyethyl)-4-methyl-N-[[4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00053
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.007
5-(2-methoxyethyl)-4-methyl-N-[[6-methyl-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]thiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00022
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0026
5-(2-methoxyethyl)-N-([4-methoxy-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00042
5-ethyl-7-nitro-3-[3-oxo-3-[(thiophene-2-sulfonyl)amino]propyl]-1H-indole-2-carboxylic acid

Homo sapiens
pH and temperature not specified in the publication
0.0005
5-ethyl-7-nitro-3-[3-oxo-3-[(thiophene-2-sulfonyl)amino]propyl]-1H-indole-2-carboxylic acid
Homo sapiens
pH and temperature not specified in the publication
0.004
6,7-dimethyl-4-[[(2R,4S)-4-(2-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole

Hominoidea
-
shows weak CYP3A4 inhibitor potency
0.011
6,7-dimethyl-4-[[(2R,4S)-4-(2-methylpyridin-3-yl)-2-oxido-1,3,2-dioxaphosphinan-2-yl]methoxy]-8H-indeno[1,2-d][1,3]thiazole
Hominoidea
-
-
0.0083
ADP

Trachemys scripta elegans
-
enzyme from anoxic liver, pH 7.2, 22°C
0.0118
ADP
Trachemys scripta elegans
-
enzyme from healthy liver, pH 7.2, 22°C
0.00014
AMP

Homo sapiens
-
mutant DELTA3
0.00016
AMP
Oryctolagus cuniculus
-
native rabbit muscle FBPase
0.00016
AMP
Homo sapiens
-
wild-type enzyme
0.00016
AMP
Homo sapiens
-
wild-type muscle enzyme
0.00019
AMP
Homo sapiens
wild-type, pH 7.4, 25°C, Hill-coefficient 1.34
0.0002
AMP
Pelophylax lessonae
-
pH 7.5, 25°C
0.00021
AMP
Oryctolagus cuniculus
-
mutant E69Q of rabbit muscle FBPase
0.00033
AMP
Homo sapiens
-
mutant DELTA4
0.00081
AMP
Homo sapiens
-
mutant DELTA5
0.001
AMP
Homo sapiens
-
-
0.00139
AMP
Homo sapiens
-
mutant DELTA6
0.00197
AMP
Homo sapiens
-
mutant DELTA10
0.0022
AMP
Escherichia coli
22°C, pH 7.5, the enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+
0.0025 - 0.0035
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant Y164A
0.0026
AMP
Homo sapiens
pH and temperature not specified in the publication
0.0031
AMP
Sus scrofa
30°C, pH 7.5, mutant enzyme F89W
0.0033
AMP
Homo sapiens
pH and temperature not specified in the publication
0.0034
AMP
Sus scrofa
30°C, pH 7.5, mutant enzyme F219W
0.0035 - 0.0039
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant M177A
0.0036
AMP
Trachemys scripta elegans
-
enzyme from anoxic liver, pH 7.2, 22°C
0.00365
AMP
Homo sapiens
mutant Q32R, pH 7.4, 25°C, Hill-coefficient 0.59
0.00393
AMP
Homo sapiens
-
mutant DELTA7
0.00425
AMP
Homo sapiens
-
mutant DELTA8
0.0046
AMP
Sus scrofa
30°C, pH 7.5, mutant enzyme F232W
0.00506
AMP
Homo sapiens
-
wild-type liver enzyme
0.0057
AMP
Sus scrofa
30°C, pH 7.5, mutant enzyme F16W
0.0061
AMP
Trachemys scripta elegans
-
enzyme from healthy liver, pH 7.2, 22°C
0.00695
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant L73A
0.0071
AMP
Sus scrofa
30°C, pH 7.5, recombinant wild-type enzyme
0.0072
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant M248D
0.00735
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant L56A
0.0075
AMP
Sus scrofa
pH 7.5, 37°C, recombinant wild-type enzyme
0.01
AMP
Lathyrus oleraceus
-
wild-type
0.0102
AMP
Sus scrofa
30°C, pH 7.5, nonrecombinant enzyme
0.015
AMP
Synechocystis sp.
mutant Y131A, pH 8.0, 28°C
0.0181
AMP
Escherichia coli
22°C, pH 7.5, assay is initiated by the addition of enzyme
0.02
AMP
Rattus norvegicus
-
-
0.02
AMP
Escherichia coli
22°C, pH 7.5, assay mixtures contains 1 mM phosphoenolpyruvate. Enzyme is incubated for 1 h in assay mixture. The reaction is initiated by the addition of Mg2+
0.0214
AMP
Synechocystis sp.
mutant R176A, pH 8.0, 28°C
0.027
AMP
Synechocystis sp.
mutant R178A, pH 8.0, 28°C
0.028
AMP
Synechocystis sp.
mutant K29A, pH 8.0, 28°C
0.034
AMP
Synechocystis sp.
wild-type, pH 8.0, 28°C
0.0486 - 0.0553
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant Y113A
0.0523 - 0.0685
AMP
Sus scrofa
pH 7.5, 37°C, recombinant mutant K112A
0.21
AMP
Synechocystis sp.
mutant N213A, pH 8.0, 28°C
0.225
AMP
Synechocystis sp.
mutant D200A, pH 8.0, 28°C
1.23
AMP
Synechocystis sp.
mutant D198H, pH 8.0, 28°C
1.241
AMP
Synechocystis sp.
mutant T102A, pH 8.0, 28°C
2.099
AMP
Synechocystis sp.
mutant K134A, pH 8.0, 28°C
5.81
AMP
Lathyrus oleraceus
-
mutant K115Q
15.96
AMP
Lathyrus oleraceus
-
mutant Y116F
0.75
ATP

Pyrobaculum calidifontis
recombinant enzyme, pH 8.0, 60°C
0.75
ATP
Pyrobaculum calidifontis
pH 8.0, 25°C
0.00074
Ca2+

Oryctolagus cuniculus
-
native rabbit muscle FBPase
0.00077
Ca2+
Homo sapiens
-
mutant DELTA4
0.00091
Ca2+
Homo sapiens
-
wild-type muscle enzyme
0.00099
Ca2+
Homo sapiens
-
mutant DELTA3
0.00131
Ca2+
Homo sapiens
-
mutant DELTA6
0.00137
Ca2+
Homo sapiens
-
mutant DELTA5
0.00218
Ca2+
Homo sapiens
-
mutant DELTA7
0.00689
Ca2+
Homo sapiens
-
wild-type liver enzyme, biphasic inhibition by Ca2+
0.00731
Ca2+
Homo sapiens
-
mutant DELTA10
0.091
Ca2+
Pelophylax lessonae
-
pH 7.5, 25°C
0.934
Ca2+
Homo sapiens
-
wild-type liver enzyme, biphasic inhibition by Ca2+
2
citrate

Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
2
citrate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.00062 - 0.00075
D-fructose 2,6-bisphosphate

Sus scrofa
pH 7.5, 37°C, recombinant mutant M177A
0.0007
D-fructose 2,6-bisphosphate
Sus scrofa
30°C, pH 7.5, mutant enzyme F16W
0.0007
D-fructose 2,6-bisphosphate
Sus scrofa
30°C, pH 7.5, mutant enzyme F89W
0.0009
D-fructose 2,6-bisphosphate
Sus scrofa
30°C, pH 7.5, nonrecombinant enzyme
0.00095
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant mutant Y164A
0.001
D-fructose 2,6-bisphosphate
Sus scrofa
30°C, pH 7.5, recombinant wild-type enzyme
0.0015
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant mutant K112A
0.0015
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant wild-type enzyme
0.0016
D-fructose 2,6-bisphosphate
Sus scrofa
30°C, pH 7.5, mutant enzyme F219W
0.0017 - 0.0018
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant mutant Y113A
0.0019
D-fructose 2,6-bisphosphate
Sus scrofa
30°C, pH 7.5, mutant enzyme F232W
0.00725
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant mutant L73A
0.0075
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant mutant L56A
0.0105
D-fructose 2,6-bisphosphate
Sus scrofa
pH 7.5, 37°C, recombinant mutant M248D
0.002
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate

Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.002
diethyl (5-[4-amino-1-[(1R,2R)-bicyclo[2.2.1]hept-2-ylamino]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.004
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl (5-[4-amino-1-[3-(thiophen-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0042
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl (5-[4-amino-1-[4-(furan-3-ylmethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.007
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl (5-[4-amino-1-[4-(trifluoromethyl)benzyl]-1H-benzimidazol-2-yl]furan-2-yl)phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.005
diethyl [5-(4-amino-1-benzyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl [5-(4-amino-1-benzyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00225
diethyl [5-(4-amino-1-ethyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.04
diethyl [5-(4-amino-1-ethyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.006
diethyl [5-(4-amino-1-methyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl [5-(4-amino-1-methyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0011
diethyl [5-(4-amino-1-propyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
diethyl [5-(4-amino-1-propyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0015
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.004
diethyl [5-[4-amino-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00185
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl [5-[4-amino-1-(3-hydroxybenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0095
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl [5-[4-amino-1-(4-tert-butylbenzyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0025
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl [5-[4-amino-1-(biphenyl-4-ylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0008
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
diethyl [5-[4-amino-1-(cyclobutylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00325
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
diethyl [5-[4-amino-1-(cycloheptylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.002
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0025
diethyl [5-[4-amino-1-(cyclohexylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0015
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
diethyl [5-[4-amino-1-(cyclopentylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0008
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.2
diethyl [5-[4-amino-1-(cyclopropylmethyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonate
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.2
Li+

Mycobacterium tuberculosis
-
pH 7.7, 30°C
0.25
Li+
Mycobacterium tuberculosis
pH 8.0, 22°C, recombinant wild-type enzyme
0.28
Li+
Mycobacterium tuberculosis
pH 8.0, 22°C, recombinant mutant T84S
290
Li+
Archaeoglobus fulgidus
pH 8.0, 85°C
15.8
LiCl

Escherichia coli
-
70
LiCl
Escherichia coli
-
3.3
malate

Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
3.3
malate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
3.2
malonate

Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
3.2
malonate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.318
N,4-diphenylthiazol-2-amine

Sus scrofa
-
2.5
N,4-diphenylthiazol-2-amine
Sus scrofa
-
0.0025
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfonamide

Homo sapiens
-
non-competitive
0.0025
N-(5-chloro-1,3-benzoxazol-2-yl)naphthalene-2-sulfonamide
Homo sapiens
-
-
0.0002
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0037
N-([4-bromo-6-[(2,2,2-trifluoroethyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00008
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.001
N-([4-bromo-6-[(methylcarbamoyl)amino]pyridin-2-yl]carbamoyl)-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00033
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-chlorobenzenesulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0058
N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-3-chlorobenzenesulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00013
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0015
N-[(6-amino-4-bromopyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.0004
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.03
N-[(6-amino-4-methoxypyridin-2-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00033
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0033
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00014
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0017
N-[(6-bromo-1H-indazol-4-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00035
N-[(6-bromo-1H-indol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.005
N-[(6-bromo-1H-indol-4-yl)carbamoyl]-3-chlorobenzenesulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00082
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.008
N-[(7-bromoimidazo[1,2-a]pyridin-5-yl)carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.0018
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.009
N-[[6-amino-4-(methylsulfanyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00076
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.006
N-[[6-amino-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.00042
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.004
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-hydroxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
0.0006
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0035
N-[[6-amino-5-fluoro-4-(trifluoromethyl)pyridin-2-yl]carbamoyl]-5-(2-methoxyethyl)-4-methylthiophene-2-sulfonamide
Mus musculus
-
pH not specified in the publication, temperature not specified in the publication
6.4
oxaloacetate

Mycobacterium tuberculosis
versus MtFBPaseII, pH and temperature not specified in the publication
6.4
oxaloacetate
Mycobacterium tuberculosis
pH and temperature not specified in the publication
1.2
phosphate

Escherichia coli
-
3
phosphate
Escherichia coli
-
0.00045
[5-(2-amino-1,3-thiazol-4-yl)-2-furyl]phosphonic acid

Homo sapiens
-
-
0.013
[5-(2-amino-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Rattus norvegicus
-
-
0.00012
[5-(2-amino-5-isobutyl-1,3-oxazol-4-yl)-2-furyl]phosphonic acid

Homo sapiens
-
-
0.002
[5-(2-amino-5-isobutyl-1,3-oxazol-4-yl)-2-furyl]phosphonic acid
Rattus norvegicus
-
-
0.000014
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid

Homo sapiens
-
-
0.0005
[5-(2-amino-5-phenyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Rattus norvegicus
-
-
0.000055
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00218
[5-(4-amino-5-bromo-1-cyclopropyl-1H-benzimidazol-2-yl)furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0005
[5-(5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid

Homo sapiens
-
-
0.0035
[5-(5-isobutyl-1,3-thiazol-4-yl)-2-furyl]phosphonic acid
Rattus norvegicus
-
-
0.000042
[5-(6-amino-3-phenylpyridin-2-yl)-2-furyl]phosphonic acid

Homo sapiens
-
-
0.0016
[5-(6-amino-3-phenylpyridin-2-yl)-2-furyl]phosphonic acid
Rattus norvegicus
-
-
0.000039
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
-
0.00015
[5-[2-amino-5-(2-methylpropyl)-1,3-selenazol-4-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
-
0.000001
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
0.000025
[5-[2-amino-5-(2-methylpropyl)-1,3-thiazol-4-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00015
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00085
[5-[4-amino-1-(2-ethylbutyl)-5-fluoro-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.001
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-5,7-dibromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00045
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-5,7-dichloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0004
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-5-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0002
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-5-chloro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0025
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
[5-[4-amino-5-ethyl-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0001
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00225
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00009
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0009
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-phenyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0001
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00065
[5-[4-amino-5-fluoro-1-(2-methylpropyl)-7-propyl-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00085
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00215
[5-[4-amino-5-fluoro-1-(pentan-3-yl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00008
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00045
[5-[4-amino-5-fluoro-7-(2-methoxyethyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0001
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0021
[5-[4-amino-5-fluoro-7-(3-methylbutyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00018
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0013
[5-[4-amino-5-fluoro-7-(4-fluorophenyl)-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0005
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
[5-[4-amino-5-hydroxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0007
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.003
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.02
[5-[4-amino-5-methoxy-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000225
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-6-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00021
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0016
[5-[4-amino-7-(3,3-dimethylbutyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00009
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-7-(4-chlorophenyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00007
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0005
[5-[4-amino-7-(6-chlorohexyl)-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0004
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-7-bromo-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00013
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00209
[5-[4-amino-7-bromo-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0001
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.002
[5-[4-amino-7-chloro-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00006
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00035
[5-[4-amino-7-cyclopropyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.00028
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0009
[5-[4-amino-7-ethenyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.000055
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid

Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00055
[5-[4-amino-7-ethyl-5-fluoro-1-(2-methylpropyl)-1H-benzimidazol-2-yl]furan-2-yl]phosphonic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.005
[5-[6-amino-9-(2-phenylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate

Homo sapiens
-
0.015
[5-[6-amino-9-(2-phenylethyl)-8,9-dihydro-7H-purin-8-yl]-2-furyl]phosphonate
Homo sapiens
-
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drug target

potential drug target for type 2 diabetes
drug target
the enzyme (FBPase-1) is considered to be a new target for the control of diabetes
drug target
potential drug target against Leishmania parasites
drug target
-
the enzyme (FBPase-1) is considered to be a new target for the control of diabetes
-
evolution

-
virtually all archaeal groups as well as the deeply branching bacterial lineages contain the bifunctional D-fructose 1,6-bisphosphate aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity. This enzyme is missing in most other bacteria and in eukaryota. Phylogenetic analysis, overview
evolution
-
virtually all archaeal groups as well as the deeply branching bacterial lineages contain the bifunctional D-fructose 1,6-bisphosphate aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity. This enzyme is missing in most other bacteria and in eukaryota. Phylogenetic analysis, overview
evolution
-
virtually all archaeal groups as well as the deeply branching bacterial lineages contain the bifunctional D-fructose 1,6-bisphosphate aldolase/phosphatase with both FBP aldolase and FBP phosphatase activity. This enzyme is missing inmost other Bacteria and in Eukaryota. Phylogenetic analysis, overview
evolution
YK23 is a member of the histidine phosphatase (phosphoglyceromutase) superfamily. YK23 represents the first family of metal-independent FBPases and a second FBPase family in eukaryotes
evolution
the amino acid sequence of EgFBPaseIII shows low identity (35%) with EgFBPaseI and II, while it shows higher identity of 51-52% with other cytosolic FBPases from plants. EgFBPaseIII has an additional sequence at the N-terminus that other cytosolic FBPases do not possess, this N-terminal region contains no signal peptide or known domain architecture
evolution
structures of Leishmania fructose-1,6-bisphosphatase (FBPase) reveal species-specific differences in the mechanism of allosteric inhibition of FBPases
evolution
FBPases are homotetrameric enzymes with three different isoforms present in plants, two in chloroplasts (cFBP1 and cFBP2) and one in the cytosol (cyFBP). Only cFBP1 needs to be redox activated in order to be fully active, whilst cFBP2 is not redox regulated and, despite its activity, resists higher oxidant concentrations than cFBP1
evolution
structural comparison of class I versus class II FBPases
evolution
the FBP/SBPase found in Thermosynechococcus elongatus is a type II FBPase, a member of the larger Li+-sensitive phosphatase superfamily. It shares 80% sequence identity with the Synechocystis sp. PCC 6803 FBP/SBPase
evolution
chloroplastic FBPase isoenzymes are widely distributed in photosynthetic organisms, i.e. bacteria, blue-green and green algae, lichens, and plants
evolution
the archaeal enzyme belongs to the class V of fructose-1, 6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases
evolution
-
invertebrate genomes contain a single fbp locus. In vertebrates, there are two distinct genes, fbp1 and fbp2, encoding two FBPase isozymes. Liver FBPase (FBP1), the protein product of the fbp1 gene, is expressed mainly in gluconeogenic organs, while muscle FBPase (FBP2), encoded by gene fbp2, is widely expressed in vertebrate cells, not only in glyconeogenic ones (e.g. striated muscle fibres) but also in cells such as neurons which are not thought to synthesize glycogen from carbohydrate precursors. FBP2 is also expressed in cells predominantly producing the liver isozyme, e.g. in the liver itself. In vertebrates, the two FBPase isozymes evolved to play distinct cellular roles
evolution
-
invertebrate genomes contain a single fbp locus. In vertebrates, there are two distinct genes, fbp1 and fbp2, encoding two FBPase isozymes. Liver FBPase (FBP1), the protein product of the fbp1 gene, is expressed mainly in gluconeogenic organs, while muscle FBPase (FBP2), encoded by fbp2, is widely expressed in vertebrate cells, not only in glyconeogenic ones (e.g. striated muscle fibres) but also in cells such as neurons which are not thought to synthesize glycogen from carbohydrate precursors. FBP2 is also expressed in cells predominantly producing the liver isozyme, e.g. in the liver itself. In vertebrates, the two FBPase isozymes evolved to play distinct cellular roles
evolution
-
the amino acid sequence of EgFBPaseIII shows low identity (35%) with EgFBPaseI and II, while it shows higher identity of 51-52% with other cytosolic FBPases from plants. EgFBPaseIII has an additional sequence at the N-terminus that other cytosolic FBPases do not possess, this N-terminal region contains no signal peptide or known domain architecture
-
evolution
-
chloroplastic FBPase isoenzymes are widely distributed in photosynthetic organisms, i.e. bacteria, blue-green and green algae, lichens, and plants
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evolution
-
the archaeal enzyme belongs to the class V of fructose-1, 6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases
-
evolution
-
the archaeal enzyme belongs to the class V of fructose-1, 6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases
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evolution
-
structural comparison of class I versus class II FBPases
-
evolution
-
the archaeal enzyme belongs to the class V of fructose-1, 6-bisphosphatases. Gene expression of class V FBPase is regulated at the transcription level. The substrate binding residues, including Tyr229, Lys232, and Tyr358, and the residues involved in metal binding, including Asp11, His18, Asp52, Asp53, Gln95, Asp132, Asp233, and Glu357 are completely conserved in all the archaeal FBPases
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malfunction

genetic silencing of enzyme fructose-1,6-bisphosphatase (FBP1) reduces aerobic glycolysis and the malignant potential of breast cancer cells. FBP1 down-regulation enhances the activity of Wnt/b-Catenin pathway and increases the level of its downstream targets, including c-Myc and MMP7
malfunction
no significant differences are observed in the production of paramylon in transiently suppressed EgFBPaseIII gene expression cells by RNAi (KD-EgFBPaseIII), but FBPase activity is markedly decreased in KD-EgFBPaseIII cells. Growth of KD-EgFBPaseIII cells is slightly increased compared to control cells
malfunction
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
malfunction
homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type MtFBPase by Ser84 results in subtle alterations of the position and orientation that reduce the catalytic efficiency
malfunction
EgFBPaseI gene suppression by gene silencing markedly decreases photosynthetic activity and inhibits cell growth
malfunction
two significant mutations in the coding region of the FBPase gene in patients with hypoglycemia link the AMP-binding site to the active site of the enzyme. Individuals with FBPase deficiency exhibit hypoglycemia and metabolic acidosis due to impaired gluconeogenesis. In rare cases, hypoglycemia, an autosomal recessive disorder characterized by insufficient blood glucose levels, is genetically linked to FBPase deficiency in clinical studies. The M177 and Y164 interfacial residues are positioned between the AMP-binding site and active sites and are mutated in humans with hypoglycemia
malfunction
-
fluoroquinolones suppress gluconeogenesis by inhibiting fructose 1,6-bisphosphatase in primary monkey hepatocytes
malfunction
-
FBP1 deficiency is a rare inborn metabolic error, that causes severe hypoglycemia, lactic acidosis, seizures, hepatomegaly, hyperlipidemia, hepatosteatosis and liver damage in carbohydrate starved, but not in fed infants. Inborn human FBP1 deficiency does not cause hypoglycemia unless accompanied by fasting or starvation, which also trigger paradoxical hepatomegaly, hepatosteatosis, and hyperlipidemia. Hepatomegaly and elevated hepatic lipogenesis also affect non-starved older FBP1-deficient individuals. Enhanced by fasting and weakened by elevated insulin, FBP1:PP2A-C:ALDOB:AKT complex formation, which is disrupted by human FBP1 deficiency mutations or a C-terminal FBP1 truncation, prevents insulin-triggered liver pathologies and maintains lipid and glucose homeostasis. Conversely, an FBP1-derived complex disrupting peptide reverses diet-induced insulin resistance. FBP1-deficient individuals exhibit mild hereditary fructose intolerance (HFI), a metabolic disorder associated with ALDOB deficiency, which blocks F1,6-P2 breakdown. ALDOB deficiency also causes hepatomegaly, hepatosteatosis and liver damage. This phenotypic overlap suggested that FBP1 may regulate AKT activity through its interaction with ALDOB
malfunction
hepatocyte FBP1-ablated mice exhibit identical fasting-conditional pathologies along with AKT hyperactivation, whose inhibition reverses hepatomegaly, hepatosteatosis and hyperlipidemia but not hypoglycemia. Fasting-mediated AKT hyperactivation is insulin-dependent. Independently of its catalytic activity, FBP1 prevents insulin hyperresponsiveness by forming a stable complex with AKT, PP2A-C and aldolase-B (ALDOB) which specifically accelerates AKT dephosphorylation. Fasted Fbp1DELTAHep mice exhibit enhanced AKT-mTOR signaling and de novo lipogenesis. Catalytically inactive FBP1 prevents hepatomegaly, steatosis, and hyperlipidemia. Phenotypes of fasted and fed wild-type and mutant mice, detailed overview
malfunction
expression of the gluconeogenic isozyme fructose-1,6-bisphosphatase 2 (FBP2) is silenced in a broad spectrum of sarcoma subtypes, revealing an apparent common metabolic feature shared by diverse STSs. Enforced FBP2 expression inhibits sarcoma cell and tumor growth through two distinct mechanisms. First, cytosolic FBP2 antagonizes elevated glycolysis associated with the Warburg effect, thereby inhibiting sarcoma cell proliferation. Second, nuclear-localized FBP2 restrains mitochondrial biogenesis and respiration in a catalytic activity-independent manner by inhibiting the expression of nuclear respiratory factor and mitochondrial transcription factor A (TFAM). Specifically, nuclear FBP2 colocalizes with the c-Myc transcription factor at the TFAM locus and represses c-Myc-dependent TFAM expression. This unique dual function of FBP2 provides a rationale for its selective suppression in STSs, identifying a potential metabolic vulnerability of this malignancy and possible therapeutic target. Glycolysis and TCA cycle activity are inhibited by FBP2 restoration
malfunction
the expression levels of Tgfb1, Csf1, Csf3 and Kitl are upregulated in the tumors from Fbp1N213K/N213K mice than those from Fbp1+/+ mice. These results suggest that disrupting Fbp1-mediated IkappaBalpha dephosphorylation recruits MDSCs in tumor microenvironment and promotes tumor immune evasion
malfunction
under both feeding and fasting conditions, Fbp2 KO mice showed similar phenotypes regarding energy and glucose metabolism compared to wild-type mice. Fbp2 KO mice are severely intolerant to cold challenge under fasting conditions. Mechanistically, the cold-induced intramuscular conversion of lactate to glycogen (glyconeogenesis) is completely abolished in the KO muscle, which leads to a lack of glycogen source for thermogenesis in Fbp2 KO mice. The cold-intolerant phenotype of KO mice disappears after feeding, and the KO mice are equally as cold tolerant as the wild-type mice and survive during the cold challenge for three weeks. Fbp2 deletion does not alter glucose metabolism during the feeding condition
malfunction
transgenic plants coexpressing cyFBPase and SBPase (TpFS), or expressing single cyFBPase (TpF) or SBPase (TpS) have 1.77, 1.55, 1.23fold cyFBPase and 1.45, 1.12, 1.36fold SBPase activities as compared to the wild-type plants, respectively. Photosynthesis rates of TpF, TpS and TpFS increase 4, 20 and 25% compared with wild-type plants. The SBPase and cyFBPase positively regulate each other and functioned synergistically in transgenic tobacco plants
malfunction
-
during anoxia in liver, the maximal activity of the enzyme is significantly decreased with decreased sensitivity to its substrate fructose-1,6-bisphosphate (FBP) when compared to the control. The anoxic FBPase shows about 1.4fold increased threonine phosphorylation
malfunction
FBPase is associated with a rare, autosomal recessive inherited metabolic disease. The incidence is estimated to be between 1/900000 and 1/350000 in European populations. Disease-associated mutations include frameshifts, deletions, splice donor variants, and missense mutations. Patients suffer from impaired gluconeogenesis and, consequently, hypoglycaemia, ketosis and lactic acidosis. In clear cell renal cell carcinoma (ccRCC, the most common form of kidney cancer), cells lack FBPase activity, due to a chromosomal deletion. Complementation of ccRCC cells with the wild-type FBPase gene inhibits their growth. Thus lack of FBPase activity is necessary for the survival of these cells. Reduced FBPase activity has also been observed in some other forms of cancer cells (e.g. gastric, liver and cervical cancer). This effect is believed to be due to two factors. First, the loss of FBPase activity blocks gluconeogenesis and stimulates glycolysis. Cancer cells typically rely heavily on glycolysis as a source of ATP and glycolytic intermediates, precursors of building blocks for synthetic reactions, even in aerobic conditions (the Warburg effect). Second, FBPase interacts with, and inhibits the activity of, hypoxia-inducible factors (HIFs). This inhibition promotes aerobic metabolism and restrains cell proliferation. Its loss results in a second factor which up-regulates the glycolytic pathway and removes a block on cell proliferation
malfunction
-
the block of the cell cycle progression by withdrawal of serum from a culture medium which results in a quiescent, G0-like cell stage not only stimulates FBP2 export from nuclei to cytoplasm but also significantly reduces the amount of the enzyme simultaneously elevating the level of mRNA for FBP2
malfunction
-
the cells with partially silenced FBP2 expressions are almost 2- and 4-times more viable than, respectively, wild-type cells and cells overexpressing FBP2
malfunction
LTP induction regulates Fbp2 association with neuronal mitochondria and Camk2 and that the Fbp2-Camk2 interaction correlates with Camk2 autophosphorylation. Silencing of Fbp2 expression or simultaneous inhibition and tetramerization of the enzyme with a synthetic effector mimicking the action of physiological inhibitors (NAD+ and AMP) abolishes Camk2 autoactivation and blocks formation of the early phase of LTP and expression of the late phase LTP markers. Astrocyte-derived lactate reduces NAD+/NADH ratio in neurons and thus diminishes the pool of tetrameric and increases the fraction of dimeric Fbp2. The NAD+-level-dependent increase of the Fbp2 dimer/tetramer ratio might be a crucial mechanism in which astrocyte-neuron lactate shuttle stimulates LTP formation. Silencing of Fbp2 expression or inhibition/tetramerization of the enzyme decreases mitochondrial polarity and blocks the LTP formation. The Fbp2 silencing/inhibition also blocks nuclear accumulation of Camk4 and abolishes the expression of LTP late phase markers such as c-Fos and c-Jun. Fbp2 silencing or inhibition/tetramerization significantly decreases neuronal mitochondria polarization and makes it insensitive to LTP induction
malfunction
-
no significant differences are observed in the production of paramylon in transiently suppressed EgFBPaseIII gene expression cells by RNAi (KD-EgFBPaseIII), but FBPase activity is markedly decreased in KD-EgFBPaseIII cells. Growth of KD-EgFBPaseIII cells is slightly increased compared to control cells
-
malfunction
-
EgFBPaseI gene suppression by gene silencing markedly decreases photosynthetic activity and inhibits cell growth
-
malfunction
-
homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type MtFBPase by Ser84 results in subtle alterations of the position and orientation that reduce the catalytic efficiency
-
malfunction
-
LTP induction regulates Fbp2 association with neuronal mitochondria and Camk2 and that the Fbp2-Camk2 interaction correlates with Camk2 autophosphorylation. Silencing of Fbp2 expression or simultaneous inhibition and tetramerization of the enzyme with a synthetic effector mimicking the action of physiological inhibitors (NAD+ and AMP) abolishes Camk2 autoactivation and blocks formation of the early phase of LTP and expression of the late phase LTP markers. Astrocyte-derived lactate reduces NAD+/NADH ratio in neurons and thus diminishes the pool of tetrameric and increases the fraction of dimeric Fbp2. The NAD+-level-dependent increase of the Fbp2 dimer/tetramer ratio might be a crucial mechanism in which astrocyte-neuron lactate shuttle stimulates LTP formation. Silencing of Fbp2 expression or inhibition/tetramerization of the enzyme decreases mitochondrial polarity and blocks the LTP formation. The Fbp2 silencing/inhibition also blocks nuclear accumulation of Camk4 and abolishes the expression of LTP late phase markers such as c-Fos and c-Jun. Fbp2 silencing or inhibition/tetramerization significantly decreases neuronal mitochondria polarization and makes it insensitive to LTP induction
-
malfunction
Picosynechococcus sp. PCC 7002 PR-6
-
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
-
malfunction
-
homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type MtFBPase by Ser84 results in subtle alterations of the position and orientation that reduce the catalytic efficiency
-
malfunction
-
under both feeding and fasting conditions, Fbp2 KO mice showed similar phenotypes regarding energy and glucose metabolism compared to wild-type mice. Fbp2 KO mice are severely intolerant to cold challenge under fasting conditions. Mechanistically, the cold-induced intramuscular conversion of lactate to glycogen (glyconeogenesis) is completely abolished in the KO muscle, which leads to a lack of glycogen source for thermogenesis in Fbp2 KO mice. The cold-intolerant phenotype of KO mice disappears after feeding, and the KO mice are equally as cold tolerant as the wild-type mice and survive during the cold challenge for three weeks. Fbp2 deletion does not alter glucose metabolism during the feeding condition
-
malfunction
Picosynechococcus sp. PCC 7002 ATCC 27264
-
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
-
metabolism

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fructose bisphosphatase is the key enzyme of gluconeogenesis
metabolism
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fructose bisphosphatase is the key enzyme of gluconeogenesis
metabolism
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fructose-1,6-bisphosphatase is a key enzyme in gluconeogenesis
metabolism
-
fructose 1,6-bisphosphatase II is a key gluconeogenic enzyme
metabolism
-
fructose-1,6-bisphosphatase is secreted into the periplasm during prolonged glucose starvation and is internalized into vacuole import and degradation vesicles/endosomes following glucose re-feeding. Fructose-1,6-bisphosphatase does not contain signal sequences required for the classical secretory and endocytic pathways, the secretion and internalization are mediated via the non-classical pathways and involves protein Vps34, which is involved in multiple protein trafficking events
metabolism
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effects of the enzyme activity on the flux balance analyses of Kluyveromyces marxianus grown on glucose and xylose as respective carbon sources (e.g. cofactor balances and sugar uptake fluxes), simulations, detailed overview. Simulation of anaerobic conditions
metabolism
the enzyme is part of the carbohydrate metabolism in the carnivorous fish species. Fructose-1,6-bisphosphatase (FBPase) plays a crucial role in glucose metabolism, together with glucokinase. Feeding with dietary carbohydrates causes no significant differences in FBPase activity and mRNA expression in the glucose as well as dextrin group, while both hepatic glucokinase activity and mRNA expression are highly induced in turbot. The increased hepatic glucokinase activity and gene expression indicates that the first step of glycolysis is activated in turbot by dietary carbohydrates
metabolism
fructose-1,6-bisphosphatase (FBPase) is the key enzyme in the Calvin-Benson cycle (CBC). The enzyme is involved in redox regulation in chloroplasts, model of the redox regulation, overview
metabolism
fructose-1,6-bisphosphatase (FBPase) catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate and is a key enzyme of gluconeogenesis and glyconeogenesis
metabolism
the enzyme fructose 1,6-bisphosphatase takes part in the Calvin cycle, but unlike the situation in higher plants, FBPase probably does not catalyze a rate-limiting step in the Chlamydomonas reinhardtii Calvin cycle, since under photoautotrophic growth conditions and/or with elevated CO2 levels, an elevation in FBPase activity has a negative effect overall on growth rate and biomass production
metabolism
the chloroplastic fructose-1,6-bisphosphatase (FBPase) is a late-limiting enzyme in the Calvin cycle
metabolism
enzyme FBPase is a key rate-controlling enzyme in the gluconeogenic pathway
metabolism
enzyme FBPase is a key rate-controlling enzyme in the gluconeogenic pathway
metabolism
the enzyme (EgFBPaseI) is critical for the Calvin cycle in Euglena chloroplasts in order to maintain normal cell growth under photoautotrophic conditions
metabolism
key enzyme of the gluconeogenic pathway
metabolism
-
simulation study of yeast metabolism, that investigates the complex interplay between the cofactors ATP, NAD+ and NADP+, in particular, how they may affect the possible roles of fructose-1,6-bisphosphatase, the pentose phosphate pathway, glycerol production and the pyruvate dehydrogenase bypass. Using flux balance analysis, it is found that the potential role of fructose-1,6-bisphosphatase is highly dependent on the cofactor specificity of the oxidative pentose phosphate pathway and on the carbon source. The fructose-1,6-bisphosphatase/phosphofructokinase substrate cycle and its regulation probably plays a key role in energy homeostasis, even in yeasts under selected conditions, which could determine phenotype switching
metabolism
metabolic conditions modulate aldolase B and FBPase-1 activity at the cellular level through the regulation of their interaction, suggesting that their association confers a catalytic advantage for both enzymes
metabolism
the enzyme (FBP1) is rate-limiting in gluconeogenes. Its downregulation enhances the activity of Wnt/beta-catenin pathway and increases the level of its downstream targets, including c-Myc and MMP7. Elevated fructose-1,6-bisphosphatase is a critical modulator in breast cancer progression by altering glucose metabolism and the activity of Wnt/beta-Catenin pathway. The enzyme is a tumor suppressor that is frequently down-regulated in cancers, especially breast cancer. Lower FBP1 expression is associated with poor clinical outcome. Up-regulated FBP1 predicts a good prognosis in breast cancer
metabolism
key enzyme in gluconeogenesis and position branch point of carbon partitioning between paramylon and wax ester biosynthesis. The activity of the enzyme (EgFBPaseIII) is not regulated by AMP or reversible redox modulation
metabolism
one of the key enzymes in gluconeogenesis
metabolism
gluconeogenic enzyme
metabolism
-
the increased fructose 1,6-bisphosphatase activity in nodules of RIL115 positively correlates with higher use efficiency of both the rhizobial symbiosis (23%) and P for symbiotic nitrogen fixation (14% calculated as the ratio of N2 fixed per nodule total P content)
metabolism
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase leads to enhanced photosynthesis and global reprogramming of carbon metabolism
metabolism
the enzyme belongs to the Calvin-Benson cycle
metabolism
-
regulatory enzyme in the gluconeogenesis pathway
metabolism
Calvin cycle enzyme
metabolism
essential enzyme for pathogenesis
metabolism
-
the enzyme is important in the gluconeogenesis. Trypanosoma brucei is unique in that most of the glycolytic and gluconeogenic pathways are localized to the peroxisome-like glycosomes
metabolism
liver fructose-1,6-bisphosphatase (FBPase) is a key enzyme in the gluconeogenesis
metabolism
both canonical and noncanonical NF-kappaB pathways play important role in CRC development, FBP1 does not regulate the noncanonical NF-kappaB pathway in vivo. NF-kappaB transcription factor regulates expression of numerous components of the immune system, including innate immune response and the specific immune response
metabolism
FBP1 is the regulatory enzyme of the gluconeogenesis pathway, gluconeogenesis process, overview. The reaction catalyzed by fructose 1,6-bisphosphatase (FBPase) occurs in the cytoplasm, with its intracellular activity regulated by the competitive inhibitor fructose 2,6-bisphoshate and the allosteric inhibitor AMP
metabolism
seduheptoluse-1,7-bisphosphatase (SBPase, EC 3.1.3.37) and cyFBPase positively regulate each other and function synergistically in transgenic tobacco plants. SBPase is at the branch point of the regeneration of ribulose bisphosphate (RuBP) or exportion from the cycle for carbohydrate biosynthesis. Therefore, SBPase is essential for regulating carbon flow in the Calvin cycle. Elevated SBPase and cyFBPase activities promote carbohydrate accumulation and growth
metabolism
-
fructose-1,6-bisphosphatase (FBPase) and phosphofructokinase (PFK) act as rate-limiting enzymes to control the gluconeogenic versus glycolytic pathways, respectively, resulting in the regulation of glucose homeostasis and energy metabolism
metabolism
fructose 1,6-bisphosphatase (FBPase) is a key enzyme in gluconeogenesis. FBPase interacts with, and inhibits the activity of, hypoxia-inducible factors (HIFs). This inhibition promotes aerobic metabolism and restrains cell proliferation. Its loss results in a second factor which up-regulates the glycolytic pathway and removes a block on cell proliferation
metabolism
-
key enzyme in gluconeogenesis and position branch point of carbon partitioning between paramylon and wax ester biosynthesis. The activity of the enzyme (EgFBPaseIII) is not regulated by AMP or reversible redox modulation
-
metabolism
-
the chloroplastic fructose-1,6-bisphosphatase (FBPase) is a late-limiting enzyme in the Calvin cycle
-
metabolism
-
the enzyme (EgFBPaseI) is critical for the Calvin cycle in Euglena chloroplasts in order to maintain normal cell growth under photoautotrophic conditions
-
metabolism
-
fructose-1,6-bisphosphatase is a key enzyme in gluconeogenesis
-
metabolism
-
fructose 1,6-bisphosphatase II is a key gluconeogenic enzyme
-
metabolism
-
essential enzyme for pathogenesis
-
metabolism
-
key enzyme of the gluconeogenic pathway
-
metabolism
-
metabolic conditions modulate aldolase B and FBPase-1 activity at the cellular level through the regulation of their interaction, suggesting that their association confers a catalytic advantage for both enzymes
-
metabolism
Picosynechococcus sp. PCC 7002 PR-6
-
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase leads to enhanced photosynthesis and global reprogramming of carbon metabolism
-
metabolism
-
key enzyme of the gluconeogenic pathway
-
metabolism
-
essential enzyme for pathogenesis
-
metabolism
-
key enzyme of the gluconeogenic pathway
-
metabolism
Picosynechococcus sp. PCC 7002 ATCC 27264
-
overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase leads to enhanced photosynthesis and global reprogramming of carbon metabolism
-
metabolism
-
the enzyme fructose 1,6-bisphosphatase takes part in the Calvin cycle, but unlike the situation in higher plants, FBPase probably does not catalyze a rate-limiting step in the Chlamydomonas reinhardtii Calvin cycle, since under photoautotrophic growth conditions and/or with elevated CO2 levels, an elevation in FBPase activity has a negative effect overall on growth rate and biomass production
-
metabolism
-
Calvin cycle enzyme
-
metabolism
-
effects of the enzyme activity on the flux balance analyses of Kluyveromyces marxianus grown on glucose and xylose as respective carbon sources (e.g. cofactor balances and sugar uptake fluxes), simulations, detailed overview. Simulation of anaerobic conditions
-
metabolism
-
simulation study of yeast metabolism, that investigates the complex interplay between the cofactors ATP, NAD+ and NADP+, in particular, how they may affect the possible roles of fructose-1,6-bisphosphatase, the pentose phosphate pathway, glycerol production and the pyruvate dehydrogenase bypass. Using flux balance analysis, it is found that the potential role of fructose-1,6-bisphosphatase is highly dependent on the cofactor specificity of the oxidative pentose phosphate pathway and on the carbon source. The fructose-1,6-bisphosphatase/phosphofructokinase substrate cycle and its regulation probably plays a key role in energy homeostasis, even in yeasts under selected conditions, which could determine phenotype switching
-
physiological function

-
the enzyme's bifunctionality ensures that heat-labile triosephosphates are quickly removed and trapped in stable D-fructose 6-phosphate, rendering gluconeogenesis unidirectional
physiological function
-
the enzyme's bifunctionality ensures that heat-labile triosephosphates are quickly removed and trapped in stable D-fructose 6-phosphate, rendering gluconeogenesis unidirectional
physiological function
-
the enzyme's bifunctionality ensures that heat-labile triosephosphates are quickly removed and trapped in stabie D-fructose 6-phosphate, rendering gluconeogenesis unidirectional
physiological function
-
the enzyme plays a regulatory role in gluconeogenesis in the retina. FBPase, in addition to its gluconeogenic role, participates in the protection of the retina against reactive oxygen species, it is also involved in non-enzymatic nuclear processes
physiological function
fructose-1,6-bisphosphatase is a key enzyme of gluconeogenesis and photosynthetic CO2 fixation, catalyzes the hydrolysis of fructose 1,6-bisphosphate to produce fructose 6-phosphate, an important precursor in various biosynthetic pathways
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
a fructose bisphosphatase-negative Corynebacterium glutamicum mutant can be phenotypically complemented with both the chromosome-encoded and the plasmid-encoded isoforms from Bacillus methanolicus
physiological function
-
heterologous expression in Corynebacterium glutamicum leads to a recombinant protein that is insensitive to fructose 1-phosphate and fructose 2,6-bisphosphate, whereas the homologous fructose-1,6-bisphosphatase is inhibited by fructose 1-phosphate and fructose 2,6-bisphosphate. The relative enzyme activity of heterologous fructose-1,6-bisphosphatase is 90.8% and 89.1% during supplement with 3 mM fructose 1-phosphate and fructose 2,6-bisphosphate, respectively. Phosphoenolpyruvate is an activator of heterologous fructose-1,6-bisphosphatase, whereas the homologous fructose-1,6-bisphosphatase is very sensitive to phosphoenolpyruvate. Overexpression of the heterologous fructose 1,6-bisphosphatase in wild-type Corynebacterium glutamicum has no effect on L-lysine production, but fructose-1,6-bisphosphatase activities are increased 9- to 13fold. Overexpression increases L-lysine production in Corynebacterim glutamicum lysC(T311I) by 57.3% on fructose, 48.7% on sucrose, and 43% on glucose. The dry cell weight and maximal specific growth rate are increased by overexpression of heterologous fructose 1,6-bisphosphatase
physiological function
compared with negative littermates, liver-specific FBPase transgenic mice have 50% less adiposity and eat 15% less food but do not have altered energy expenditure. The reduced food consumption is associated with increased circulating leptin and cholecystokinin, elevated fatty acid oxidation, and 3-beta-hydroxybutyrate ketone levels, and reduced appetite-stimulating neuropeptides, neuropeptide Y and Agouti-related peptide
physiological function
the quaternary structure of isoform FBP2 plays a crucial role in the binding binds to mitochondria where it interacts with proteins involved in regulation of energy homeostasis interaction. The AMP-driven transition of the FBP2 subunit arrangement from active to inactive precludes its association with the mitochondria. Truncation of the evolutionarily conserved N-terminal residues of FBP2 results in a loss of its mitochondria-protective functions
physiological function
fructose-1,6-bisphosphatase is a highly regulated key enzyme in gluconeogenesis and glyconeogenesis (glycogen synthesis from gluconeogenic precursors). The enzyme catalyses the hydrolysis of fructose-1,6-bisphosphate to fructose 6-phosphate and phosphate in the presence of divalent metal cations. In vitro protein-protein interaction analysis between liver fructose 1,6-bisphosphate aldolase B and liver FBPase-1 shows a specific and regulable interaction between them, whereas aldolase A (muscle isozyme) and FBPase-1 show no interaction, by real-time interaction analysis by surface plasmon resonance. The interaction between aldolase B and FBPase-1 is specific and reversible. The affinity of the aldolase B and FBPase-1 complex is modulated by intermediate metabolites, but only in the presence of K+. A decreased association constant is observed in the presence of adenosine monophosphate, fructose-2,6-bisphosphate, fructose-6-phosphate and inhibitory concentrations of fructose-1,6-bisphosphate. Conversely, the association constant of the complex increases in the presence of dihydroxyacetone phosphate (DHAP) and non-inhibitory concentrations of fructose-1,6-bisphosphate
physiological function
fructose-1,6-bisphosphatase (FBP1), the rate-limiting enzyme in gluconeogenesis, is a tumor suppressor, especially of breast cancer. The enzyme is commonly upregulated in tumor tissues compared with non-tumor tissues regardless of histological type, and lower FBP1 expression is associated with poor clinical outcome. Genetic silencing of FBP1 reduces aerobic glycolysis and the malignant potential of breast cancer cells. Elevated FBP1 is a critical modulator in breast cancer progression by altering glucose metabolism and the activity of Wnt/ beta-catenin pathway. Mechanism by which FBP1 inhibits tumor progression in breast cancer, overview. The inhibitory effect of FBP1 in glycolysis might be mediated by downregulation of c-Myc
physiological function
cytosolic fructose-1,6-bisphosphatase (FBPase) appears to be a key enzyme in gluconeogenesis and position branch point of carbon partitioning between paramylon and wax ester biosynthesis. Euglena gracilis accumulates the storage polysaccharide paramylon, a beta-1,3-glucan, under aerobic conditions. Under anaerobic conditions, the cells degrade paramylon and synthesize wax esters. The activity of EgFBPaseIII is not regulated by AMP or reversible redox modulation
physiological function
fructose-1,6-bisphosphatase (FBPase) plays a crucial role in glucose metabolism, together with glucokinase
physiological function
-
the enzyme contributes to phosphate use efficiency (PUE) under symbiotic nitrogen fixation (SNF) in Phaseolus vulgaris, expression of a phosphate-starvation inducible fructose-1,6-bisphosphatase gene in common bean nodules correlates with phosphorus use efficiency. Two contrasting recombinant inbred lines (RILs) of Phaseolus vulgaris, namely RILs 115 (phosphate-efficient) and 147 (phosphate-inefficient), that are grown under sufficient versus deficient phosphate supply. Under phosphate deficiency, higher FBPase transcript fluorescence is found in the inner cortex as compared to the infected zone of RIL115. In addition, both the specific FBPase and total APase enzyme activities significantly increase in both RILs, but to a more significant extent in RIL115 as compared to RIL147. Furthermore, the increased FBPase activity in nodules of RIL115 positively correlates with higher use efficiency of both the rhizobial symbiosis (23%) and phosphate for symbiotic nitrogen fixation (14% calculated as the ratio of N2 fixed per nodule total phosphate content). The abundant tissue-specific localized FBPase transcript along with induced enzymatic activity provides evidence of a specific tolerance mechanism where N2-fixing nodules overexpress under phosphate-deficiency conditions
physiological function
the Calvin-Benson cycle (CBC) fructose-1,6-bisphosphatase (FBPase) isoform is well known to be redox activated by thioredoxin f through the reduction of a disulfide bridge involving Cys153 and Cys173. cFBP1 needs to be redox activated in order to be fully active
physiological function
the physiological role of muscle FBPase goes beyond its enzymatic function, as this isozyme is localized inside cell nuclei and is shown to interact with mitochondria, where it is involved in regulation of the cell cycle. The behaviour of the muscle isozyme differs greatly from the liver isozyme
physiological function
class II fructose-1,6-bisphosphatase enzyme in Mycobacterium tuberculosis is an essential enzyme for pathogenesis
physiological function
expression of enzyme in Euglena gracilis cells to enhance its photosynthetic activity. The cell volume of the transgenic cell line is significantly larger than that of wild-type cells under normal growth conditions and the photosynthetic activity is significantly higher than that of wild type under high light and high CO2, resulting in enhanced biomass production. The accumulation of paramylon is increased. Transgenic cell lines grown under high light and high CO2 and placed on anaerobiosis show approximately 13- to 100fold higher productivity of wax esters than in wild-type cells
physiological function
fructose 1,6-bisphosphatase (FBPase) is a major control point in gluconeogenesis, catalyzing the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and phosphate. This step in gluconeogenesis is synergistically downregulated by fructose 2,6-bisphosphate and AMP, which bind to the active site and an allosteric site of FBPase, respectively
physiological function
overexpression of BiBPase enhances growth, cell size, and photosynthetic O2 evolution, and coordinately upregulates enzymes in the Calvin Benson cycle including RuBisCO and fructose-1,6-bisphosphate aldolase. Overexpression downregulates enzymes in respiratory carbon metabolism including glucose-6-phosphate dehydrogenase. The content of glycogen is significantly reduced while the soluble carbohydrate content is increased
physiological function
bifunctional enzyme FBP/SBPase is unique in that it catalyses two separate reactions in the Calvin cycle, both of which are catalysed by separate enzymes in plants. The reactions catalysed by FBP/SBPase are important for Calvin cycle flux, as indicated by their high predicted metabolic control coefficients
physiological function
fructose-1,6-bisphophatase catalyzes the breakdown of fructose 1,6-bisphosphate to fructose 6-phosphate and phosphate. Two FBPase isoenzymes are identified in photosynthetic eukaryotic cells: a cytosolic form, a key enzyme in gluconeogenesis, and a chloroplastic form, a rate-limiting enzyme involved in the Calvin cycle
physiological function
enzyme FBPase is a key rate-controlling enzyme in the gluconeogenic pathway. FBPase activity is regulated synergistically by the allosteric inhibitors AMP and fructose-2,6-bisphosphate (F2,6-BP). FBPase functions in the degradation of fructose-1,6-bisphosphate (FBP), which hydrolyzes to fructose-6-phosphate (F6P) and phosphate
physiological function
enzyme FBPase is a key rate-controlling enzyme in the gluconeogenic pathway. FBPase activity is regulated synergistically by the allosteric inhibitors AMP and fructose-2,6-bisphosphate. FBPase functions in the degradation of fructose-1,6-bisphosphate, which hydrolyzes to fructose-6-phosphate and phosphate
physiological function
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
physiological function
key regulator of gluconeogenesis
physiological function
-
the enzyme is involved in the Calvin cycle
physiological function
overexpression of fructose 1,6-bisphosphatase has a detrimental effect on growth
physiological function
key enzyme in hepatic gluconeogenesis pathway
physiological function
-
the enzyme may be regulated via post-translational modifications
physiological function
-
fructose 1,6-bisphosphatase is involved in the rate-limiting catalytic step of fructose-1,6-bisphosphate conversion to fructose-6-phosphate
physiological function
Campylobacter jejuni serotype O:2
enzyme regulation, overview. Campylobacter jejuni FBPase is not inhibitred by AMP. The enzyme also shows limited sensitivity to other glycolytic and gluconeogenic intermediates. The allosteric cooperative control of the enzyme's activity found in type I FBPases appears to have been lost
physiological function
-
regulation of fructose-1,6-bisphosphatase (FBPase) from wood frog liver during freezing, FBPase is a crucial enzyme regulating gluconeogenesis. FBPase is suppressed, and gluconeogenesis is inhibited during freezing. This response acts as an important component of the metabolic survival strategy of the wood frog
physiological function
-
while not a direct target for insulin signaling, fructose-1,6-bisphosphatase (FBP1) is rate controlling for gluconeogenesis converting F1,6-P2 to F6-P which is then converted to glucose 6-P by phosphoglucoseisomerase (PGI).Fructose-1,6-bisphosphatase is a nonenzymatic safety valve that curtails AKT activation to prevent insulin hyperresponsiveness. FBP1 may regulate AKT activity through its interaction with ALDOB. FBP1 assembles the AKT inhibitory complex through separate and distinct contacts with AKT, PP2A-C and ALDOB
physiological function
fructose-1,6-bisphosphatase (FBP1) is rate controlling for gluconeogenesis. Fructose-1,6-bisphosphatase is a nonenzymatic safety valve that curtails AKT activation to prevent insulin hyperresponsiveness. Enzyme FBP1 is a critical regulator of insulin signaling, serving as an endogenous safety valve that prevents insulin hyperresponsiveness and balances glucose and lipid metabolism. FBP1 negatively controls insulin signaling by nucleating a stable multiprotein complex that also contains aldolase B (ALDOB), an enzyme that acts upstream to FBP1 in the gluconeogenesis pathway, the catalytic subunit of protein phosphatase 2A (PP2A-C) which dephosphorylates AKT, the key effector of insulin signaling. Complex formation which keeps AKT activation in check is enhanced by fasting and weakened during the fed state by insulin. Defective complex assembly causes hyperresponsiveness to the small amounts of insulin that are released in response to lipolysis-generated free fatty acids (FFA), thereby triggering hepatosteatosis and hyperlipidemia. Conversely, pharmacological complex disruption with an FBP1-derived peptide reverses diet-induced insulin resistance. FBP1 associates with PP2A-C and ALDOB to bind AKT and inhibit its activation
physiological function
glucose metabolism is balanced by catabolic glycolysis/oxidative phosphorylation (OXPHOS) and anabolic gluconeogenesis/glycogen production. Since FBP2 is a rate-limiting enzyme in gluconeogenesis, FBP2 re-expression is likely to antagonize glycolysis and therefore reduce glucose uptake. FBP2 has catalytic activity-independent cellular functions. Nuclear FBP2 regulates mitochondrial function independent of its enzymatic activity. FBP2 co-localizes with c-Myc at the promoter region of TFAM, which encodes a master regulator of mitochondrial biogenesis, and inhibits c-Myc-mediated TFAM expression. FBP2 inhibits glycolysis, which further affects serine and TCA cycle metabolism. Nuclear FBP2 contributes functionally to its growth inhibitory properties, nuclear FBP2 is required for inhibiting OXPHOS in an enzymatic activity-independent manner. FBP2 suppresses mitochondrial respiration and the TCA cycle. FBP2 inhibits c-Myc transcriptional activation of TFAM, by direct physical association at its promoter
physiological function
the gluconeogenic enzyme fructose 1,6-biphosphatase 1 (FBP1) that catalyzes the hydrolysis of fructose 1,6-bisphosphate (F-1,6-BP) to fructose 6-phosphate (F-6-P) as a protein phosphatase. FBP1 dephosphorylates IkappaBalpha as a protein phosphatase and suppresses colorectal tumorigenesis, FBP1 functions as a protein phosphatase to dephosphorylate IkappaBalpha, the key inhibitory regulator of NF-kappaB signaling. FBP1-catalyzed IkappaBalpha dephosphorylation sensitizes tumor cells to inflammation-associated cell death by downregulating the expression of prosurvival genes. FBP1-catalyzed IkappaBalpha dephosphorylation suppresses colorectal tumorigenesis by promoting inflammation-associated cell death and preventing MDSCs mobilization. FBP1 expression inversely correlates with NF-kappaB activation, cell survival, and MDSC infiltration in human CRC tumors, clinical association among FBP1-regulated NF-kappaB activation, cell survival and MDSCs abundance in human CRC patients
physiological function
Skeletal muscle is a major organ for glucose disposal and thermogenesis, essential role of fructose-1,6-bisphosphatase 2 (Fbp2) enzyme in thermal homeostasis upon cold stress. Fbp2 is essential for muscle thermogenesis by replenishing the intramuscular glycogen pool through glyconeogenesis when the exogenous glucose source is limited. Fbp2 is necessary for intramuscular glyconeogenesis and affects mitochondrial respiration
physiological function
fructose-1,6-biphosphatase (FBP1) is a key enzyme in gluconeogenesis and is associated with tumor initiation in several cancers. Intratumoral FBP1 expression is significantly associated with a better prognosis. In multivariate analysis, elevated FBP1 expression is an independent biomarker associated with a favorable prognosis. The presence of the FBP1 protein increases the sensitivity of pancreatic cancer cells to the bromodomain and extraterminal domain (BET) inhibitor JQ1. FBP1 inhibits catabolic metabolic pathways such as glycolysis guaranteeing tumor cells an ongoing supply of nutrients via lactate or amino acids to feed the biosynthetic pathways
physiological function
liver fructose 1,6-bisphosphatase (FBPase) is a recognized regulatory enzyme of the gluconeogenesis pathway
physiological function
cytosolic fructose-1,6-bisphosphatase (cyFBPase) is a key enzyme of the sucrose biosynthesis pathway, working in coordination with sucrose phosphate synthase (SPS) catalyzing the first irreversible reaction in the conversion
physiological function
-
the red-eared slider (Trachemys scripta elegans) undergoes numerous changes to its physiological and metabolic processes to survive without oxygen. During anoxic conditions, its metabolic rate drops drastically to minimize energy requirements. The alterations in the central metabolic pathways are often accomplished by the regulation of key enzymes. The metabolism is reduced to about 10-20% of the aerobic values, causing tissues to switch to a reliance on glycolysis alone for ATP production. Maintaining cellular energetics is one of the major concerns under anoxic conditions. This is because the conversion of glucose to lactate via glycolysis yields only 2 ATP per glucose molecule catabolized compared with the full aerobic oxidation of glucose to CO2 and H2O, which yields 36 ATP per glucose. Fructose-1,6-bisphosphatase, FBPase, is a crucial enzyme of gluconeogenesis. FBPase catalyzes the removal of a phosphate from Fructose-1,6-bisphosphate to form fructose-6-phosphate, in the presence of metal ions, magnesium or manganese. The phosphorylation of liver FBPase is an important step in suppressing FBPase activity, ultimately leading to the inhibition of gluconeogenesis in the liver of the red-eared slider during anaerobic conditions. FBPase is an allosteric enzyme. Its activity is stimulated by high ATP concentrations, whereas AMP and fructose 2,6-biphosphate are negative regulators. The regulation of FBPase is also accomplished by reversible protein phosphorylation
physiological function
fructose 1,6-bisphosphatase (FBPase) is a key enzyme in gluconeogenesis. It is a potential drug target in the treatment of type II diabetes. The protein is also associated with a rare inherited metabolic disease and some cancer cells lack FBPase activity which promotes glycolysis facilitating the Warburg effect
physiological function
-
distinct allosteric regulation of isozyme FBP1 and FBP2, detailed overview. FBPases as regulators of nuclear processes
physiological function
long-term potentiation (LTP), a synaptic plasticity in the hippocampus, is a molecular basis of memory formation. LTP critically depends on fructose 1,6-bisphosphatase 2 (Fbp2), a glyconeogenic enzyme and moonlighting protein protecting mitochondria against stress. The NAD+-level-dependent increase of the Fbp2 dimer/tetramer ratio might be a crucial mechanism in which astrocyte-neuron lactate shuttle stimulates LTP formation. Fbp2 is an inherent element of the machinery of memory formation in the hippocampal structures. Hippocampal neurons express predominantly the Fbp2 isoform and that its colocalization with mitochondria is associated with the LTP induction. Upon the LTP induction, Fbp2 interacts with Camk2 and stimulates its autophosphorylation, which is an indispensable step leading to formation of the early phase of the LTP. The capability of Fbp2 to adopt various quaternary conformations in the presence of AMP and NAD+, and hence its ability to interact with different cellular binding partners suggests that Fbp2 may be a decision center linking neurotransmitter signaling with energetic and redox state of brain during formation of memory traces. Expression of the late-phase LTP depends on Fbp2 structure and concentration
physiological function
-
in plants, at least two distinct FBPase isozymes exist. One is located in the chloroplasts stroma (chloroplastic FBPase, cpFBPase), which acts as a key regulator of the Calvin cycle by taking part in the production of ribulose-l,5-bisphosphate, an acceptor of CO2 fixation . The other is related to the gluconeogenesis and sucrose metabolism, cytosolic fructose-1,6-bisphosphatase (cFBPase) from mung bean is a rate-limiting enzyme in gluconeogenesis catalysing the irreversible conversion of the substrate fructose-1,6-bisphosphate (F16BP) into fructose-6-phosphate. Isozyme cFBPase controls the rate of triose phosphates withdrawal from the chloroplast. Vr-cFBPase and its related metabolism might be regulated by the AMP content in mung bean
physiological function
-
cytosolic fructose-1,6-bisphosphatase (FBPase) appears to be a key enzyme in gluconeogenesis and position branch point of carbon partitioning between paramylon and wax ester biosynthesis. Euglena gracilis accumulates the storage polysaccharide paramylon, a beta-1,3-glucan, under aerobic conditions. Under anaerobic conditions, the cells degrade paramylon and synthesize wax esters. The activity of EgFBPaseIII is not regulated by AMP or reversible redox modulation
-
physiological function
-
fructose-1,6-bisphophatase catalyzes the breakdown of fructose 1,6-bisphosphate to fructose 6-phosphate and phosphate. Two FBPase isoenzymes are identified in photosynthetic eukaryotic cells: a cytosolic form, a key enzyme in gluconeogenesis, and a chloroplastic form, a rate-limiting enzyme involved in the Calvin cycle
-
physiological function
-
class II fructose-1,6-bisphosphatase enzyme in Mycobacterium tuberculosis is an essential enzyme for pathogenesis
-
physiological function
-
long-term potentiation (LTP), a synaptic plasticity in the hippocampus, is a molecular basis of memory formation. LTP critically depends on fructose 1,6-bisphosphatase 2 (Fbp2), a glyconeogenic enzyme and moonlighting protein protecting mitochondria against stress. The NAD+-level-dependent increase of the Fbp2 dimer/tetramer ratio might be a crucial mechanism in which astrocyte-neuron lactate shuttle stimulates LTP formation. Fbp2 is an inherent element of the machinery of memory formation in the hippocampal structures. Hippocampal neurons express predominantly the Fbp2 isoform and that its colocalization with mitochondria is associated with the LTP induction. Upon the LTP induction, Fbp2 interacts with Camk2 and stimulates its autophosphorylation, which is an indispensable step leading to formation of the early phase of the LTP. The capability of Fbp2 to adopt various quaternary conformations in the presence of AMP and NAD+, and hence its ability to interact with different cellular binding partners suggests that Fbp2 may be a decision center linking neurotransmitter signaling with energetic and redox state of brain during formation of memory traces. Expression of the late-phase LTP depends on Fbp2 structure and concentration
-
physiological function
-
fructose-1,6-bisphosphatase is a highly regulated key enzyme in gluconeogenesis and glyconeogenesis (glycogen synthesis from gluconeogenic precursors). The enzyme catalyses the hydrolysis of fructose-1,6-bisphosphate to fructose 6-phosphate and phosphate in the presence of divalent metal cations. In vitro protein-protein interaction analysis between liver fructose 1,6-bisphosphate aldolase B and liver FBPase-1 shows a specific and regulable interaction between them, whereas aldolase A (muscle isozyme) and FBPase-1 show no interaction, by real-time interaction analysis by surface plasmon resonance. The interaction between aldolase B and FBPase-1 is specific and reversible. The affinity of the aldolase B and FBPase-1 complex is modulated by intermediate metabolites, but only in the presence of K+. A decreased association constant is observed in the presence of adenosine monophosphate, fructose-2,6-bisphosphate, fructose-6-phosphate and inhibitory concentrations of fructose-1,6-bisphosphate. Conversely, the association constant of the complex increases in the presence of dihydroxyacetone phosphate (DHAP) and non-inhibitory concentrations of fructose-1,6-bisphosphate
-
physiological function
-
expression of enzyme in Euglena gracilis cells to enhance its photosynthetic activity. The cell volume of the transgenic cell line is significantly larger than that of wild-type cells under normal growth conditions and the photosynthetic activity is significantly higher than that of wild type under high light and high CO2, resulting in enhanced biomass production. The accumulation of paramylon is increased. Transgenic cell lines grown under high light and high CO2 and placed on anaerobiosis show approximately 13- to 100fold higher productivity of wax esters than in wild-type cells
-
physiological function
-
overexpression of BiBPase enhances growth, cell size, and photosynthetic O2 evolution, and coordinately upregulates enzymes in the Calvin Benson cycle including RuBisCO and fructose-1,6-bisphosphate aldolase. Overexpression downregulates enzymes in respiratory carbon metabolism including glucose-6-phosphate dehydrogenase. The content of glycogen is significantly reduced while the soluble carbohydrate content is increased
-
physiological function
-
the enzyme regulates the intracellular balance of NAD(H) and NADP(H)
-
physiological function
-
a fructose bisphosphatase-negative Corynebacterium glutamicum mutant can be phenotypically complemented with both the chromosome-encoded and the plasmid-encoded isoforms from Bacillus methanolicus
-
physiological function
-
class II fructose-1,6-bisphosphatase enzyme in Mycobacterium tuberculosis is an essential enzyme for pathogenesis
-
physiological function
-
Skeletal muscle is a major organ for glucose disposal and thermogenesis, essential role of fructose-1,6-bisphosphatase 2 (Fbp2) enzyme in thermal homeostasis upon cold stress. Fbp2 is essential for muscle thermogenesis by replenishing the intramuscular glycogen pool through glyconeogenesis when the exogenous glucose source is limited. Fbp2 is necessary for intramuscular glyconeogenesis and affects mitochondrial respiration
-
physiological function
-
overexpression of fructose 1,6-bisphosphatase has a detrimental effect on growth
-
physiological function
Campylobacter jejuni serotype O:2 ATCC 700819
-
enzyme regulation, overview. Campylobacter jejuni FBPase is not inhibitred by AMP. The enzyme also shows limited sensitivity to other glycolytic and gluconeogenic intermediates. The allosteric cooperative control of the enzyme's activity found in type I FBPases appears to have been lost
-
physiological function
Campylobacter jejuni serotype O:2 NCTC 11168
-
enzyme regulation, overview. Campylobacter jejuni FBPase is not inhibitred by AMP. The enzyme also shows limited sensitivity to other glycolytic and gluconeogenic intermediates. The allosteric cooperative control of the enzyme's activity found in type I FBPases appears to have been lost
-
additional information

-
active site structures, overview
additional information
-
active site structures, overview
additional information
cytosolic EgFBPaseIII is identical to the neutral FBPase
additional information
-
cytosolic EgFBPaseIII is identical to the neutral FBPase
additional information
the apoform of enzyme LmFBPase is a homotetramer in which the dimer of dimers adopts a planar conformation with disordered dynamic loops. The structure of LmFBPase, complexed with manganese and the catalytic product phosphate, shows the dynamic loops locked into the active sites. The dynamic loop (residues 52-71), which has been shown to be catalytically important in mammalian FBPases, is in a similar position in LmFBPase but shows functionally important sequence differences and has two insertions (Tyr57 and Gln61) compared with mammalian and bacterial sequences. Enzyme structure analysis and structure-function relationship, modeling, overview. Conformational variability of the FBPase active site
additional information
-
the apoform of enzyme LmFBPase is a homotetramer in which the dimer of dimers adopts a planar conformation with disordered dynamic loops. The structure of LmFBPase, complexed with manganese and the catalytic product phosphate, shows the dynamic loops locked into the active sites. The dynamic loop (residues 52-71), which has been shown to be catalytically important in mammalian FBPases, is in a similar position in LmFBPase but shows functionally important sequence differences and has two insertions (Tyr57 and Gln61) compared with mammalian and bacterial sequences. Enzyme structure analysis and structure-function relationship, modeling, overview. Conformational variability of the FBPase active site
additional information
redox pattern displayed by cFBP1, overview
additional information
-
the FBP active site works by stabilizing the FBPase, and the allosteric site impairs the activity of FBPase through its binding of a nonsubstrate molecule. Competitive inhibition of AMP, fructose 1,6-bisphosphate, or fructose 6-phosphate binding to FBPase with fluorescent AMP analogue, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP)-binding FBPase
additional information
the transition from the inactive, AMP-associated T state towards the active R state involves a reversible refolding of a key helix that is part of the allosteric centre of muscle FBPase
additional information
-
the transition from the inactive, AMP-associated T state towards the active R state involves a reversible refolding of a key helix that is part of the allosteric centre of muscle FBPase
additional information
Thr84 in MtFBPaseII protein (Thr90 in Escherichia coli) is a conserved residue in the active site as shown in other FBPases
additional information
active-site residue are Asp33, Glu57, Glu100, Thr102, Tyr131, Lys134, Arg176, Arg178, Asp198, Asp200, and Glu225
additional information
sequence comparisons of human and porcine FBPase 1, overview. Residue L56 coordinates the (4-[3-(6,7-diethoxy-quinazolin-4-ylamino)-phenyl]-thiazol-2-yl)-methanol (PFE) inhibitor ligand, as does residue L73, both of which exhibit hydrophobic interactions with the ligand in the PFE-binding site. In addition, L73 and L56 are part of a network that leads from the allosteric binding site to the active site of the enzyme. Residue M248 is positioned near the triad of acidic residues co-ordinating manganese and is found in the active site to co-ordinate D-fructose 6-phosphate
additional information
sequence comparisons of human and porcine FBPase 1, overview. The M177 and Y164 interfacial residues are positioned between the AMP-binding site and active sites
additional information
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sequence comparisons of human and porcine FBPase 1, overview. The M177 and Y164 interfacial residues are positioned between the AMP-binding site and active sites
additional information
the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
additional information
-
FBPase activity differs significantly between PF 2913 and PF AnTat1.1 cells and is influenced by extracellular glucose levels and cell density. Identification of conditions in which FBPase activity levels change while protein abundance remain constant, suggesting enzyme activity is modulated by post-translational modifications
additional information
Campylobacter jejuni serotype O:2
three-dimensional structure homology modelling of cjFBPase using pig FBPase structure (PDB ID 1NUW) as the template
additional information
high-throughput screening of metabolic phosphatases with molecular docking followed by molecular dynamics (MD) simulations
additional information
A0A7T7JA26
two residues from the symmetry-related chain D (Glu238 and Glu239) make distinct interactions with residues in the active site which, although providing a more rigid environment, are likely to affect the resulting structure by their presence
additional information
highly hydrophilic nature of the FBPase active site
additional information
allosteric changes are transmitted through proteins by conformational changes, alterations in mobility or a combination of the two. Crystal structures of FBPase with and without AMP bound have provided considerable information on the changes which occur at the ligand binding site and at the interface between subunits of the tetramer. Mutational analysis and molecular dynamics simulations are used to analyze structure-function relationships in the allosteric enzyme, overview
additional information
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the tertiary structure of each monomer is composed of two domains, a domain containing the substrate binding site (FBP domain) and an allosteric domain which may interact with AMP and NAD+ (AMP domain). Binging of AMP, and presumably NAD+, stabilizes an inactive, T-state of FBPase. Divalent cations such as Mg2+, Mn2+, Co2+ or Zn2+ are indispensable for catalysis while Ca2+ is a strong inhibitor of the muscle FBPase having only minor effect on the liver isoform. While the inactive T-states of FBP1 and FBP2 are similar, the active R-state of FBP2 adopts the cruciform structure while in the liver enzyme, the R-state is planar
additional information
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the tertiary structure of each monomer is composed of two domains, a domain containing the substrate binding site (FBP domain) and an allosteric domain which may interact with AMP and NAD+ (AMP domain). Binding of AMP, and presumably NAD+, stabilizes an inactive, T-state of FBPase. Divalent cations such as Mg2+, Mn2+, Co2+ or Zn2+ are indispensable for catalysis while Ca2+ is a strong inhibitor of the muscle FBPase having only minor effect on the liver isoform. While the inactive T-states of FBP1 and FBP2 are similar, the active R-state of FBP2 adopts the cruciform structure while in the liver enzyme, the R-state is planar
additional information
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the cFBPase active site residues are Asn218 and Met251. Structural model of FBP from Vigna radiata obtained from homology modelling using the crystal structure of FBP from pig kidney (PDB ID 1FSA) as the template. Molecular docking study of wild-type enzyme with substrate D-fructose 1,6-bisphosphate
additional information
-
analysis of the interatomic distances among the substrate, product, and divalent metal cations in the catalytic centers of the enzyme leads to a revision of the catalytic mechanism suggested previously for class II FBPases. It is proposed that phosphate-1 is cleaved from the substrate fructose-1,6-bisphosphate by residue T89 in a proximal alpha-helix backbone (G88-T89-T90-I91-T92-S93-K94) in which the substrate transition state is stabilized by the positive dipole of the h-helix backbone. Once cleaved a water molecule found in the active site liberates the inorganic phosphate from T89 completing the catalytic mechanism
additional information
analysis of the interatomic distances among the substrate, product, and divalent metal cations in the catalytic centers of the enzyme leads to a revision of the catalytic mechanism suggested previously for class II FBPases. It is proposed that phosphate-1 is cleaved from the substrate fructose-1,6-bisphosphate by residue T89 in a proximal alpha-helix backbone (G88-T89-T90-I91-T92-S93-K94) in which the substrate transition state is stabilized by the positive dipole of the h-helix backbone. Once cleaved a water molecule found in the active site liberates the inorganic phosphate from T89 completing the catalytic mechanism
additional information
-
cytosolic EgFBPaseIII is identical to the neutral FBPase
-
additional information
-
Thr84 in MtFBPaseII protein (Thr90 in Escherichia coli) is a conserved residue in the active site as shown in other FBPases
-
additional information
-
the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
-
additional information
-
the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
-
additional information
-
Thr84 in MtFBPaseII protein (Thr90 in Escherichia coli) is a conserved residue in the active site as shown in other FBPases
-
additional information
-
the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
-
additional information
Campylobacter jejuni serotype O:2 ATCC 700819
-
three-dimensional structure homology modelling of cjFBPase using pig FBPase structure (PDB ID 1NUW) as the template
-
additional information
Campylobacter jejuni serotype O:2 NCTC 11168
-
three-dimensional structure homology modelling of cjFBPase using pig FBPase structure (PDB ID 1NUW) as the template
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C157S
-
slightly more active than wild type enzyme
C157S/C174S
-
activity remains unchanged
C174S
-
mildly less active than wild type enzyme
C174S/C179S
-
slightly more active than wild type enzyme
C174S/C307S
-
activity remains unchanged
C179S
-
slightly more active than wild type enzyme
C307S
-
activity remains unchanged
C53S
-
mildly less active than wild type enzyme
C53S/C174S
-
mildly less active than wild type enzyme
C96S
-
slightly more active than wild type enzyme
D186A
Km (mM) (D-fructose 1,6-bisphosphate): 0.2 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 1.2 (wild-type: 5.7/sec)
E59A
Km (mM) (D-fructose 1,6-bisphosphate): 0.1 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 1.1 (wild-type: 5.7/sec)
K239A
Km (mM) (D-fructose 1,6-bisphosphate): 0.1 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 7.5 (wild-type: 5.7/sec)
K29A
Km (mM) (D-fructose 1,6-bisphosphate): 0.06 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 14 (wild-type: 5.7/sec)
L54A
-
enzymic activity similar to wild-type, but much less sensitive to inhibition by AMP. Crystallization data in presence of AMP
R235A
Km (mM) (D-fructose 1,6-bisphosphate): 0.2 (wild-type: 0.07 mM), kcat (1/sec)(D-fructose 1,6-bisphosphate): 5.4 (wild-type: 5.7/sec)
T89A
A0A7T7JA26
site-directed mutagenesis, inactive mutant
T89S
A0A7T7JA26
site-directed mutagenesis, the mutant shows 4fold reduced activity compared to wild-type
A177D
site-directed mutagenesis, inactive mutant
Delta1
-
deletion of the first and the first two N-terminal amino acids of FBPase affects neither the kinetic properties of the enzyme nor its association with aldolase
DELTA10
-
deletion of the first 10 amino acids: affinity to aldolase is significantly reduced, cooperativitiy of Mg2+ activation is abolished and results in biphasic inhibition of the enzyme by AMP. Truncation lowers affinity of muscle FBPase to aldolase about 14times, making it resemble the liver isozyme, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA2
-
deletion of the first and the first two N-terminal amino acids of FBPase affects neither the kinetic properties of the enzyme nor its association with aldolase
DELTA3
-
deletion of the first 3 amino acids: kinetic properties similar to wild-type, affinity to aldolase is significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA4
-
deletion of the first 4 amino acids: kinetic properties similar to wild-type, affinity to aldolase is significantly reduced, mutant shows a lower sensitivity to inhibition by AMP and a little weaker activation by Mg2+, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA5
-
deletion of the first 5 amino acids: mutant is significantly weaker inhibited by AMP than wild-tpye, affinity to aldolase is significantly reduced, kcat and activation by Mg2+ are significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA6
-
deletion of the first 6 amino acids: mutant is significantly weaker inhibited by AMP than wild-tpye, affinity to aldolase is significantly reduced, kcat and activation by Mg2+ are significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA7
-
deletion of the first 7 amino acids: mutant is significantly weaker inhibited by AMP than wild-tpye, affinity to aldolase is significantly reduced, kcat and activation by Mg2+ are significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
DELTA8
-
deletion of the first 8 amino acids: mutant is significantly weaker inhibited by AMP than wild-tpye, affinity to aldolase is significantly reduced, kcat significantly reduced, Km (D-fructose 1,6-bisphosphate) similar to wild-type
E20K
liver enzyme, mutation towards the muscle enzyme
E20K/M177T/C179Q
liver enzyme, mutation towards the muscle enzyme
E98A
-
site-directed mutagenesis, catalytically inactive mutant. FBP1E98A does associate with AKT, ALDOB and PP2A-C
G123A
site-directed mutgenesis, the interaction of the mutant enzyme aand Ikappa Balpha is unaltered compared to wild-type
G260R
site-directed mutagenesis, a catalytically inactive FBP2 mutant is generated by replacing a glycine residue at position 260 with arginine. FBP2G260R inhibits cell growth, although to a lesser extent than wild-type FBP2. Catalytically inactive FBP2G260R downregulates mitochondrial gene expression to a similar level as wild-type FBP2
G261A
site-directed mutagenesis, inactive mutant
K112A
site-directed mutagenesis, the mutation alters the AMP binding site
K203A/K204A/K205A/K207A
site-directed mutagenesis, by replacing four lysine residues in the NLS with alanine, a nucleus-excluded form of FBP2 is generated without disrupting its catalytic activity, FBP24KA expression in LPS246 cells decreases cell proliferation albeit, not as dramatically as wild-type FBP2
K203E
-
mutation results in a noticeable drop in the amount of cells having nuclear FBPase
K204E
-
mutation results in a noticeable drop in the amount of cells having nuclear FBPase
K205E
-
mutation results in a noticeable drop in the amount of cells having nuclear FBPase
K207E
-
mutation results in a noticeable drop in the amount of cells having nuclear FBPase
K208F
site-directed mutgenesis, the interaction of the mutant enzyme aand Ikappa Balpha is unaltered compared to wild-type
K20E
muscle enzyme, mutation towards the liver enzyme
K20E/T177M/Q179C
muscle enzyme, mutation towards the liver enzyme
K270A
site-directed mutgenesis, the interaction of the mutant enzyme aand Ikappa Balpha is unaltered compared to wild-type
L329P
-
site-directed mutagenesis, the mutant no longer inhibits insulin stimulated AKT phosphorylation. FBP1L329P in exon 7 is relatively well expressed with only a partial loss of FBP1 catalytic activity but completely devoid of AKT inhibitory activity. FBP1L329P does not associate with AKT, ALDOB and PP2A-C
L56A
site-directed mutagenesis, the mutant shows altered binding to inhibitor compared to wild-type enzyme
L73A
site-directed mutagenesis, the mutant shows altered binding to inhibitor compared to wild-type enzyme
M177A
site-directed mutagenesis, the mutation alters the subunit interface
M177T/C179Q
liver enzyme, mutation towards the muscle enzyme
M248D
site-directed mutagenesis, the mutant shows increased metal affinity and a 5fold increase in enzymatic activity compared to wild-type
Q32R
conentration of AMP required for 50% inhibition of the Q32R mutant is increased 19fold, and the cooperativity of both AMP and Mg2+ is abolished or decreased. The mutation affects the conformations of both N-terminal residues and the dynamic loop 5272
R158W
-
site-directed mutagenesis, the mutant no longer inhibits insulin stimulated AKT phosphorylation
R277A
site-directed mutgenesis, the interaction of the mutant enzyme aand Ikappa Balpha is unaltered compared to wild-type
R314A
site-directed mutgenesis, the interaction of the mutant enzyme aand Ikappa Balpha is unaltered compared to wild-type
S124A
site-directed mutgenesis, the interaction of the mutant enzyme aand Ikappa Balpha is unaltered compared to wild-type
T177M/Q179C
muscle enzyme, mutation towards the liver enzyme
Y113A
site-directed mutagenesis, the mutation alters the AMP binding site
Y113F
site-directed mutagenesis, the mutant shows greatly reduced sensitivity to AMP, but also to fructose 2,6-bisphosphate
Y164A
site-directed mutagenesis, the mutation alters the subunit interface
H20A
-
the mutant shows reduced activity compared to the wild type enzyme
H20N
-
the mutant shows reduced activity compared to the wild type enzyme
H20Q
-
the mutant shows reduced activity compared to the wild type enzyme
K76A
-
the mutant shows reduced activity compared to the wild type enzyme
T16P
-
the mutant shows reduced activity compared to the wild type enzyme
C153S
site-directed mutagenesis
C173S/C178S
site-directed mutagenesis
K115Q
-
Km (D-fructose 1,6-bisphosphate) and Ki (D-fructose 2,6-bisphosphate) comparable to wild-type, IC50 (AMP): 5.8 mM
Y116Q
-
Km (D-fructose 1,6-bisphosphate) and Ki (D-fructose 2,6-bisphosphate) comparable to wild-type, IC50 (AMP): 15.9 mM
E98A
site-directed mutagenesis, catalytically inactive mutant
D40N
-
almost complete loss of both inositol monophosphatase and fructose 1,6-bisphosphatase activity
D94N
-
almost complete loss of both inositol monophosphatase and fructose 1,6-bisphosphatase activity
L71A
-
no loss of either of the activities, activity toward inositol is more resisitant to inhibition by calcium than wild-type
D40N
-
almost complete loss of both inositol monophosphatase and fructose 1,6-bisphosphatase activity
-
D94N
-
almost complete loss of both inositol monophosphatase and fructose 1,6-bisphosphatase activity
-
L71A
-
no loss of either of the activities, activity toward inositol is more resisitant to inhibition by calcium than wild-type
-
D221A
loss of 60-70% of activity for both FBPase and IMPase activities
G94A/T95A
mutations partially restore the IMPase activity compared to the single mutants
T95A
about 60% loss of both FBPase and IMPase activities
T95S
about 35% loss of both FBPase and IMPase activities
W220A
loss of 60-70% of activity for both FBPase and IMPase activities
W220A/D221A
mutations reduces both FBPase and IMPase activity drastically
G94A/T95A
-
mutations partially restore the IMPase activity compared to the single mutants
-
T95A
-
about 60% loss of both FBPase and IMPase activities
-
T95S
-
about 35% loss of both FBPase and IMPase activities
-
W220A
-
loss of 60-70% of activity for both FBPase and IMPase activities
-
W220A/D221A
-
mutations reduces both FBPase and IMPase activity drastically
-
E69Q
-
mutation of E69Q results in a 500fold increase of muscle isozyme I0.5 versus Ca2+
D233N
mutant protein is impaired in both aldolase and phosphatase activity
E357Q
mutation abolishes phosphatase activity, no effect on aldolase activity
K232R
mutation abolishes aldolase activity, phosphatase activity is enhanced
Y229F
mutation abolishes aldolase activity, phosphatase activity is slightly reduced
Y358F
mutation abolishes phosphatase activity, no effect on aldolase activity
D233N
-
mutant protein is impaired in both aldolase and phosphatase activity
-
E357Q
-
mutation abolishes phosphatase activity, no effect on aldolase activity
-
K232R
-
mutation abolishes aldolase activity, phosphatase activity is enhanced
-
Y229F
-
mutation abolishes aldolase activity, phosphatase activity is slightly reduced
-
Y358F
-
mutation abolishes phosphatase activity, no effect on aldolase activity
-
E99A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
H13A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
H178A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
H244A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
H268A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
R181A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
R69A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
S11A
-
properties are closely similar compared to wild type enzyme
S11D
-
properties are closely similar compared to wild type enzyme
S19A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
S65A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
W131A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
Y24A
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
G20D
-
kcat for fructose 1,6-bisphosphate is 1.62fold lower than wild-type enzyme, Km-value for fructose 1,6-diphosphate is 1.86fold higherr than wild-type enzyme
T23I
-
kcat for fructose 1,6-bisphosphate is 1.2fold lower than wild-type enzyme, Km-value for fructose 1,6-diphosphate is 1.3fold lower than wild-type enzyme
T91I
-
kcat for fructose 1,6-bisphosphate is 1.1fold higher than wild-type enzyme, Km-value for fructose 1,6-diphosphate is 1.14fold lower than wild-type enzyme
Y229F
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 1.1fold higher than the wild-type value, no fructose-bisphosphate aldolase activity
Y348F
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 3.5fold lower than the wild-type value, the kcat/Km-value for the fructose-bisphosphate aldolase reaction of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) in the anabolic direction is 16fold lower than wild-type value
Y229F
-
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 1.1fold higher than the wild-type value, no fructose-bisphosphate aldolase activity
-
Y348F
-
the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 3.5fold lower than the wild-type value, the kcat/Km-value for the fructose-bisphosphate aldolase reaction of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) in the anabolic direction is 16fold lower than wild-type value
-
A51P
The mutation has little effect on the binding affinity of AMP, but increases the KI value. The KM value is unchanged.
D118A
mutant tetramer with one wild-type subunit and three mutant subunits. Kinetic parameters similar to wild-type, kcat-value is about one-fourth that of wild-type
D121A
mutant tetramer with one wild-type subunit and three mutant subunits. Kinetic parameters similar to wild-type, kcat-value is about one-fourth that of wild-type
D68E
-
mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 8.5 for the mutant enzyme, decreased binding affinity for Mg2+ compared to wild type enzyme
D74A
-
50000fold reduced turnover number relative to wild type enzyme
D74E
-
mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 8.5 for the mutant enzyme, decreased binding affinity for Mg2+ compared to wild type enzyme, no AMP cooperativity, kinetic mechanism of AMP inhibition with respect to Mg2+ is changed from competitive to noncompetitive
D74N
-
2000fold reduced turnover number relative to wild type enzyme
E280Q
-
K+ loses the ability to activate and became a noncompetitive inhibitor
E97A
mutant tetramer with one wild-type subunit and three mutant subunits. Kinetic parameters similar to wild-type, kcat-value is about one-fourth that of wild-type
F16W
mutant FBPases exhibits identical electrophoretic mobility as FBPase isolated from pig kidney. Mutation does not affect catalytic properties significantly, except the loss of AMP cooperativity
F89W
mutant FBPases exhibits identical electrophoretic mobility as FBPase isolated from pig kidney. Mutation does not affect catalytic properties significantly
G191A
decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate and decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity, mechanism of AMP inhibition changes from competitive to noncompetitive
I10D
mutation introduces an electrostatic charge that destabilizes the R and T states. Structure and molcular dynamic simulation show that the AMP/Mg2+ and AMP/Zn2+ complexes of mutant I10D are in intermediate quaternary conformations completing 12° of the subunit-pair rotation, but the complex with Zn2+ provides an engaged loop in a near-T quaternary state. The 12° subunit-pair rotation generates close contacts involving the hinges, residues 50-57 and hairpin turns, residues 58-72, of the engaged loops. Additional subunit-pair rotation toward the T state would make such contacts unfavorable
I190T
decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity, mechanism of AMP inhibition changes from competitive to noncompetitive
K112A
site-directed mutagenesis, mutation in the AMP-binding site to eliminate AMP hydrogen bonding to amino acids in the binding pocket
K42E
decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate and decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity
K42T
decreased Km-value for fructose 1,6-diphosphate, decreased inhibition constant for fructose 1,6-diphosphate decreased Mg2+ affinity compared to the wild type enzyme. The 50% inhibiting concentration of AMP is increased over 2000fold relative to the wild type enzyme, loss of AMP cooperativity, mechanism of AMP inhibition changes from competitive to noncompetitive
K50P
The mutation has little effect on the binding affinity of AMP, but increases the KI value. The KM value is unchanged, but 40fold loss if specific activity in comparison of wild-type enzyme, the Hill coefficients of Mg2+ are significantly reduced
K50P/Y57W
the KI value of AMP is increased, the mutant displays a biphasic bahavior toward AMP, the KM value is unchanged
K71A
-
mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 7.5 for the mutant enzyme
K71M/K72M
-
mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 7.5 for the mutant enzyme, 175fold increased inhibition constant for AMP, 2fold increased affinity for Mg2+
L56A
site-directed mutagenesis, interfacial mutant, that displays an about 5fold increased Ki for D-fructose 2,6-bisphosphate compared to wild-type
L73A
site-directed mutagenesis, interfacial mutant, that displays an about 5fold increased Ki for D-fructose 2,6-bisphosphate compared to wild-type
M177A
site-directed mutagenesis, the mutant data correlates with clinical data
M248D
site-directed mutagenesis, active site mutant, that displays an about 7fold increase in Ki for D-fructose 2,6-bisphosphate, a 4fold decrease in its apparent Km, and a 6fold increase in catalytic efficiency as compared to wild-type. The M248 residue is mutated to aspartic acid in an attempt to activate the enzyme as a means to enhance its binding affinity to the activating metals manganese and magnesium
N64A
-
mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 8.5 for the mutant enzyme, decreased binding affinity for Mg2+ compared to wild type enzyme, no AMP cooperativity, kinetic mechanism of AMP inhibition with respect to Mg2+ is changed from competitive to noncompetitive
N64Q
-
mutation shifts the pH-optimum from pH 7.0 for the wild type enzyme to pH 8.5 for the mutant enzyme, decreased binding affinity for Mg2+ compared to wild type enzyme
Q32L
decreased Km-value for fructose 1,6-diphosphate and decreased inhibition constant for fructose 1,6-diphosphate compared to the wild type enzyme. 1.7fold increase in turnover number, 8fold increase in Mg2+ affinity. 8fold increase in 50% inhibiting concentration of AMP
R49C
-
less thermostable than wild type enzyme, wild type values for turnover number and Km-value
R49D
-
less thermostable than wild type enzyme, wild type values for turnover number and Km-value, increased inhibition constant for fructose 2,6-diphosphate. Mechanism of AMP inhibition with respect to fructose 1,6-diphosphate changes from noncompetitive, wild type, to competitive. Mechanism of AMP inhibition with respect to fructose 1,6-diphosphate changes from noncompetitive, wild type, to uncompetitive. Loss of AMP cooperativity
R49L
-
less thermostable than wild type enzyme, wild type values for turnover number and Km-value, increased inhibition constant for fructose 2,6-diphosphate. Mechanism of AMP inhibition with respect to fructose 1,6-diphosphate changes from noncompetitive, wild type, to competitive. Loss of AMP cooperativity
R49M
-
enzyme is more thermostable than wild type enzyme, kinetic properties are similar to the wild type enzyme. Loss of AMP cooperativity
Y113A
site-directed mutagenesis, mutation in the AMP-binding site to eliminate AMP hydrogen bonding to amino acids in the binding pocket
Y164A
site-directed mutagenesis, the mutant data correlates with clinical data
D198H
more than 10fold reduction in kcat value, reduction in IC50 value of AMP
D200A
simultaneous decrease in substrate affinity and kcat value
D97A
almost complete loss of activity
E100A
almost complete loss of activity
E225A
almost complete loss of activity
E57A
almost complete loss of activity
F309A
greatly reduced activity
H215A
greatly reduced activity
K134A
greatly reduced activity, reduction in IC50 value of AMP
K29A
2fold increase in activity
N213A
greatly reduced activity
R164A
greatly reduced activity
R176A
simultaneous decrease in substrate affinity and kcat value
R178G
greatly reduced activity
R307A
greatly reduced activity
R314A
greatly reduced activity
T102A
more than 10fold reduction in kcat value, reduction in IC50 value of AMP
Y131A
greatly reduced activity
D32E
-
site-directed mutagenesis, binding energy of the mutant to AMP is improved, the Ki for AMP is increased in the mutant compared to wild-type enzyme. The mutant shows reduced Km for substrate D-fructose 1,6-bisphosphate compared to wild-type
F33L
-
site-directed mutagenesis, the Ki for AMP is increased in the mutant compared to wild-type enzyme. The mutant shows reduced Km for substrate D-fructose 1,6-bisphosphate compared to wild-type
R30T
-
site-directed mutagenesis, the mutant shows increased Km for substrate D-fructose 1,6-bisphosphate compared to wild-type
R30T/D32E
-
site-directed mutagenesis, the Ki for AMP is increased in the mutant compared to wild-type enzyme. The mutant shows increased Km for substrate D-fructose 1,6-bisphosphate compared to wild-type
R30T/D32E/F33L
-
site-directed mutagenesis, docking analysis of the mutant shows that the replaced Thr30 forms a hydrogen bond with AMP. The mutant shows increased Km for substrate D-fructose 1,6-bisphosphate compared to wild-type
R30T/F33L
-
site-directed mutagenesis, the mutant shows increased Km for substrate D-fructose 1,6-bisphosphate compared to wild-type
G164S

-
site-directed mutagenesis, the mutant no longer inhibits insulin stimulated AKT phosphorylation
G164S
site-directed mutagenesis, inactive mutant
K274L

-
site-directed mutagenesis, active site mutant. The residue K274 is very important for AMP analogue TNP-AMP to bind to the active site of FBPase
K274L
-
equivalent activity to the wild-type enzyme. Wild-type and mutant FBPases behaved identically throughout expression and purification. When the residue K274 is mutated to L274, 2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate can not bind to the active site, but can bind to the allosteric site
N213K

-
site-directed mutagenesis, the mutant no longer inhibits insulin stimulated AKT phosphorylation
N213K
site-directed mutgenesis, the mutant almost completely loses its binding with IkappaBalpha, the FBP1 mutation disrupts FBP1/IkappaBalpha interaction and enhances NF-kappaB activation. But FBP1 mutant N213K ha similar F-1,6-BP binding affinity and gluconeogenic activity compared to FBP1 wild-type
N213K
site-directed mutgenesis, the interaction of the mutant enzyme aand Ikappa Balpha is unaltered compared to wild-type
T84A

site-directed mutagenesis, the codon ACC for Thr84 is replaced by GCA for alanine, the active site mutant shows fully abolished enzyme activity while retaining substrate binding affinity
T84A
site-directed mutagenesis, catalytically inactive active-site mutant
T84A
inactive mutant enzyme
T84A
mutantion fully abolishes enzyme activity while retaining substrate binding affinity
T84S

site-directed mutagenesis, the codon ACC for Thr84 is replaced by AGC for serine, the active site mutant retains some activity having a 10times reduction in Vmax and exhibit similar sensitivity to lithium when compared to the wild-type enzyme
T84S
site-directed mutagenesis, active-site mutant, the mutant shows reduced activity compared to wild-type. One Mg2+ ion is found in T84S MtFBPaseII, coordinated to a glycerol molecule and to Asp79, Asp82, and Glu208 near the cleaved 1-phosphate group of the substrate
T84S
lower catalytic activity than wild-type enzyme
T84S
mutantion retains some activity having a 10 times reduction in Vmax and exhibits similar sensitivity to lithium when compared to the wild-type enzyme. Homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type enzyme by Ser84 results in subtle alterations of the position and orientation that reduces the catalytic efficiency. This mutant can be used to trap reaction intermediates, through crystallographic methods, facilitating the design of potent inhibitors via structure-based drug design
T84A

-
site-directed mutagenesis, the codon ACC for Thr84 is replaced by GCA for alanine, the active site mutant shows fully abolished enzyme activity while retaining substrate binding affinity
-
T84A
-
mutantion fully abolishes enzyme activity while retaining substrate binding affinity
-
T84A
-
site-directed mutagenesis, catalytically inactive active-site mutant
-
T84S

-
site-directed mutagenesis, the codon ACC for Thr84 is replaced by AGC for serine, the active site mutant retains some activity having a 10times reduction in Vmax and exhibit similar sensitivity to lithium when compared to the wild-type enzyme
-
T84S
-
mutantion retains some activity having a 10 times reduction in Vmax and exhibits similar sensitivity to lithium when compared to the wild-type enzyme. Homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type enzyme by Ser84 results in subtle alterations of the position and orientation that reduces the catalytic efficiency. This mutant can be used to trap reaction intermediates, through crystallographic methods, facilitating the design of potent inhibitors via structure-based drug design
-
T84S
-
site-directed mutagenesis, active-site mutant, the mutant shows reduced activity compared to wild-type. One Mg2+ ion is found in T84S MtFBPaseII, coordinated to a glycerol molecule and to Asp79, Asp82, and Glu208 near the cleaved 1-phosphate group of the substrate
-
T84A

-
site-directed mutagenesis, the codon ACC for Thr84 is replaced by GCA for alanine, the active site mutant shows fully abolished enzyme activity while retaining substrate binding affinity
-
T84A
-
mutantion fully abolishes enzyme activity while retaining substrate binding affinity
-
T84S

-
site-directed mutagenesis, the codon ACC for Thr84 is replaced by AGC for serine, the active site mutant retains some activity having a 10times reduction in Vmax and exhibit similar sensitivity to lithium when compared to the wild-type enzyme
-
T84S
-
mutantion retains some activity having a 10 times reduction in Vmax and exhibits similar sensitivity to lithium when compared to the wild-type enzyme. Homology modeling using the Escherichia coli enzyme structure suggests that the replacement of the critical nucleophile OH- in the Thr84 residue of the wild-type enzyme by Ser84 results in subtle alterations of the position and orientation that reduces the catalytic efficiency. This mutant can be used to trap reaction intermediates, through crystallographic methods, facilitating the design of potent inhibitors via structure-based drug design
-
C155S

-
mutant is active
C155S
-
lowest Mg2+ requirement, when the regulatory site disulfide is opened by mutation, in comparison to wild-type enzyme and mutant C179S
C174S

-
mutant is active and can be inactivated by oxidation
C174S
-
lowest Mg2+ requirement, when the regulatory site disulfide is opened by mutation, in comparison to wild-type enzyme and mutant C179S
C179S

-
mutant is inactive
C179S
-
mutant significantly decreases the Mg2+ requirement of the oxidized enzyme, mutant is more easily activated by thioredoxin f in comparison to wild-type enzyme
F219W

mutant FBPases exhibits identical electrophoretic mobility as FBPase isolated from pig kidney. Mutation does not affect catalytic properties significantly
F219W
-
mutation introduced to allow for fluorescence measurements. At concentrations near the Km value, the substrate fructose 1,6-bispohosphate causes a 15% increase in the intrinsic fluorescence of the mutant
F232W

mutant FBPases exhibits identical electrophoretic mobility as FBPase isolated from pig kidney. Mutation does not affect catalytic properties significantly
F232W
-
mutation introduced to allow for fluorescence measurements. The fluorescence emission of the mutant is not altered significantly by the substrate
M251L

-
site-directed mutagenesis, the mutant shows enhanced substrate affinity and activity compared to wild-type, resulting from decreased binding energy and molecular distance
M251L
-
site-directed mutagenesis, the mutant shows reduced Km for substrate D-fructose 1,6-bisphosphate compared to wild-type
N218Y

-
site-directed mutagenesis
N218Y
-
site-directed mutagenesis, the mutant shows reduced Km for substrate D-fructose 1,6-bisphosphate compared to wild-type
additional information

-
reduction of expression level by corresponding Pisum sativum antisense construct. Reduction of foliar enzyme activity in transformants T2and T3 generation ranges from 20% to 42% and correlates with lower levels of protein. Antisense plants display different phenotypes with a clear increase in leaf fresh weight, a shift in sucrose-to-starch ratio reaching a maximum of 0.99
additional information
-
fusion of C-terminal half of Beta vulgaris with C-terminal half of Pisum sativum enzyme, or insertion of cysteine-rich light regulatory sequence of Pisum sativum enzyme into corresponding site of Beta vulgaris enzyme. Both mutants show a decrease in pH-optimum, decrease in sensitivity to AMP, increase in sensitivity to substrate fructose 1,6-bisphosphate and negligible activation by thioredoxin f
additional information
transgenic plants coexpressing cyFBPase and sedoheptulose-1,7-bisphosphatase (SBPase, TpFS, EC 3.1.3.37), or expressing single cyFBPase (TpF) or SBPase (TpS) have 1.77, 1.55, 1.23fold cyFBPase and 1.45, 1.12, 1.36fold SBPase activities as compared to the wild-type, respectively. Photosynthesis rates of TpF, TpS and TpFS increase 4, 20 and 25% compared with wild-type plants. The SBPase and cyFBPase positively regulate each other and function synergistically in transgenic tobacco plants. In addition, the sucrose contents of the three transgenic plants are higher than that of the wild-type plants. The starch accumulation of the TpFS and TpS plants is improved by 53 and 37%, but slightly decreased in TpF plants. Moreover, the transgenic tobacco plants harbouring SBPase and/or cyFBPase genes show improvements in their growth, biomass, dry weight, plant height, stem diameter, leaf size, flower number, and pod weight. Phenotypes, detailed overview
additional information
silencing of EgFBPaseIII by RNAi
additional information
-
silencing of EgFBPaseIII by RNAi
additional information
EgFBPaseI gene suppression by by RNAi gene silencing
additional information
EgFBPaseI gene suppression by by RNAi gene silencing
additional information
-
EgFBPaseI gene suppression by by RNAi gene silencing
additional information
EgFBPaseII gene suppression by by RNAi gene silencing
additional information
EgFBPaseII gene suppression by by RNAi gene silencing
additional information
-
EgFBPaseII gene suppression by by RNAi gene silencing
additional information
-
silencing of EgFBPaseIII by RNAi
-
additional information
-
EgFBPaseI gene suppression by by RNAi gene silencing
-
additional information
-
EgFBPaseII gene suppression by by RNAi gene silencing
-
additional information
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fusion of C-terminal half of Beta vulgaris with C-terminal half of Pisum sativum enzyme, or insertion of cysteine-rich light regulatory sequence of Pisum sativum enzyme into corresponding site of Beta vulgaris enzyme. Both mutants show a decrease in pH-optimum, decrease in sensitivity to AMP, increase in sensitivity to substrate fructose 1,6-bisphosphate
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deletion of the first and the first two N-terminal amino acids of FBPase affects neither the kinetic properties of the enzyme not its association with aldolase. The kinetic properties of the mutant with deletion of the first three N-terminal amino acids are entirely the same as these of the wild-type muscle enzyme, its affinity to aldolase is significanltly reduced. The same affinity reduction is observed for the FPase construct lacking the first four N-terminal residues. This protein shows a slight perturbation of its kinetics, a lower sensitivity to inhibition by AMP and a little weaker activation by Mg2+
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transgenic mouse lines overexpressing huFBPase gene specifically in pancreatic islet beta-cells are generated to determine whether a specific increase in islet beta-cell FBPase can result in reduced glucose-mediated insulin secretion. FBPase transgenic mice show reduced insulin secretion in response to an intravenous glucose bolus. Pancreatic beta-cell lines (MIN6) stably overexpressing huFBPase show a decreased cell proliferation rate and significantly depressed glucose-induced insulin secretion. These defects are associated with a decrease in the rate of glucose utilization, resulting in reduced cellular ATP levels
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to determine the role of upregulated liver FBPase in glucose homeostasis human liver FBPase transgenic mice under the control of the transthyretin promoter are generated, expressing the transgene specifically in liver. Hemizygous transgenic mice have an approximately 3fold increase in total liver FBPase mRNA with concomitant increases in FBPase protein and enzyme activity levels. After high-fat feeding, hemizygous transgenics are glucose intolerant compared to wild-type. Homozygous chow-fed transgenic mice show a 5.5fold increase in liver FBPase levels and are glucose intolerant with a significantly higher rate of endogenous glucose production
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deletion of first 7 N-terminal amino acids of isoform FBP2 markedly impairs colocalization of the enzyme with mitochondria in the presence of GSK3 inhibitor. Deletion of the next 3 residues further enhanced this effect
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genetic silencing of fructose-1,6-bisphosphatase (FBP1), FBP1 downregulation enhances the activity of Wnt/beta-catenin pathway and increases the level of its downstream targets, including c-Myc and MMP7
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genetic silencing of fructose-1,6-bisphosphatase (FBP1), FBP1 downregulation enhances the activity of Wnt/beta-catenin pathway and increases the level of its downstream targets, including c-Myc and MMP7
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ectopically expressed wild-type enzyme and catalytically inactive FBP1E98A interact with AKT1, AKT2, ALDOB and PP2A-C in 293T cells, and ectopic ALDOB IPs contains endogenous AKT1 and FBP1. Likewise, ectopic PP2A-C interacts with AKT1 and FBP1, which enhances the AKT1-PP2A-C interaction. Ectopic wild-type enzyme or FBP1E98A expression in Huh7 cells potentiates the interaction between AKT, ALDOB and PP2A-C, but FBP1 or ALDOB silencing disrupts the interactions between AKT, PP2A-C, ALDOB and FBP1. In addition to deletion and nonsense mutations that block FBP1 expression, human FBP1 deficiency can be caused by missense mutations. Construction of FBP1 deletion mutants, DELTE1-DELTAE7, each lacking one FBP1 exon (E). DELTAE6 and DELTAE7 do not bind AKT nor inhibit its activity and DELTAE7 does not interact with PP2A-C, DELTAE1 is only defective in ALDOB binding
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ectopically expressed FBP2 in five STS cell lines and examined glucose metabolism. FBP2 significantly decreases glucose uptake and lactate secretion without affecting glutamine uptake in LPS224, LPS246, T1000, HT1080, and KP250 cells cultured in 10 mM glucose. Upon wild-type FBP2 and mutant FBP2G260R expression at comparable levels in LPS246 cells, FBP2G260R inhibits cell growth, although to a lesser extent than wild-type FBP2, implying that FBP2 has catalytic activity-independent cellular functions
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alterations of two residues at the subunit interfaces (Tyr164 and Met177) result in increased responsiveness to AMP. ENzyme inactivation by displacement of a loop in the active site. This loop is critical for catalysis and its movement away from the substrate binding site renders the enzyme less active
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enzyme null-mutant, unable to grow in the absence of hexose, null mutant promastigotes are internalized by macrophages and differentiate into amastigotes but are unable to replicate in the macrophage phagolysosome. Mutant persists in mice but fails to generate normal lesions
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generation of hepatocyte-specific Fbp1 knockout mice (Fbp1DELTAHep) by crossing Fbp1F/F and Alb-Cre mice. Fasted Fbp1DELTAHep mice are phenotypically and metabolically identical to starved FBP1-deficient infants. In addition to low glycogen stores and severe hypoglycemia, these mice manifest fasting-induced liver pathologies, including hepatomegaly, hepatosteatosis and hyperlipidemia. Mutant phenotype, overview. Despite hypoglycemia, the Fbp1DELTAHep livers contain more NADPH, ATP, and acetyl-CoA, which support lipid synthesis, than Fbp1F/F livers. No genotype-related differences in serum insulin or glucagon are observed in the fast state, although serum lactate is elevated in fasted Fbp1DELTAHep mice. Fasted Fbp1DELTAHep mice exhibit enhanced AKT-mTOR signaling and de novo lipogenesis. AKT IPs from Fbp1F/F or Fbp1DELTAHep livers reconstituted with wild-type FBP1 or inactive mutant FBP1E98A contain FBP1, ALDOB and PP2A-C. Similar results are obtained when AKT is IP'ed from primary mouse hepatocytes, in which the absence of FBP1 diminishes the association of AKT with ALDOB and PP2A-C, indicating that FBP1 plays a pivotal role in complex formation. Fbp1DELTAHep mice are hyperresponsive to insulin. Construction of a human synthetic E7 peptide, encompassing FBP1 AA 275 to 300 preceded by a TAT-derived cell penetrating peptide. The synthetic FBP1 E7 peptide injected into HFD-fed BL6 mice reduces the association of PP2A-C with FBP1, AKT1 and ALDOB, as well as the AKT-PP2A-C, AKT-FBP1 and FBP1-PP2A-C interactions, but has no effect on the FBP1-ALDOB interaction, which is mediated by FBP1 E1
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generation of FBP2 KO mice, Fbp2 KO mice are backcrossed with the C57BL/6J strain over five generations, phenotype, overview. Fbp2 KO mice show slight but significantly lower body weight than wild-type mice, which is mostly accounted for by decreased lean body mass, as measured by 1H-NMR. Indeed, the weight of several skeletal muscles is significantly reduced in KO mice compared to that in wild-type mice, and the decreased muscle mass is associated with reduced locomotor activity. Fbp2 deletion does not alter glucose metabolism during the feeding condition. Cold exposure does not accelerate the glycogenolysis rate by Fbp2 deletion. But there is a decrease in the basal glycogen content in the quadriceps muscle from overnight-fasted KO mice even at room temperature (22°C). Reduced glycogen content in KO mouse muscle
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generation of FBP2 KO mice, Fbp2 KO mice are backcrossed with the C57BL/6J strain over five generations, phenotype, overview. Fbp2 KO mice show slight but significantly lower body weight than wild-type mice, which is mostly accounted for by decreased lean body mass, as measured by 1H-NMR. Indeed, the weight of several skeletal muscles is significantly reduced in KO mice compared to that in wild-type mice, and the decreased muscle mass is associated with reduced locomotor activity. Fbp2 deletion does not alter glucose metabolism during the feeding condition. Cold exposure does not accelerate the glycogenolysis rate by Fbp2 deletion. But there is a decrease in the basal glycogen content in the quadriceps muscle from overnight-fasted KO mice even at room temperature (22°C). Reduced glycogen content in KO mouse muscle
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OscFBP1 mutants (mutant allele oscfbp1-1 containing a Tos17 insertion in the second exon, and mutant allele oscfbp1-2 harbouring a T-DNA insertion in the third intron) exhibit markedly decreased photosynthetic rates and severe growth retardation with reduced chlorophyll content, which results in plant death. Analysis of primary carbon metabolites reveals both significantly reduced levels of sucrose, glucose, fructose and starch in leaves of these mutants, and a high accumulation of sucrose to starch in leaves of rice plants. In the oscfbp1 mutants, products of glycolysis and the TCA cycle are significantly increased. A partitioning experiment of 14C-labelled photoassimilates reveals altered carbon distributions including a slight increase in the insoluble fraction representing transitory starch, a significant decrease in the neutral fraction corresponding to soluble sugars and a high accumulation of phosphorylated intermediates and carboxylic acid fractions in the oscfbp1 mutants
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overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
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Picosynechococcus sp. PCC 7002 ATCC 27264
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overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
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Picosynechococcus sp. PCC 7002 PR-6
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overexpression of bifunctional fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase (BiBPase) alters the carbon partitioning to extracellular carbohydrate. It induces carbohydrate partitioning which is significantly different from that in the wild-type and more towards extracellular carbohydrate and less towards glycogen. The activities of aldolase and ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) are enhanced by overexpression of BiBPase compared to wild-type, while glucose 6-phosphate dehydrogenase activity is decreased. Overexpression of BiBPase leads to enhanced cell size and photosynthetic O2 evolution. Overexpression of BiBPase in Synechococcus sp. PCC 7002 confers faster growth under elevated [CO2] and light conditions, but not under conditions where the amount of either light or CO2 is limiting
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enzyme deletion mutant, reduced sensitivity to alkylating agent methymethane sulfonate and reduced production of reactive oxygen species. Overexpression of enzyme increases sensitivity to methymethane sulfonate, shortens life span and increases induction of RNR2 gene
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to avoid the decrease in accumulation of a foreign protein in the chloroplasts caused by excess expression of FBP/SBPase for enhancing plant growth, transplastomic tobacco plants are generated carrying a S.7942 fbp/sbp transgene with a different promoter in the plastid genome. Analyses of the photosynthetic parameters and the metabolites of transformants indicates that a 2 to 3fold increase in levels of FBPase and SBPase activity is sufficient to increase the final amount of dry matter by up to 1.8fold relative to the wild-type plants
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to avoid the decrease in accumulation of a foreign protein in the chloroplasts caused by excess expression of FBP/SBPase for enhancing plant growth, transplastomic tobacco plants are generated carrying a S.7942 fbp/sbp transgene with a different promoter in the plastid genome. Analyses of the photosynthetic parameters and the metabolites of transformants indicates that a 2 to 3fold increase in levels of FBPase and SBPase activity is sufficient to increase the final amount of dry matter by up to 1.8fold relative to the wild-type plants
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a mutant defective in photoautotrophic growth is isolated from a random insertion mutant library. The interrupted gene is identified to be slr2094 (fbp1), which encodes the FBPase/sedoheptulose-1,7-biphosphatase bifunctional enzyme. Two other independently constructed slr2094 mutants by targeted insertion show an identical phenotype. The FBPase activity is found to be virtually lacking in an slr2094 mutant, which is sensitive to light under mixotrophic growth conditions
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a Yarrowia lipolytica strain with two different disrupted versions of YlFBP1 is constructed. The mutant strain grows much slower than the wild type in gluconeogenic carbon sources but growth is not abolished due to the existance of an alternative phosphatase with a high Km for fructose-1,6-bisphosphate
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a Yarrowia lipolytica strain with two different disrupted versions of YlFBP1 is constructed. The mutant strain grows much slower than the wild type in gluconeogenic carbon sources but growth is not abolished due to the existance of an alternative phosphatase with a high Km for fructose-1,6-bisphosphate
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