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2 acetaldehyde
5-deoxy-D-threo-2-pentulose
2 butyraldehyde
5,6,7-trideoxy-D-threo-2-heptulose
2 D-glyceraldehyde
D-fructose
-
-
yield 60%
-
?
2 pentanaldehyde
5,6,7,8-tetradeoxy-D-threo-2-octulose
2 propionaldehyde
5,6-dideoxy-D-threo-2-hexulose
5-fluoro-5-deoxy-D-ribulose 1-phosphate
fluoroacetaldehyde + dihydroxyacetone phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde 3-phosphate
aldolase is involved in the metabolism of fructose, converting fructose 1-phosphate to dihydroxyacetone phosphate and glyceraldehyde
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
D-fructose 6-phosphate
D-glyceraldehyde 3-phosphate + dihydroxypropanone
-
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
D-fructose-1,6-bisphosphate
glyceraldehyde-3-phosphate + dihydroxyacetone phosphate
-
-
-
-
r
D-glyceraldehyde 3-phosphate + glycerone phosphate
tagatose-1,6-bisphosphate
D-Xylulose 1-phosphate
?
-
110% of the activity with fructose 1,6-diphosphate
-
-
?
dihydroxyacetone + phenyl [(2R)-1-oxopropan-2-yl]carbamate
phenyl [(2R,3R,4S)-3,4,6-trihydroxy-5-oxohexan-2-yl]carbamate
-
i.e. (S)-N-Cbz-alaninal,substrate only for mutant A129S/A165G
aldol adduct is a key intermediates for the expedient synthesis of the pyrrolidine type iminocyclitol, 2,5-imino-1,2,5-trideoxy-D-mannitol
-
?
dihydroxyacetone + phenyl [(2S)-1-oxopropan-2-yl]carbamate
phenyl [(2S,3R,4S)-3,4,6-trihydroxy-5-oxohexan-2-yl]carbamate
-
i.e. (S)-N-Cbz-alaninal, substrate only for mutant A129S/A165G
aldol adduct is a key intermediates for the expedient synthesis of the pyrrolidine type iminocyclitol, 2,5-imino-1,2,5-trideoxy-D-glucitol
-
?
dihydroxyacetone phosphate
?
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate
Glycerone phosphate + D-glyceraldehyde
Fructose 1-phosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
hydroxyacetone + phenoxyacetaldehyde
?
-
substrate only for mutant A129S/A165G
-
-
?
hydroxyacetone + phenyl (2-oxoethyl)carbamate
?
-
substrate only for mutant A129S/A165G
-
-
?
hydroxyacetone + phenyl (3-oxopropyl)carbamate
?
-
substrate only for mutant A129S/A165G
-
-
?
hydroxyacetone + phenyl [(2R)-1-oxopropan-2-yl]carbamate
phenyl [(2R,3R,4S)-3,4-dihydroxy-5-oxohexan-2-yl]carbamate
-
substrate only for mutant A129S/A165G
-
-
?
hydroxyacetone + phenyl [(2S)-1-oxopropan-2-yl]carbamate
phenyl [(2S,3R,4S)-3,4-dihydroxy-5-oxohexan-2-yl]carbamate
-
substrate only for mutant A129S/A165G
-
-
?
L-glyceraldehyde
L-sorbose
-
-
yield 28%
-
?
L-glyceraldehyde 3-phosphate + butanone
(2S,3S)-2,3-dihydroxy-5-oxoheptyl phosphate
-
-
-
?
L-glyceraldehyde 3-phosphate + cyclopentane
(2S,3S)-2,3-dihydroxy-3-(2-oxocyclopentyl)propylphosphate
-
-
-
?
L-glyceraldehyde 3-phosphate + ethanol
2-deoxy-5-O-phosphono-L-threo-pentose
-
-
-
?
L-glyceraldehyde 3-phosphate + propanone
1,3-dideoxy-6-O-phosphono-L-threo-hex-2-ulose
-
-
-
?
propanal + dihydroxyacetone phosphate
?
-
-
-
?
sedoheptulose 1,7-bis-phosphate
?
-
-
-
-
?
sedoheptulose 1,7-bis-phosphate
glycerone phosphate + D-erythrose 4-phosphate
sedoheptulose 1,7-bisphosphate
?
-
-
-
?
sedoheptulose 1,7-bisphosphate
glycerone phosphate + D-erythrose 4-phosphate
sedoheptulose 7-phosphate
?
additional information
?
-
2 acetaldehyde
5-deoxy-D-threo-2-pentulose
-
-
yield 29%
-
?
2 acetaldehyde
5-deoxy-D-threo-2-pentulose
-
-
yield 33%
-
?
2 butyraldehyde
5,6,7-trideoxy-D-threo-2-heptulose
-
-
yield 38%
-
?
2 butyraldehyde
5,6,7-trideoxy-D-threo-2-heptulose
-
-
yield 40%
-
?
2 pentanaldehyde
5,6,7,8-tetradeoxy-D-threo-2-octulose
-
-
yield 13%
-
?
2 pentanaldehyde
5,6,7,8-tetradeoxy-D-threo-2-octulose
-
-
yield 23%
-
?
2 propionaldehyde
5,6-dideoxy-D-threo-2-hexulose
-
-
yield 34%
-
?
2 propionaldehyde
5,6-dideoxy-D-threo-2-hexulose
-
-
yield 37%
-
?
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
Anacystis sp.
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
Chlamydomonas sp.
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
ir
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
rate of reaction to form the Schiff-base intermediate is faster than ring-opening in solution
-
ir
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
Listeria monocytogenes Murray B
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?, r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
100% activity
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
100% activity
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
100% activity
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
100% activity
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
preferred substrate, reaction intermediate is Schiff base
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?, r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?, r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
high stereoselectivity for both newly created asymmetric centers
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
a combined quantum mechanics and molecular mechanics (QM/MM) method is used to study the mechanism of the enzme. The whole reaction process can be divided into seven steps. The calculations demonstrat the formation of the Schiff intermediate in the . The rate-limiting step undergoes a concerted mechanism, in which the formation of C3-C4 bond of D-fructose 1,6-bisphosphate and proton transfer from Tyr229 occurs simultaneously
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
a combined quantum mechanics and molecular mechanics (QM/MM) method is used to study the mechanism of the enzme. The whole reaction process can be divided into seven steps. The calculations demonstrat the formation of the Schiff intermediate in the . The rate-limiting step undergoes a concerted mechanism, in which the formation of C3-C4 bond of D-fructose 1,6-bisphosphate and proton transfer from Tyr229 occurs simultaneously
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
preferred substrate, reaction intermediate is Schiff base
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
enzyme uses a Schiff-base mechanism
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?, r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
preferred substrate
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
preferred substrate
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
preferred substrate
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
preferred substrate
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
r
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
at 3.5% of the activity with fructose 1,6-diphosphate
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
the D-fructose 1,6-bisphosphate/D-fructose 1-phosphate cleavage ratio is 55:1
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
5% of the activity with fructose 1,6-diphosphate
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
recombinant enzyme: 7.4% of the activity with fructose 1,6-diphosphate
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
99% of the activity with fructose 1,6-diphosphate
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
at 2.5% of the activity with fructose 1,6-diphosphate
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
muscle-type enzyme: at 3% of the activity with fructose 1,6-diphosphate
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
non-muscle-type enzyme: at about 23% of the activity with fructose 1,6-diphosphate
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
at 2% of the activity with fructose 1,6-diphosphate
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
no activity
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
at 25% of the activity with fructose 1,6-diphosphate
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
r
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
at 15% of the activity with fructose 1,6-diphosphate
-
-
?
D-Fructose 1-phosphate
Glycerone phosphate + D-glyceraldehyde
-
-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
r
D-glyceraldehyde 3-phosphate + glycerone phosphate
tagatose-1,6-bisphosphate
-
-
-
?
D-glyceraldehyde 3-phosphate + glycerone phosphate
tagatose-1,6-bisphosphate
-
-
-
?
dihydroxyacetone phosphate
?
-
-
-
-
?
dihydroxyacetone phosphate
?
-
-
-
-
?
dihydroxyacetone phosphate
?
-
-
-
-
?
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate
-
-
-
r
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate
-
-
-
r
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate
-
-
-
r
dihydroxyacetone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate
-
-
-
-
r
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
Anacystis sp.
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
r
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
r
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
Chlamydomonas sp.
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
aldol synthesizing activity is only 1.5% of fructose 1,6-diphosphate cleavage
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
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
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
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
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
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
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
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
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
-
r
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
the bifunctional enzyme also shows activity of EC 3.1.3.11. 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
-
-
r
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
a combined quantum mechanics and molecular mechanics (QM/MM) method is used to study the mechanism of the enzme. The whole reaction process can be divided into seven steps. The calculations demonstrat the formation of the Schiff intermediate in the . The rate-limiting step undergoes a concerted mechanism, in which the formation of C3-C4 bond of D-fructose 1,6-bisphosphate and proton transfer from Tyr229 occurs simultaneously
-
-
r
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
the bifunctional enzyme also shows activity of EC 3.1.3.11. 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
-
-
r
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
a combined quantum mechanics and molecular mechanics (QM/MM) method is used to study the mechanism of the enzme. The whole reaction process can be divided into seven steps. The calculations demonstrat the formation of the Schiff intermediate in the . The rate-limiting step undergoes a concerted mechanism, in which the formation of C3-C4 bond of D-fructose 1,6-bisphosphate and proton transfer from Tyr229 occurs simultaneously
-
-
r
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
-
-
-
?
sedoheptulose 1,7-bis-phosphate
glycerone phosphate + D-erythrose 4-phosphate
-
-
-
-
?
sedoheptulose 1,7-bis-phosphate
glycerone phosphate + D-erythrose 4-phosphate
-
-
-
-
?
sedoheptulose 1,7-bis-phosphate
glycerone phosphate + D-erythrose 4-phosphate
-
-
-
-
?
sedoheptulose 1,7-bis-phosphate
glycerone phosphate + D-erythrose 4-phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate
glycerone phosphate + D-erythrose 4-phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate
glycerone phosphate + D-erythrose 4-phosphate
-
20% of the activity with D-fructose 1,6-diphosphate
-
-
?
sedoheptulose 1,7-bisphosphate
glycerone phosphate + D-erythrose 4-phosphate
-
-
-
?
sedoheptulose 1,7-bisphosphate
glycerone phosphate + D-erythrose 4-phosphate
-
at 59% of the activity with fructose 1,6-diphosphate
-
-
?
sedoheptulose 1,7-bisphosphate
glycerone phosphate + D-erythrose 4-phosphate
-
-
-
-
?
sedoheptulose 1,7-bisphosphate
glycerone phosphate + D-erythrose 4-phosphate
-
-
-
-
?
sedoheptulose 7-phosphate
?
-
-
-
-
r
sedoheptulose 7-phosphate
?
-
-
-
-
r
additional information
?
-
-
no substrate: fructose 1-phosphate, fructose 6-phosphate
-
-
?
additional information
?
-
no substrate: fructose 1-phosphate, fructose 6-phosphate
-
-
?
additional information
?
-
-
no substrate: fructose 1-phosphate, fructose 6-phosphate. No additional phosphates activity is observed
-
-
?
additional information
?
-
no substrate: fructose 1-phosphate, fructose 6-phosphate. No additional phosphates activity is observed
-
-
?
additional information
?
-
-
no substrate: fructose 1-phosphate, fructose 6-phosphate. No additional phosphates activity is observed
-
-
?
additional information
?
-
no substrate: fructose 1-phosphate, fructose 6-phosphate. No additional phosphates activity is observed
-
-
?
additional information
?
-
-
no substrate: fructose 1-phosphate, fructose 6-phosphate
-
-
?
additional information
?
-
no substrate: fructose 1-phosphate, fructose 6-phosphate
-
-
?
additional information
?
-
-
a trace of activity towards fructose 6-phosphate, deoxyribose 5-phosphate and ribose 5-phosphate
-
-
?
additional information
?
-
-
enzyme binds to heparin and modified heparins
-
?
additional information
?
-
-
role in glycerol biosynthesis
-
-
?
additional information
?
-
-
FBPA exhibits very low activity toward D-tagatose-1,6-bisphosphate
-
-
?
additional information
?
-
-
no activity of MJ0400-His6 is measured with 10 mM fructose-1-phosphate as a substrate. MJ0400 also acts as an 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, this indicates that MJ0400 is involved in both the carbon metabolism and the shikimate pathway in Methanocaldococcus jannaschii
-
-
?
additional information
?
-
similar to other Class II FBA, neither fructose 1-phosphate nor fructose 6-phosphate (up to 50 mM each) act as substrates for both rMtFBA
-
-
?
additional information
?
-
product glycerone phosphate is leaving first followed by dihydroxyacetone phosphate in a uni-bi kinetic scheme
-
-
?
additional information
?
-
-
product glycerone phosphate is leaving first followed by dihydroxyacetone phosphate in a uni-bi kinetic scheme
-
-
?
additional information
?
-
similar to other Class II FBA, neither fructose 1-phosphate nor fructose 6-phosphate (up to 50 mM each) act as substrates for both rMtFBA
-
-
?
additional information
?
-
-
the enzyme binds to human glu-plasminogen in a dose-dependent manner
-
-
?
additional information
?
-
-
the partitioning of EC 4.1.2.13 and other glycolytic enzymes, between the fluid and solid phases of cytoplasm can play a fundamental role in the control of glycolysis, the organization of cytoplasm, and cell motility
-
-
?
additional information
?
-
-
the enzyme is regulated by gibberellin in roots of rice seedlings. The enzyme may regulate the vacuolar H+-ATPase mediated control of cell elongation that determines root length
-
-
?
additional information
?
-
the enzyme is a plasminogen-binding protein
-
-
?
additional information
?
-
-
the enzyme is a plasminogen-binding protein
-
-
?
additional information
?
-
the enzyme is a plasminogen-binding protein
-
-
?
additional information
?
-
the enzyme is a plasminogen-binding protein
-
-
?
additional information
?
-
-
enzyme is essential for synthesis of alginate from glucose
-
-
?
additional information
?
-
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. Substrate binding residues include Tyr229, Lys232, and Tyr358
-
-
?
additional information
?
-
-
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. Substrate binding residues include Tyr229, Lys232, and Tyr358
-
-
?
additional information
?
-
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. Substrate binding residues include Tyr229, Lys232, and Tyr358
-
-
?
additional information
?
-
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. Substrate binding residues include Tyr229, Lys232, and Tyr358
-
-
?
additional information
?
-
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. Substrate binding residues include Tyr229, Lys232, and Tyr358
-
-
?
additional information
?
-
-
aldolase A specifically participates in glycolysis
-
-
?
additional information
?
-
-
aldolase B specifically participates in gluconeogenic pathway
-
-
?
additional information
?
-
-
enzyme FruA has a flexible substrate specificity and accepts various aldehydes. It is applcable for synthesis of a number of ketoses using simple aliphatic aldehydes as acceptors in a one-pot reaction system. The yields are quite similar for reactions of which acetaldehyde, propionaldehyde, and butyraldehyde are acceptors
-
-
?
additional information
?
-
-
enzyme favors D-fructose-1,6-bisphosphate as a substrate over D-fructose-1-phosphate and is unchanged between normoxia and anoxia
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-fructose 1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde 3-phosphate
aldolase is involved in the metabolism of fructose, converting fructose 1-phosphate to dihydroxyacetone phosphate and glyceraldehyde
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
D-fructose 6-phosphate
D-glyceraldehyde 3-phosphate + dihydroxypropanone
-
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
D-fructose-1,6-bisphosphate
glyceraldehyde-3-phosphate + dihydroxyacetone phosphate
-
-
-
-
r
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
additional information
?
-
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
ir
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
Listeria monocytogenes Murray B
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?, r
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
glycerone phosphate + D-glyceraldehyde 3-phosphate
-
-
-
?
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
r
D-fructose-1,6-bisphosphate
dihydroxyacetone phosphate + glyceraldehyde-3-phosphate
-
-
-
r
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
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
-
-
?
Glycerone phosphate + D-glyceraldehyde 3-phosphate
D-Fructose 1,6-bisphosphate
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
-
-
?
additional information
?
-
-
enzyme binds to heparin and modified heparins
-
?
additional information
?
-
-
role in glycerol biosynthesis
-
-
?
additional information
?
-
-
no activity of MJ0400-His6 is measured with 10 mM fructose-1-phosphate as a substrate. MJ0400 also acts as an 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, this indicates that MJ0400 is involved in both the carbon metabolism and the shikimate pathway in Methanocaldococcus jannaschii
-
-
?
additional information
?
-
-
the partitioning of EC 4.1.2.13 and other glycolytic enzymes, between the fluid and solid phases of cytoplasm can play a fundamental role in the control of glycolysis, the organization of cytoplasm, and cell motility
-
-
?
additional information
?
-
-
the enzyme is regulated by gibberellin in roots of rice seedlings. The enzyme may regulate the vacuolar H+-ATPase mediated control of cell elongation that determines root length
-
-
?
additional information
?
-
-
enzyme is essential for synthesis of alginate from glucose
-
-
?
additional information
?
-
-
aldolase A specifically participates in glycolysis
-
-
?
additional information
?
-
-
aldolase B specifically participates in gluconeogenic pathway
-
-
?
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(1E)-1-benzylidene-2-(4-nitrophenyl)hydrazine
0.05 mM, 43% inhibition; 43% inhibition at 0.05 mM
(1E)-1-[(4-chlorophenyl)methylidene]-2-(4-nitrophenyl)hydrazine
0.05 mM, 91% inhibition; 91% inhibition at 0.05 mM
(1E)-1-[(4-fluorophenyl)methylidene]-2-(4-nitrophenyl)hydrazine
0.05 mM, 94% inhibition; 94% inhibition at 0.05 mM
(1E)-1-[(4-methylphenyl)methylidene]-2-(4-nitrophenyl)hydrazine
0.05 mM, 80% inhibition; 80% inhibition at 0.05 mM
(1E)-1-[([1,1'-biphenyl]-4-yl)methylidene]-2-(4-nitrophenyl)hydrazine
0.05 mM, 92% inhibition; 92% inhibition at 0.05 mM
(1E)-1-[1-(4-bromophenyl)ethylidene]-2-(4-nitrophenyl)hydrazine
0.05 mM, 99% inhibition; 99% inhibition at 0.05 mM
(1E)-1-[1-([1,1'-biphenyl]-4-yl)ethylidene]-2-(4-nitrophenyl)hydrazine
62% inhibition at 0.05 mM
(1E)-1-[2-(4-nitrophenyl)hydrazinylidene]propan-2-one
0.05 mM, 6% inhibition; 6% inhibition at 0.05 mM
(2E)-1-(4-nitrophenyl)-2-(1-phenylethylidene)hydrazine
0.05 mM, 62% inhibition
(2E)-1-(4-nitrophenyl)-2-[(4-nitrophenyl)methylidene]hydrazine
0.05 mM, 100% inhibition; complete inhibition at 0.05 mM
(2E)-1-(4-nitrophenyl)-2-[(5-nitrothiophen-2-yl)methylidene]hydrazine
0.05 mM, 97% inhibition; 97% inhibition at 0.05 mM
(2E)-1-(4-nitrophenyl)-2-[[4-(trifluoromethyl)phenyl]methylidene]hydrazine
0.05 mM, 60% inhibition; 60% inhibition at 0.05 mM
(2E)-2-[2-(2-hydroxy-4-nitrophenyl)hydrazinylidene]-3-oxobutanamide
94% inhibition at 0.05 mM
(2E)-2-[2-(4-nitrophenyl)hydrazinylidene]-1-phenylethan-1-one
0.05 mM, 91% inhibition; 91% inhibition at 0.05 mM
([3-hydroxy-2-oxo-4-[(phosphonomethoxy)methyl]pyridin-1(2H)-yl]methyl)phosphonic acid
-
-
([3-hydroxy-2-oxo-4-[2-(phosphonooxy)ethyl]pyridin-1(2H)-yl]methyl)phosphonic acid
-
-
([3-hydroxy-4-[(1R)-1-hydroxy-2-(phosphonooxy)ethyl]-2-oxopyridin-1(2H)-yl]methyl)phosphonic acid
-
-
([3-hydroxy-4-[(1S)-1-hydroxy-2-(phosphonooxy)ethyl]-2-oxopyridin-1(2H)-yl]methyl)phosphonic acid
-
-
([4,5-dihydroxy-6-[2-(phosphonooxy)ethyl]pyridin-3-yl]methyl)phosphonic acid
-
-
1-(4-[(E)-[2-(4-nitrophenyl)hydrazinylidene]methyl]phenyl)-1H-1,2,4-triazole
0.05 mM, 83% inhibition; 83% inhibition at 0.05 mM
1-hydroxy-2-naphthaldehyde 6-phosphate
slow-binding
2,2'-bipyridyl
-
2 mM, 76% inhibition
2,2'-dipyridyl
-
aldolase class II
2,4-Dihydroxybenzaldehyde 4-phosphate
-
-
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl dihydrogen phosphate
-
-
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
2-carboxy-6-(phosphonomethyl)pyridinium chloride
2-hydroxy-2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl dihydrogen phosphate
-
-
2-oxo-2-[(phenylsulfonyl)amino]ethyl phosphate
-
-
2-propanol
at 12.5% (v/v) remaining activity, 69.99%, and 25% (v/v) remaining activity, 3.72%
2-[(methylsulfonyl)amino]-2-oxoethyl phosphate
-
-
2-[(trihydroxyphosphoranyl)oxy]acetohydrazide
2-[2-(2,4-dioxopentan-3-ylidene)hydrazinyl]-5-nitrobenzoic acid
0.05 mM, 10% inhibition; 10% inhibition at 0.05 mM
2-[2-(2,4-dioxopentan-3-ylidene)hydrazinyl]benzonitrile
0.05 mM, 16% inhibition; 16% inhibition at 0.05 mM
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
3-(2-phenylhydrazinylidene)pentane-2,4-dione
0.05 mM, 10% inhibition; 10% inhibition at 0.05 mM
3-[2-(2,4-dinitrophenyl)hydrazinylidene]pentane-2,4-dione
0.05 mM, 1% inhibition; 1% inhibition at 0.05 mM
3-[2-(2-chloro-4-nitrophenyl)hydrazinylidene]pentane-2,4-dione
0.05 mM, 68% inhibition; 68% inhibition at 0.05 mM
3-[2-(2-fluorophenyl)hydrazinylidene]pentane-2,4-dione
0.05 mM, 3% inhibition; 3% inhibition at 0.05 mM
3-[2-(2-hydroxy-4-nitrophenyl)hydrazinylidene]pentane-2,4-dione
0.05 mM, 94% inhibition; 0.05 mM, 96% inhibition; 96% inhibition at 0.05 mM
3-[2-(2-hydroxy-5-nitrophenyl)hydrazinylidene]pentane-2,4-dione
0.05 mM, 14% inhibition; 14% inhibition at 0.05 mM
3-[2-(2-hydroxyphenyl)hydrazinylidene]pentane-2,4-dione
0.05 mM, 73% inhibition; 73% inhibition at 0.05 mM
3-[2-(2-methyl-4-nitrophenyl)hydrazinylidene]pentane-2,4-dione
0.05 mM, 65% inhibition; 65% inhibition at 0.05 mM
3-[2-(2-methylphenyl)hydrazinylidene]pentane-2,4-dione
0.05 mM, 9% inhibition; 9% inhibition at 0.05 mM
3-[2-(4-bromophenyl)hydrazinylidene]pentane-2,4-dione
0.05 mM, 27% inhibition; 27% inhibition at 0.05 mM
3-[2-(4-chlorophenyl)hydrazinylidene]pentane-2,4-dione
0.05 mM, 20% inhibition; 20% inhibition at 0.05 mM
3-[2-(4-fluorophenyl)hydrazinylidene]pentane-2,4-dione
0.05 mM, 7% inhibition; 7% inhibition at 0.05 mM
3-[2-(4-hydroxyphenyl)hydrazinylidene]pentane-2,4-dione
0.05 mM, 5% inhibition; 5% inhibition at 0.05 mM
3-[2-(4-nitrophenyl)hydrazinylidene]pentane-2,4-dione
0.05 mM, 92% inhibition; 92% inhibition at 0.05 mM
3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
4-Hydroxybenzaldehyde phosphate
-
competitive
4-nitro-N'-[(E)-(4-nitrophenyl)methylidene]benzohydrazide
0.05 mM, 59% inhibition; 59% inhibition at 0.05 mM
4-[(E)-[2-(4-nitrophenyl)hydrazinylidene]methyl]benzonitrile
0.05 mM, 100% inhibition; complete inhibition at 0.05 mM
4-[2-(2,4-dioxopentan-3-ylidene)hydrazinyl]benzene-1-sulfonic acid
0.05 mM, 14% inhibition; 14% inhibition at 0.05 mM
4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
5,5'-dithiobis(2-nitrobenzoic acid)
-
1 mM, complete inhibition
5-bromo-3-[(E)-[2-(4-nitrophenyl)hydrazinylidene]methyl]-1H-indole
0.05 mM, 97% inhibition; 97% inhibition at 0.05 mM
5-chloro-8-hydroxyquinoline
non-competitive (mixed type)
5-formyl-6-hydroxynaphthalen-2-yl dihydrogen phosphate
8-hydroxyquinoline-2-carboxylic acid
mixed type inhibitor
Agaricic acid
50% inhibition at 0.03 mM
alpha-glycerophosphate
-
-
Benzene
at 12.5% (v/v) remaining activity, 88.94%, and 25% (v/v) remaining activity, 88.94%
Cd2+
1 mM, no residual activity; 1 mM, no residual activity
Cr3+
1 mM, 36% decrease of activity
CuCl2
-
1 mM, complete inhibition
D-erythrose 4-phosphate
-
competitive
D-erythrulose 1-phosphate
-
slow reversible
D-fructose 1,6-bisphosphate
substrate inhibition; substrate inhibition
D-glucitol 1,6-bisphosphate
D-hexitol-1,6-bisphosphate
-
D-mannitol 1,6-bisphosphate
D-mannitol-1,6-bisphosphate
competitive inhibitor
D-ribulose 1,5-bisphosphate
-
-
D-tagatose 1,6-bisphosphate
competitive inhibitor
dihydroxyacetone phosphate
dimethylsulfoxid
at 12.5% (v/v) remaining activity, 131.26%, and 25% (v/v) remaining activity, 133.2%
erythrose 4-phosphate
-
-
ethanol
at 12.5% (v/v) remaining activity, 79.19%, and 25% (v/v) remaining activity, 33.41%
ethyl acetate
at 12.5% (v/v) remaining activity, 71.96%, and 25% (v/v) remaining activity, 41.62%
Fluorescein 5'-isothiocyanate
results in a minimal loss of enzyme activity
glutathione
-
10 mM, 62% residual activity
glyceraldehyde 3-phosphate
glycerol
at 20% (v/v) reduced enzyme activity by 65%
Glycerol 2,3-diphosphate
-
-
hexane
at 12.5% (v/v) remaining activity, 98.25%, and 25% (v/v) remaining activity, 92.22%
hexitol-1,6-bisphosphate
-
strong competitive inhibitor
HgCl2
-
1 mM, complete inhibition
hydrogen peroxide
-
inhibitory at 0.25%, at pH 7
Hydroquinone diphosphate
-
competitive
iodoacetamide
-
76% residual activity at 10 mM
L-cysteine
-
10 mM, complete inhibition
mannitol-1,6-bis(phosphate)
competitive
N'-hydroxy-2-[(trihydroxyphosphoranyl)oxy]ethanimidamide
-
-
N'-[(E)-(4-cyanophenyl)methylidene]-4-nitrobenzohydrazide
0.05 mM, 21% inhibition; 21% inhibition at 0.05 mM
N,N-dimethylmethanamide
at 12.5% (v/v) remaining activity, 118.40%, and 25% (v/v) remaining activity, 73.93%
N-(3-hydroxypropyl)-glycolohydrazide-bisphosphate
N-(3-hydroxypropyl)-glycolohydroxamic acid bisphosphate
N-(3-hydroxypropyl)-phosphoglycolohydroxamic acid
N-(4-hydroxybutyl)-glycolohydroxamic acid bisphosphate
inhibitor attachment has no effect on the plasminogen binding activity of the enzyme but competes with the natural substrate, fructose 1,6-bisphosphate, and substantiates a reaction mechanism associated with metallodependent aldolases involving recruitment of the catalytic zinc ion by the substrate upon active site binding
N-hydroxy-2-[(trihydroxyphosphoranyl)oxy]acetamide
-
-
naphthalene-2,6-bisphosphate
-
strong competitive inhibitor
naphthyl 2,6-bisphosphate
competitive
Ni2+
-
cells stressed by 8 microM Ni(II) for 20 min lose 75% of their FbaA activity. In presence of 8 microM Ni(II), purified FbaA loses 80% of its activity within 2 min. Inhibition is due to Ni(II) binding to a secondary zinc binding site
o-phenanthroline
0.06 mM, inactivation
peroxynitrite
decrease of Vmax and KM for fructose-1,6-bisphosphate after incubation with peroxynitrite. Tyrosine residues in the carboxyl-terminal region of the aldolase are major targets of nitration. Tyrosine nitration of aldolase A can contribute to an impaired cellular glycolytic activity
phosphoglycolo hydroxamic acid
phosphoglycolo-amidoxime
-
PGA, i.e. 2-amino-2-(hydroxyimino)ethyl phosphate
phosphoglycolo-hydrazide
-
PGHz, i.e. 2-hydrazino-2-oxoethyl phosphate
Phosphoglycolohydroxamate
Resorcinol diphosphate
-
competitive
Sodium borohydride
incubation with sodium borohydride in the presence of substrate results more than 80% of decrease in aldolase activity; more than 80% of decrease in aldolase activity in the presence of substrate. Negligible decrease in aldolase activity when Pcal_0111 and sodium borohydride are incubated in the absence of the substrate; results in more than 80% of decrease in aldolase activity of Pcal_0111 in the presence of substrate, also a negligible decrease in aldolase activity is observed when Pcal_0111 and sodium borohydride are incubated in the absence of the substrate
tagatose 1,6-bisphosphate
Toluene
at 12.5% (v/v) remaining activity, 89.70%, and 25% (v/v) remaining activity, 91.02%
[(3-hydroxy-2-oxopyridin-1(2H)-yl)methyl]phosphonic acid
-
-
[2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl]phosphonic acid
-
-
[[(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)methoxy]methyl]phosphonic acid
-
-
[[3-hydroxy-2-oxo-4-(2-phosphonoethyl)pyridin-1(2H)-yl]methyl]phosphonic acid
-
-
(NH4)2SO4
-
50% inhibition at 2.1 mM at 37°C, 50% inhibition at 1.9 mM at 5°C
(NH4)2SO4
-
50% inhibition at 6.2 mM at 37°C, 50% inhibition at 5.27 mM at 5°C
1,10-phenanthroline
-
2 mM, 85% inhibition
1,10-phenanthroline
-
aldolase class II
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
-
-
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
-
-
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
-
-
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
-
-
2-(3-hydroxy-2-oxo-1,2-dihydropyridin-4-yl)ethyl phosphate
-
-
2-carboxy-6-(phosphonomethyl)pyridinium chloride
-
metal-chelating inhibitor
2-carboxy-6-(phosphonomethyl)pyridinium chloride
-
metal-chelating inhibitor
2-carboxy-6-(phosphonomethyl)pyridinium chloride
-
metal-chelating inhibitor
2-carboxy-6-(phosphonomethyl)pyridinium chloride
-
metal-chelating inhibitor
2-mercaptoethanol
-
5 mM, 19% loss of activity
2-mercaptoethanol
-
10 mM, 38% residual activity
2-[(trihydroxyphosphoranyl)oxy]acetohydrazide
-
-
2-[(trihydroxyphosphoranyl)oxy]acetohydrazide
-
-
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
2-[hydroxy(3-hydroxypropyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
2-[hydroxy(4-hydroxybutyl)amino]-2-oxoethyl dihydrogen phosphate
-
-
3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
-
-
3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
-
-
3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
-
-
3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
-
-
3-[hydroxy[(phosphonooxy)acetyl]amino]propyl dihydrogen phosphate
-
-
4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
-
-
4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
-
-
4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
-
-
4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
-
-
4-[hydroxy[(phosphonooxy)acetyl]amino]butyl hexanoate
-
-
5-formyl-6-hydroxynaphthalen-2-yl dihydrogen phosphate
-
1 mM, 15 min incubation time, 80% residual activity
5-formyl-6-hydroxynaphthalen-2-yl dihydrogen phosphate
-
5 mM, 15 min incubation time, no residual activity
8-hydroxyquinoline
-
aldolase class II
ADP
1 mM, 47% residual activity; 1 mM, 58% residual activity
ADP
-
50% inhibition at 1.6 mM at 37°C, 50% inhibition at 1.7 mM at 5°C
ADP
-
50% inhibition at 2.7 mM at 37°C, 50% inhibition at 5.4 mM at 5°C
AMP
-
50% inhibition at 2.3 mM at 37°C, 50% inhibition at 2.6 mM at 5°C
AMP
-
strong allosteric inhibition. I0.5: 0.00023 mM
AMP
-
50% inhibition at 4.5 mM at 37°C, 50% inhibition at 6.0 mM at 5°C
ATP
1 mM, 34% residual activity; 1 mM, 39% residual activity
ATP
-
50% inhibition at 1.4 mM at 37°C, 50% inhibition at 1.1 mM at 5°C
ATP
-
50% inhibition at 2.1 mM at 37°C, 50% inhibition at 2.1 mM at 5°C
Borohydride
-
-
citrate
-
50% inhibition at 2.4 mM at 37°C, 50% inhibition at 1.9 mM at 5°C
citrate
-
50% inhibition at 2.7 mM at 37°C, 50% inhibition at 3.4 mM at 5°C
Cu2+
1 mM, 57% decrease of activity
Cu2+
1 mM, 3% residual activity; 1 mM, 5% residual activity
Cu2+
-
complete inhibition of aldolase II above 0.5 mM
CuSO4
-
-
CuSO4
0.02 mM, inactivation
Cys
-
-
Cys
-
inhibits aldolase II above 0.8 mM
D-glucitol 1,6-bisphosphate
competitive inhibitor
D-glucitol 1,6-bisphosphate
competitive inhibitor
D-glucitol 1,6-bisphosphate
competitive inhibitor, better inhibitor
D-mannitol 1,6-bisphosphate
competitive inhibitor, better inhibitor
D-mannitol 1,6-bisphosphate
competitive inhibitor
D-mannitol 1,6-bisphosphate
competitive inhibitor
dihydroxyacetone phosphate
-
dihydroxyacetone phosphate
competitive with fructose 1,6-bisphosphate
diphosphate
-
-
dipicolinic acid
-
metal-chelating inhibitor
dipicolinic acid
-
metal-chelating inhibitor
dipicolinic acid
-
metal-chelating inhibitor
dipicolinic acid
-
metal-chelating inhibitor
EDTA
Anacystis sp.
-
inhibition is fully reversed by a divalent metal ion
EDTA
1 mM, complete inhibition
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
-
the specific activity of the Bacillus cereus aldolase is partially restored after EDTA inactivation by Co2+ and Cd2+, as well as Zn2+, but not significantly restored by Cu2+, Mn2+, Mg2+, or Ni2+
EDTA
-
metal-chelating inhibitor
EDTA
1 mM, no residual activity; 1 mM, no residual activity
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
Chlamydomonas sp.
-
inhibition is fully reversed by a divalent metal ion
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
-
0.67 mM, complete inhibition
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
-
activity restored after addition of Zn2+, Co2+ or Mn2+
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
-
0.025 mM and above, no residual activity
EDTA
-
1 mM, 7% inhibition
EDTA
-
2 mM, complete inhibition. Activity can be completely restored only by Fe2+. Other divalent metal ions such as Mn2+, Mg2+, and Zn2+ have no effect. Co2+ and Ca2+ can restore 20% and 10%, respectively, of enzyme activity
EDTA
2 mM, complete inhibition of activity, which could be reversed by the addition of Mn2+ (3 mM)
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
complete inhibition at 1 mM
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
1 mM, completely abolishes activity
EDTA
-
the activity of the EDTA-inactivated enzyme increases more than 6fold upon the addition of 0.002 mM Zn2+ and increases by a factor 2 with the addition of 0.002 mM Co2+. The addition of Cu2+, Ni2+, Cd2+, Mn2+, or Mg2+ does not reactivate the enzyme significantly
EDTA
-
metal-chelating inhibitor
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
-
the specific activity of the recombinant Pseudomonas aeruginosa aldolase is 5.5times higher after inactivation by EDTA followed by the addition of 0.02 mM cobalt chloride, and increases more than 2fold after EDTA inactivation followed by the addition of 0.1 mM manganese(II)-chloride
EDTA
-
metal-chelating inhibitor
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
-
metal-chelating inhibitor
EDTA
-
inhibition is fully reversed by a divalent metal ion
EDTA
-
inhibition is fully reversed by a divalent metal ion
Fe2+
1 mM, 15% residual activity; 1 mM, 18% residual activity
Fe2+
-
optimum aldolase activity (137%) is observed with 1.0 mM Fe2+ concentration. Inhibition at concentrations baove 1.0 mM
glucose 1-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
glyceraldehyde 3-phosphate
non-competitive inhibitor
glycerone phosphate
-
-
glycerone phosphate
-
inhibition in presence of glycerone phosphate and NaBH4
glycerone phosphate
-
inhibition in presence of glycerone phosphate and NaBH4
glycerone phosphate
-
inhibition in presence of glycerone phosphate and NaBH4
IMP
-
50% inhibition at 1.3 mM at 37°C, 50% inhibition at 1.3 mM at 5°C
IMP
-
50% inhibition at 4.2 mM at 37°C, 50% inhibition at 8.5 mM at 5°C
iodoacetate
-
10 mM, 28% loss of activity
iodoacetate
-
1 mM, 46% inhibition
KCl
-
50% inhibition at 38.2 mM at 37°C, 50% inhibition at 36.1 mM at 5°C
KCl
-
50% inhibition at 111 mM at 37°C, 50% inhibition at 63.3 mM at 5°C
Magnesium citrate
-
50% inhibition at 1.9 mM at 37°C, 50% inhibition at 2.5 mM at 5°C
Magnesium citrate
-
50% inhibition at 9 mM at 37°C, 50% inhibition at 2.5 mM at 5°C
N-(3-hydroxypropyl)-glycolohydrazide-bisphosphate
fructose-1,6-bisphosphate analogue
N-(3-hydroxypropyl)-glycolohydrazide-bisphosphate
fructose-1,6-bisphosphate analogue
N-(3-hydroxypropyl)-glycolohydrazide-bisphosphate
fructose-1,6-bisphosphate analogue
N-(3-hydroxypropyl)-glycolohydrazide-bisphosphate
fructose-1,6-bisphosphate analogue
N-(3-hydroxypropyl)-glycolohydroxamic acid bisphosphate
fructose-1,6-bisphosphate analogue, best results
N-(3-hydroxypropyl)-glycolohydroxamic acid bisphosphate
fructose-1,6-bisphosphate analogue, weakly active
N-(3-hydroxypropyl)-glycolohydroxamic acid bisphosphate
fructose-1,6-bisphosphate analogue, best results
N-(3-hydroxypropyl)-glycolohydroxamic acid bisphosphate
fructose-1,6-bisphosphate analogue, best results
N-(3-hydroxypropyl)-phosphoglycolohydroxamic acid
fructose-1,6-bisphosphate analogue
N-(3-hydroxypropyl)-phosphoglycolohydroxamic acid
fructose-1,6-bisphosphate analogue
N-(3-hydroxypropyl)-phosphoglycolohydroxamic acid
fructose-1,6-bisphosphate analogue
N-(3-hydroxypropyl)-phosphoglycolohydroxamic acid
fructose-1,6-bisphosphate analogue
NaBH4
Chlamydomonas sp.
-
metalloaldolases are indifferent
NaBH4
-
in presence of substrate
NaBH4
-
irreversible inactivation
NaBH4
-
inhibition in presence of glycerone phosphate and NaBH4
NaBH4
-
inhibition in presence of glycerone phosphate and NaBH4
NaBH4
-
in presence of substrate
NaCl
-
50% inhibition at 14.7 mM at 37°C, 50% inhibition at 31 mM at 5°C
NaCl
-
50% inhibition at 110 mM at 37°C, 50% inhibition at 52 mM at 5°C
NH4Cl
-
50% inhibition at 51.5 mM at 37°C, 50% inhibition at 34.1 mM at 5°C
NH4Cl
-
50% inhibition at 166 mM at 37°C, 50% inhibition at 40.6 mM at 5°C
phosphate
-
50% inhibition at 1.7 mM at 37°C, 50% inhibition at 0.63 mM at 5°C
phosphate
-
50% inhibition at 6.1 mM at 37°C, 50% inhibition at 1.7 mM at 5°C
phosphoenolpyruvate
-
mixed-type inhibitor
phosphoglycolo hydroxamic acid
-
PGH, i.e. 2-(hydroxyamino)-2-oxoethyl phosphate
phosphoglycolo hydroxamic acid
-
PGH, i.e. 2-(hydroxyamino)-2-oxoethyl phosphate
phosphoglycolo hydroxamic acid
-
PGH, i.e. 2-(hydroxyamino)-2-oxoethyl phosphate
phosphoglycoloamidoxime
dihydroxyacetone phosphate analogue
phosphoglycoloamidoxime
dihydroxyacetone phosphate analogue
phosphoglycoloamidoxime
dihydroxyacetone phosphate analogue
phosphoglycoloamidoxime
dihydroxyacetone phosphate analogue
phosphoglycolohydrazide
dihydroxyacetone phosphate analogue
phosphoglycolohydrazide
dihydroxyacetone phosphate analogue
phosphoglycolohydrazide
dihydroxyacetone phosphate analogue
phosphoglycolohydrazide
dihydroxyacetone phosphate analogue
Phosphoglycolohydroxamate
-
-
Phosphoglycolohydroxamate
use as a mimic of the hydroxyenolate intermediate- and dihydroxyacetone phosphate-bound form of the enzyme
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
ribose 5-phosphate
-
-
ribose 5-phosphate
-
competitive
suramin
50% inhibition at 0.025 mM
tagatose 1,6-bisphosphate
-
-
tagatose 1,6-bisphosphate
competitive inhibitor
Zn2+
1 mM, 15% residual activity; 1 mM, 8% residual activity
Zn2+
-
complete inhibition of aldolase II above 0.5 mM
additional information
-
EDTA has no effect
-
additional information
-
-
-
additional information
-
high pH, high temperature, and ionic detergents either inhibit or prevent the reaction of fluorescein 5'-isothiocyanate with aldolase. Certain metabolites (ATP, ADP, CTP, GTP, FBP) and erythrosin B also inhibited the fluorescein 5'-isothiocyanate modification of aldolase
-
additional information
high pH, high temperature, and ionic detergents either inhibit or prevent the reaction of fluorescein 5'-isothiocyanate with aldolase. Certain metabolites (ATP, ADP, CTP, GTP, FBP) and erythrosin B also inhibited the fluorescein 5'-isothiocyanate modification of aldolase
-
additional information
-
-
-
additional information
all methyl 4-oxo-2-butenoates, 3-hydroxy-2-pyrrolones, 1,4-bezoxazines and compounds containing 4-quinolone fragment does not inhibit rMtFBA
-
additional information
the enzyme does not show any inhibition in the presence of 10 mM AMP
-
additional information
-
the enzyme does not show any inhibition in the presence of 10 mM AMP
-
additional information
-
EDTA has no effect
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.00016 - 20
D-fructose 1,6-bisphosphate
0.0017 - 40
D-Fructose 1-phosphate
0.01503 - 0.45
D-fructose-1,6-bisphosphate
0.052 - 1.17
D-glyceraldehyde 3-phosphate
0.0016
D-Xylulose 1-phosphate
-
-
0.095
dihydroxyacetone phosphate
in the absence of Co2+, at pH 7.5, 30°C
0.0036 - 0.009
fructose 1,6-bisphosphate
0.007 - 27
fructose 1-phosphate
0.065 - 2
glycerone phosphate
0.008 - 0.19
sedoheptulose 1,7-bisphosphate
0.006 - 10
sedoheptulose 1,7-diphosphate
0.0167 - 0.0195
sedoheptulose 7-phosphate
additional information
additional information
-
0.00016
D-fructose 1,6-bisphosphate
-
-
0.00018
D-fructose 1,6-bisphosphate
-
pH 7.2, 25°C, anoxic liver preparation
0.00024
D-fructose 1,6-bisphosphate
-
pH 7.2, 25°C, normoxic liver preparation
0.0003
D-fructose 1,6-bisphosphate
-
-
0.000547
D-fructose 1,6-bisphosphate
-
-
0.00065
D-fructose 1,6-bisphosphate
-
enzyme form I
0.00084
D-fructose 1,6-bisphosphate
30°C, aldolase B
0.0009
D-fructose 1,6-bisphosphate
-
pH 7.3, 37°C
0.001
D-fructose 1,6-bisphosphate
-
-
0.0011
D-fructose 1,6-bisphosphate
-
cytosolic enzyme
0.0011
D-fructose 1,6-bisphosphate
30°C, AB_All mutant
0.00113
D-fructose 1,6-bisphosphate
-
at 33°C
0.0013
D-fructose 1,6-bisphosphate
-
pH 7.3, 37°C
0.00145
D-fructose 1,6-bisphosphate
-
pH 7.3, 5°C
0.0016
D-fructose 1,6-bisphosphate
-
cytosolic enzyme
0.0016
D-fructose 1,6-bisphosphate
-
liver enzyme,
0.0017
D-fructose 1,6-bisphosphate
-
pH 7.4, 10°C, wild-type enzyme
0.0017
D-fructose 1,6-bisphosphate
-
at pH 7.5 and 25°C, in the absence of Zn2+
0.0017
D-fructose 1,6-bisphosphate
wild type enzyme, in 50 mM K+-HEPES (pH 7.5), at 25°C
0.002
D-fructose 1,6-bisphosphate
-
-
0.002
D-fructose 1,6-bisphosphate
-
cytosolic enzyme
0.002
D-fructose 1,6-bisphosphate
-
liver
0.002
D-fructose 1,6-bisphosphate
-
at pH 7.5 and 25°C
0.0023
D-fructose 1,6-bisphosphate
-
cytosolic enzyme
0.0023
D-fructose 1,6-bisphosphate
wild-type enzyme, 22°C
0.0024
D-fructose 1,6-bisphosphate
-
pH 7.4, 30°C, wild-type enzyme
0.00245
D-fructose 1,6-bisphosphate
-
5°C
0.0027
D-fructose 1,6-bisphosphate
-
mutant aldolase C Y363S
0.0028
D-fructose 1,6-bisphosphate
-
pH 7.4, 10°C, enzyme from patients with intolerance
0.0035
D-fructose 1,6-bisphosphate
-
recombinant enzyme
0.0037
D-fructose 1,6-bisphosphate
-
-
0.004
D-fructose 1,6-bisphosphate
-
wild-type, 22°C, pH 7.6
0.00405
D-fructose 1,6-bisphosphate
pH 7.5, 25°C
0.00411
D-fructose 1,6-bisphosphate
-
pH 7.3, 5°C
0.0042
D-fructose 1,6-bisphosphate
mutant enzyme D33N
0.0043
D-fructose 1,6-bisphosphate
-
-
0.0045
D-fructose 1,6-bisphosphate
at pH 7.5 and 25°C
0.0048
D-fructose 1,6-bisphosphate
-
non-muscle-type enzyme
0.005
D-fructose 1,6-bisphosphate
-
recombinant non-muscle-type enzyme
0.0051
D-fructose 1,6-bisphosphate
native wild type enzyme
0.0052
D-fructose 1,6-bisphosphate
in the presence of 0.02 mM Co2+, at substrate concentrations of 0.008-0.5 mM, at pH 7.5, 30°C
0.0055
D-fructose 1,6-bisphosphate
W147R mutant, 22°C
0.0056
D-fructose 1,6-bisphosphate
-
plastidic enzyme
0.0058
D-fructose 1,6-bisphosphate
-
cytosolic enzyme
0.0059
D-fructose 1,6-bisphosphate
-
L256P, 22°C, pH 7.6
0.006
D-fructose 1,6-bisphosphate
-
-
0.0061
D-fructose 1,6-bisphosphate
mutant enzyme E187A
0.007
D-fructose 1,6-bisphosphate
-
pH 8, class I aldolase, recombinant enzyme
0.0071
D-fructose 1,6-bisphosphate
-
-
0.0073
D-fructose 1,6-bisphosphate
L256P mutant, 22°C
0.008
D-fructose 1,6-bisphosphate
-
chloroplastic enzyme
0.008
D-fructose 1,6-bisphosphate
-
pH 7.5, class II aldolase, purified enzyme
0.008
D-fructose 1,6-bisphosphate
-
pH 7.5, class II aldolase, recombinant enzyme
0.0081
D-fructose 1,6-bisphosphate
-
-
0.0083
D-fructose 1,6-bisphosphate
-
chloroplastic enzyme
0.0084
D-fructose 1,6-bisphosphate
mutant enzyme D33S
0.0085
D-fructose 1,6-bisphosphate
-
pH 7.4, 30°C, enzyme from patients with intolerance
0.0088
D-fructose 1,6-bisphosphate
-
pH 7.6
0.0089
D-fructose 1,6-bisphosphate
-
aldolase C
0.009
D-fructose 1,6-bisphosphate
-
pH 8, class I aldolase, purified enzyme
0.0091
D-fructose 1,6-bisphosphate
-
chloroplastic enzyme
0.0091
D-fructose 1,6-bisphosphate
Q354E mutant, 22°C
0.0092
D-fructose 1,6-bisphosphate
-
pH 7.6, native enzyme
0.0095
D-fructose 1,6-bisphosphate
at 30°C
0.0095
D-fructose 1,6-bisphosphate
30°C, aldolase A
0.01
D-fructose 1,6-bisphosphate
-
-
0.0102
D-fructose 1,6-bisphosphate
30°C, H156E mutant
0.0107
D-fructose 1,6-bisphosphate
-
-
0.012
D-fructose 1,6-bisphosphate
-
aldolase I
0.012
D-fructose 1,6-bisphosphate
-
aldolase B
0.012
D-fructose 1,6-bisphosphate
-
wild-type and mutants, pH 7.4
0.013
D-fructose 1,6-bisphosphate
wild-type enzyme
0.013
D-fructose 1,6-bisphosphate
-
aldolase C
0.0134
D-fructose 1,6-bisphosphate
-
enzyme form II
0.0134
D-fructose 1,6-bisphosphate
mutant enzyme E187Q
0.0138
D-fructose 1,6-bisphosphate
-
pH 7.6
0.0146
D-fructose 1,6-bisphosphate
-
native enzyme, in Tris-HCl buffer (40 mM, pH 8.0), at 25°C
0.015
D-fructose 1,6-bisphosphate
-
-
0.016
D-fructose 1,6-bisphosphate
-
recombinant muscle-type enzyme
0.016
D-fructose 1,6-bisphosphate
mutant enzyme D255A, in 50 mM K+-HEPES (pH 7.5), at 25°C
0.0167
D-fructose 1,6-bisphosphate
-
pH 7.5, 30°C
0.0168
D-fructose 1,6-bisphosphate
-
pH 7.6, recombinant enzyme
0.018
D-fructose 1,6-bisphosphate
-
muscle-type enzyme
0.018
D-fructose 1,6-bisphosphate
in the absence of Co2+, at pH 7.5, 30°C
0.0188
D-fructose 1,6-bisphosphate
-
recombinant fusion protein DLF, in Tris-HCl buffer (40 mM, pH 8.0), at 25°C
0.02
D-fructose 1,6-bisphosphate
-
0.02
D-fructose 1,6-bisphosphate
-
enzyme from cytoplasm and chloroplast
0.02
D-fructose 1,6-bisphosphate
-
E182A mutant, 30°C
0.02
D-fructose 1,6-bisphosphate
pH 7.3, 28°C
0.0204
D-fructose 1,6-bisphosphate
mutant enzyme K146M
0.0205
D-fructose 1,6-bisphosphate
-
-
0.022
D-fructose 1,6-bisphosphate
-
-
0.022
D-fructose 1,6-bisphosphate
-
A337V, 22°C, pH 7.6
0.025
D-fructose 1,6-bisphosphate
-
-
0.027
D-fructose 1,6-bisphosphate
-
A149P, 22°C, pH 7.6
0.0279
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30°C
0.03
D-fructose 1,6-bisphosphate
-
at pH 7.5 and pH 8.0
0.032
D-fructose 1,6-bisphosphate
N334K mutant, 22°C
0.035
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30°C
0.0401
D-fructose 1,6-bisphosphate
-
pH 9.3
0.0412
D-fructose 1,6-bisphosphate
mutant enzyme K107M
0.045
D-fructose 1,6-bisphosphate
-
-
0.0459
D-fructose 1,6-bisphosphate
-
pH 5.5
0.047
D-fructose 1,6-bisphosphate
-
W147R, 22°C, pH 7.6
0.049
D-fructose 1,6-bisphosphate
pH 7.6
0.05
D-fructose 1,6-bisphosphate
-
at 30°C in 50 mM Tris-HCl, 0.1 M potassium acetate buffer (pH 8.0)
0.051
D-fructose 1,6-bisphosphate
-
at pH 7.8
0.051
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30°C
0.0519
D-fructose 1,6-bisphosphate
wild-type enzyme
0.052
D-fructose 1,6-bisphosphate
-
aldolase A
0.055
D-fructose 1,6-bisphosphate
-
-
0.0552
D-fructose 1,6-bisphosphate
-
pH 9.3
0.0566
D-fructose 1,6-bisphosphate
mutant enzyme G346S
0.06
D-fructose 1,6-bisphosphate
-
muscle
0.0656
D-fructose 1,6-bisphosphate
-
pH 5.5
0.0728
D-fructose 1,6-bisphosphate
-
pH 5.5
0.074
D-fructose 1,6-bisphosphate
-
-
0.0777
D-fructose 1,6-bisphosphate
-
pH 9.2
0.08
D-fructose 1,6-bisphosphate
-
aldolase class II
0.1
D-fructose 1,6-bisphosphate
-
-
0.1
D-fructose 1,6-bisphosphate
-
at 48°C
0.105
D-fructose 1,6-bisphosphate
mutant enzyme E206K
0.12
D-fructose 1,6-bisphosphate
-
-
0.13
D-fructose 1,6-bisphosphate
-
E174A mutant, 30°C
0.14
D-fructose 1,6-bisphosphate
30°C
0.15
D-fructose 1,6-bisphosphate
-
immobilized enzyme
0.15
D-fructose 1,6-bisphosphate
-
30°C
0.15
D-fructose 1,6-bisphosphate
mutant enzyme K107M
0.16
D-fructose 1,6-bisphosphate
-
-
0.16
D-fructose 1,6-bisphosphate
pH 7.6, 50°C
0.1613
D-fructose 1,6-bisphosphate
-
0.17
D-fructose 1,6-bisphosphate
-
wild-type enzyme, 30°C
0.175
D-fructose 1,6-bisphosphate
-
aldolase II
0.18
D-fructose 1,6-bisphosphate
30°C, D109A mutant
0.19
D-fructose 1,6-bisphosphate
30°C, wild-type enzyme
0.2
D-fructose 1,6-bisphosphate
-
0.22
D-fructose 1,6-bisphosphate
-
Q59A mutant, 30°C
0.239
D-fructose 1,6-bisphosphate
pH 7.8, temperature not specified in the publication
0.239
D-fructose 1,6-bisphosphate
at pH 7.8 and 25°C
0.24
D-fructose 1,6-bisphosphate
pH 7.5, 42°C
0.3
D-fructose 1,6-bisphosphate
-
-
0.3
D-fructose 1,6-bisphosphate
-
E181A mutant, 30°C
0.305
D-fructose 1,6-bisphosphate
70°C, pH 6.5
0.33
D-fructose 1,6-bisphosphate
-
R303W, 22°C, pH 7.6
0.37
D-fructose 1,6-bisphosphate
30°C, N286D mutant
0.38
D-fructose 1,6-bisphosphate
-
pH 7.5, 37°C
0.38
D-fructose 1,6-bisphosphate
-
K325A mutant, 30°C
0.43
D-fructose 1,6-bisphosphate
-
S61T mutant, 30°C
0.45
D-fructose 1,6-bisphosphate
-
in Tris-HCl pH 8.0, at 30°C
0.576
D-fructose 1,6-bisphosphate
in 50 mM Tris-HCl buffer at pH 8.5 and 60°C
0.77
D-fructose 1,6-bisphosphate
30°C, D290A mutant
0.821
D-fructose 1,6-bisphosphate
pH 8.0, 25°C
0.822
D-fructose 1,6-bisphosphate
at pH 6.0 and 25°C
0.822
D-fructose 1,6-bisphosphate
recombinant enzyme, pH 8.0, 55°C
0.9
D-fructose 1,6-bisphosphate
-
N35A mutant, 30°C
0.92
D-fructose 1,6-bisphosphate
30°C, D329A mutant
0.94
D-fructose 1,6-bisphosphate
30°C, D144A mutant
1
D-fructose 1,6-bisphosphate
30°C, D288A mutant
1.07
D-fructose 1,6-bisphosphate
30°C, N286A mutant
1.1
D-fructose 1,6-bisphosphate
in the presence of 0.02 mM Co2+, at substrate concentrations of 0.5-1.5 mM, at pH 7.5, 30°C
1.8
D-fructose 1,6-bisphosphate
-
-
2
D-fructose 1,6-bisphosphate
-
-
2
D-fructose 1,6-bisphosphate
-
-
2
D-fructose 1,6-bisphosphate
-
pH 7.5, 37°C
2
D-fructose 1,6-bisphosphate
pH 7.8, 55°C
2.7
D-fructose 1,6-bisphosphate
-
S61A mutant, 30°C
4.2
D-fructose 1,6-bisphosphate
-
50°C, pH not specified in the publication
5.1
D-fructose 1,6-bisphosphate
native recombinant enzyme, pH 7.6, 22°C
5.7
D-fructose 1,6-bisphosphate
E189A mutant, pH 7.6, 22°C
6.2
D-fructose 1,6-bisphosphate
E187A mutant, pH 7.6, 22°C
10.9
D-fructose 1,6-bisphosphate
E189Q mutant, pH 7.6, 22°C
13.4
D-fructose 1,6-bisphosphate
E187Q mutant, pH 7.6, 22°C
20
D-fructose 1,6-bisphosphate
-
0.0017
D-Fructose 1-phosphate
W147R mutant, 22°C
0.00173
D-Fructose 1-phosphate
L256P mutant, 22°C
0.0022
D-Fructose 1-phosphate
wild-type enzyme, 22°C
0.0024
D-Fructose 1-phosphate
-
wild-type, 22°C, pH 7.6
0.0033
D-Fructose 1-phosphate
-
L256P, 22°C, pH 7.6
0.0098
D-Fructose 1-phosphate
-
A149P, 22°C, pH 7.6
0.022
D-Fructose 1-phosphate
N334K mutant, 22°C
0.024
D-Fructose 1-phosphate
-
A337V, 22°C, pH 7.6
0.0266
D-Fructose 1-phosphate
-
W147R, 22°C, pH 7.6
0.05
D-Fructose 1-phosphate
Q354E mutant, 22°C
0.24
D-Fructose 1-phosphate
-
pH 7.4, 10°C, wild-type enzyme
0.723
D-Fructose 1-phosphate
30°C, aldolase B
0.88
D-Fructose 1-phosphate
-
pH 7.4, 30°C, wild-type enzyme
2.6
D-Fructose 1-phosphate
30°C, AB_All mutant
4.2
D-Fructose 1-phosphate
-
pH 7.4, 10°C, enzyme from patients with intolerance
16
D-Fructose 1-phosphate
-
-
16.4
D-Fructose 1-phosphate
-
pH 7.4, 30°C, enzyme from patients with intolerance
28
D-Fructose 1-phosphate
-
pH 7.5, 37°C
39.8
D-Fructose 1-phosphate
30°C, aldolase A
40
D-Fructose 1-phosphate
at 30°C
0.01503
D-fructose-1,6-bisphosphate
purified C-His-rMtFBA, indicates that the extra five histidine residues in C-His-rMtFBA has negligible effects on the kinetic properties of the enzyme
0.01598
D-fructose-1,6-bisphosphate
purified native-rMtFBA
0.018
D-fructose-1,6-bisphosphate
mutant E169A, pH 7.8, 22°C
0.021
D-fructose-1,6-bisphosphate
mutant G167A, pH 7.8, 22°C
0.021
D-fructose-1,6-bisphosphate
mutant G167A/G166A, pH 7.8, 22°C
0.0279
D-fructose-1,6-bisphosphate
-
pH 7.3, 28°C
0.03
D-fructose-1,6-bisphosphate
mutant E168A, pH 7.8, 22°C
0.035
D-fructose-1,6-bisphosphate
-
pH 7.3, 28°C
0.04
D-fructose-1,6-bisphosphate
wild-type, pH 7.8, 22°C
0.05
D-fructose-1,6-bisphosphate
-
0.051
D-fructose-1,6-bisphosphate
-
pH 7.3, 28°C
0.055
D-fructose-1,6-bisphosphate
-
0.18
D-fructose-1,6-bisphosphate
mutant D276A, pH 7.8, 22°C
0.43
D-fructose-1,6-bisphosphate
-
at 50°C
0.45
D-fructose-1,6-bisphosphate
-
0.45
D-fructose-1,6-bisphosphate
-
pH 7.3, 28°C
0.052
D-glyceraldehyde 3-phosphate
pH 6.5, 70°C
0.057
D-glyceraldehyde 3-phosphate
-
-
0.19
D-glyceraldehyde 3-phosphate
pH 8.0, 48°C, wild-type enzyme
0.25
D-glyceraldehyde 3-phosphate
pH 7.8, 55°C
0.3
D-glyceraldehyde 3-phosphate
-
liver
0.34
D-glyceraldehyde 3-phosphate
pH 8.0, 48°C, mutant enzyme Y348F
0.58
D-glyceraldehyde 3-phosphate
pH 7.6, 50°C
1
D-glyceraldehyde 3-phosphate
-
muscle
1.17
D-glyceraldehyde 3-phosphate
in the absence of Co2+, at pH 7.5, 30°C
0.0036
fructose 1,6-bisphosphate
50°C, pH 7
0.009
fructose 1,6-bisphosphate
50°C, pH 7
0.007
fructose 1-phosphate
-
chloroplastic enzyme
0.008
fructose 1-phosphate
-
cytoplasmic enzyme
0.0103
fructose 1-phosphate
-
chloroplastic enzyme
0.6
fructose 1-phosphate
-
chloroplastic enzyme
0.71
fructose 1-phosphate
50°C, pH 7
0.8
fructose 1-phosphate
-
liver
1
fructose 1-phosphate
-
-
1
fructose 1-phosphate
-
cytosolic enzyme
1.1
fructose 1-phosphate
-
recombinant enzyme
1.4
fructose 1-phosphate
-
cytosolic enzyme
1.5
fructose 1-phosphate
-
-
1.6
fructose 1-phosphate
-
chloroplastic enzyme
1.6
fructose 1-phosphate
-
pH 5.5
1.7
fructose 1-phosphate
-
chloroplastic enzyme
1.7
fructose 1-phosphate
-
chloroplastic enzyme
1.7
fructose 1-phosphate
-
cytosolic enzyme
1.7
fructose 1-phosphate
-
mutant aldolase C Y363S
1.9
fructose 1-phosphate
-
pH 5.5
2
fructose 1-phosphate
-
-
2
fructose 1-phosphate
-
-
2.3
fructose 1-phosphate
-
liver enzyme
2.3
fructose 1-phosphate
-
cytosolic enzyme
2.9
fructose 1-phosphate
-
-
3
fructose 1-phosphate
-
-
3.7
fructose 1-phosphate
-
aldolase B
3.8
fructose 1-phosphate
-
pH 5.5
4.48
fructose 1-phosphate
50°C, pH 7
5.3
fructose 1-phosphate
-
pH 7.6
6.1
fructose 1-phosphate
-
-
6.2
fructose 1-phosphate
-
pH 7.6
8.3
fructose 1-phosphate
-
recombinant non-muscle-type enzyme
9
fructose 1-phosphate
-
pH 9.2
9.3
fructose 1-phosphate
-
muscle-type enzyme
10
fructose 1-phosphate
-
-
10
fructose 1-phosphate
-
muscle
11
fructose 1-phosphate
-
pH 9.3
11
fructose 1-phosphate
-
non-muscle-type enzyme and recombinant muscle-type enzyme
11.3
fructose 1-phosphate
-
pH 7.6
18
fructose 1-phosphate
-
aldolase C
18
fructose 1-phosphate
-
pH 9.3
18.8
fructose 1-phosphate
-
-
25
fructose 1-phosphate
-
-
25
fructose 1-phosphate
-
aldolase C
27
fructose 1-phosphate
-
aldolase A
0.065
glycerone phosphate
-
-
0.171
glycerone phosphate
pH 6.5, 70°C
0.19
glycerone phosphate
pH 8.0, 48°C, wild-type enzyme
0.34
glycerone phosphate
pH 8.0, 48°C, mutant enzyme Y348F
0.4
glycerone phosphate
-
liver
1
glycerone phosphate
pH 7.6, 50°C
2
glycerone phosphate
-
muscle
2
glycerone phosphate
pH 7.8, 55°C
0.008
sedoheptulose 1,7-bisphosphate
-
pH 7.5, class II aldolase, recombinant enzyme
0.047
sedoheptulose 1,7-bisphosphate
-
pH 8, class I aldolase, recombinant enzyme
0.19
sedoheptulose 1,7-bisphosphate
in the absence of Co2+, at pH 7.5, 30°C
0.006
sedoheptulose 1,7-diphosphate
-
-
10
sedoheptulose 1,7-diphosphate
-
-
0.0167
sedoheptulose 7-phosphate
-
pH 7.5, 30°C
0.0195
sedoheptulose 7-phosphate
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Km-values of chimeric enzymes between two human aldolases A, B, or C
-
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
-
Michaelis-Menten kinetics, from Arrhenius plots, activation energies for phosphatase and aldolase reactions are calculated 46.5 and 75.62 kJ/mol, respectively
-
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drug target
potential target for drug development against pathogenic bacteria
drug target
the enzyme (FBPase-1) is considered to be a new target for the control of diabetes
drug target
the enzyme is an attractive targets for the discovery of drugs to combat invasive fungal infection, because it is absent in animals and higher plants. It is a promising target for the discovery of drugs against azole-resistant fungal pathogens in the future
drug target
-
potential target for drug development against pathogenic bacteria
-
drug target
-
the enzyme is an attractive targets for the discovery of drugs to combat invasive fungal infection, because it is absent in animals and higher plants. It is a promising target for the discovery of drugs against azole-resistant fungal pathogens in the future
-
drug target
-
the enzyme (FBPase-1) is considered to be a new target for the control of diabetes
-
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 fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
evolution
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
evolution
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
evolution
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
evolution
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
evolution
-
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
-
evolution
-
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
-
evolution
-
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
-
evolution
-
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
-
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
-
evolution
-
the fact that fructose 1,6-bisphosphate aldolase of prokaryotes has little homology with the fructose 1,6-bisphosphate aldolase of eukaryotes provides an advantage for vaccine development
-
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
-
malfunction
deletion mutant loses the ability to grow on fructose, but growth on glucose is not inhibited and is even slightly stimulated
malfunction
-
decreasing fructose-1,6-bisphosphate aldolase activity reduces plant growth and tolerance to chilling stress in tomato seedlings
malfunction
enzyme inactivation impairs virulence and increases resistance to oxidative stress
malfunction
enzyme knockdown stops cell cycle progression and enhances apoptosis due to rapid accumulation of reactive oxygen species
malfunction
-
knockdown of fructose-1,6-bisphosphate aldolases activates AMP-activated protein kinase even in cells with abundant glucose, while the catalysis-defective D34S aldolase mutant, which still binds fructose-1,6-bisphosphate, blocks AMP-activated protein kinase activation
malfunction
knockdown of the enzyme stops cell cycle progression and enhances apoptosis due to rapid accumulation of reactive oxygen species
malfunction
-
the interference of SlFBA7 expression decreases the regeneration of ribulose-1,5-bisphosphate and the CO2 fixation in the Calvin-Benson cycle and leads to reduced growth and development of tomato seedlings. Inhibition of SlFBA7 expression and activity of fructose-1,6-bisphosphate aldolase decreases the levels of net photosynthetic rate and increases the H2O2 and O2(·-) accumulation in the RNAi transgenic tomato seedlings under chilling stress
malfunction
-
enzyme inactivation impairs virulence and increases resistance to oxidative stress
-
malfunction
-
deletion mutant loses the ability to grow on fructose, but growth on glucose is not inhibited and is even slightly stimulated
-
metabolism
the enzyme is involved in glycolysis
metabolism
-
chloroplastic fructose 1,6-bisphosphate aldolase isoforms are methylated by protein-lysine methyltransferase LSMT. Trimethylation occurs at a conserved lysyl residue located close to the C terminus. Trimethylation does not modify the kinetic properties and tetrameric organization of the aldolases in vitro
metabolism
-
the enzyme is a sensor of glucose availability that regulates AMP-activated protein kinase
metabolism
-
the enzyme is involved in the Embden-Meyerhof-Parnas glycolytic pathway and in gluconeogenesis
metabolism
-
the enzyme is involved in the Embden-Meyerhof-Parnas glycolytic pathway and in gluconeogenesis
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 is involved in glycolysis
-
metabolism
-
the enzyme is involved in the Embden-Meyerhof-Parnas glycolytic pathway and in gluconeogenesis
-
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
-
physiological function
-
ALDOA is involved in keratinocyte migration following the induction of lamellipodia formation, and ALDOA-related migration is enhanced by epidermal growth factor
physiological function
-
FBA is required for optimal adhesion of meningococci to human cells
physiological function
-
part of 4-fluorothreonine biosynthesis
physiological function
-
the enzyme is involved in glycolysis
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
gluconeogenic pathway
physiological function
gene product is required for the growth of Mycobacterium tuberculosis on gluconeogenetic substrates and in glucose-containing medium
physiological function
isoform FbaC acts as major aldolase in glycolysis, whereas isoform FbaP acts as major aldolase in gluconeogenesis in Bacillus methanolicus. The aldolase-negative Corynebacterium glutamicum mutant Dfda can be complemented by the FbaC gene
physiological function
-
mutagenesis in a unique fbaB gene of Xanthomonas oryzae pv. oryzicola, the causal agent of rice bacterial leaf streak, leads the pathogen unable to use pyruvate and malate for growth and delays its growth when fructose is used as the sole carbon source, but also reduces extracellular polysaccharide production and impairs bacterial virulence and growth in rice. The expression of hrpG and hrpX encoding a type-III secretion system is repressed and the transcripts of hrcC, hrpE and hpa3 are enhanced when fbaB is deleted
physiological function
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis. The enzyme is essential for growth on fructose
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
-
the overproduction of fructose bisphosphate aldolase Fba1 enables overcoming of a severe growth defect caused by a missense mutation rpc128-1007 in a gene encoding the C128 protein, the second largest subunit of the RNA polymerase III complex. The suppression of the growth phenotype by Fba1 is accompanied by enhanced de novo tRNA transcription in rpc128-1007 cells. Overproduction of an inactive aldolase mutant still suppresses the rpc128-1007 phenotype, and Fba1 interacts with the RNA polymerase III complex and plays a role in control of tRNA transcription
physiological function
-
the seed germination and root elongation of knock-out plants exhibits sensitivity to abscisic acid and salt stress. Gene is able to complement the salt-sensitive phenotype of a calcineurin-deficient yeast mutant
physiological function
-
transgenic Nicotiana tabacum L. cv Xanthi expressing Arabidopsis plastid aldolase shows 1.4-1.9fold higher aldolase activities than wild-type, associated with enhanced growth, culminating in increased biomass, particularly under high CO2 concentration where the increase reached 2.2fold relative to wild-type plants. This increase is associated with a 1.5fold elevation of photosynthetic CO2 fixation in the transgenic plants. Overexpression results in a decrease in 3-phosphoglycerate and an increase in ribulose 1,5-bisphosphate and its immediate precursors in the Calvin cycle
physiological function
enzyme expression is necessary for cancer cells to grow in hypoxic conditions
physiological function
the enzyme is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. In addition, there is a direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively
physiological function
-
the enzyme is required for optimal adhesion to human cells
physiological function
-
the enzyme regulates growth and chilling tolerance of tomato seedlings
physiological function
fructose-1,6-bisphosphate aldolase B catalyses the reversible reaction of glyceraldehyde-3-phosphate (G3-P) and dihydroxyacetone phosphate (DHAP) to form fructose 1,6-bisphosphate and participates in both gluconeogenesis and glycolysis. In vitro protein-protein interaction analysis between liver fructose 1,6-bisphosphate aldolase B and liver fructose 1,6-bisphosphatase (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. FBPase-1 guides the cellular localization of aldolase B
physiological function
CoFAD2 is directly involved in fatty acid metabolic pathway in the oilseeds
physiological function
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
physiological function
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
physiological function
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
physiological function
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
physiological function
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
physiological function
-
conserved glycolytic enzyme with virulence functions in bacteria. It is involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Additional it functions beyond its housekeeping role in central metabolism. Fructose-1,6-bisphosphate aldolase is immunogenic in Streptococcus suis SS9
physiological function
-
conserved glycolytic enzyme with virulence functions in bacteria. It is involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Additional it functions beyond its housekeeping role in central metabolism. The enzyme from Mycobacterium tuberculosis binds human plasminogen
physiological function
-
conserved glycolytic enzyme with virulence functions in bacteria. It is involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Additional it functions beyond its housekeeping role in central metabolism. The enzyme from Neisseria meningitidis is dispensable for survival of, but required for optimal adhesion to human cells
physiological function
-
conserved glycolytic enzyme with virulence functions in bacteria. It is involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Additional it functions beyond its housekeeping role in central metabolism. The Pneumococcal enzyme is an immunogenic adhesin which binds Flamingo cadherin receptor
physiological function
during invasion of the apicomplexan parasite Toxoplasma gondii into host cells, the enzyme serves in the role of a structural bridging protein, as opposed to its normal enzymatic role in the glycolysis pathway
physiological function
fructose-1,6-bisphosphate aldolase (CoFBA) and stearoyl-ACP desaturase (CoSAD) gene expression is well-correlated with oil content in Camellia seeds
physiological function
glycolytic enzyme
physiological function
-
important enzyme in the glycolytic pathway
physiological function
-
important enzymes in the Calvin-Benson cycle
physiological function
-
overproduction of the recombinant enzyme (msFBAld) in Escherichia coli results in increased tolerance towards salinity
physiological function
possible participation of the enzyme in the processes of cell adhesion and tissue invasion/dissemination of Paracoccidioides
physiological function
the enzyme is a key regulator of hypoxic adaptation in colorectal cancer cells
physiological function
-
the enzyme is a natural fructose-1,6-bisphosphate receptor that transmits the effects of glucose shortage to AMP-activated protein kinase via the v-ATPase-Ragulator-AXIN/LKB1 complex
physiological function
-
the enzyme is involved in adhesion to host cells. It binds human plasminogen via its C-terminal lysine residue, whereas subterminal lysine residues are not involved
physiological function
the enzyme occupies a central position in glycolysis and gluconeogenesis pathways. Fructose-bisphosphate aldolase is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. Direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively
physiological function
-
the enzyme plays vital role in glycolysis and gluconeogenesis
physiological function
the enzyme positively regulates the activity of the glycolytic pathway and the epithelial-mesenchymal transition and is necessary for cell cycle progression. It is implicated in colorectal cancer proliferation, sphere formation, therapeutic resistance and invasion
physiological function
-
possible participation of the enzyme in the processes of cell adhesion and tissue invasion/dissemination of Paracoccidioides
-
physiological function
-
gluconeogenic pathway
-
physiological function
-
possible participation of the enzyme in the processes of cell adhesion and tissue invasion/dissemination of Paracoccidioides
-
physiological function
-
the enzyme is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. In addition, there is a direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively
-
physiological function
-
the enzyme occupies a central position in glycolysis and gluconeogenesis pathways. Fructose-bisphosphate aldolase is important for bacterial multiplication in macrophages in the presence of gluconeogenic substrates. Direct role of this metabolic enzyme in transcription regulation of genes katG and rpoA, encoding catalase and an RNA polymerase subunit, respectively
-
physiological function
-
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
-
physiological function
-
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
-
physiological function
-
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
-
physiological function
-
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
-
physiological function
-
conserved glycolytic enzyme with virulence functions in bacteria. It is involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Additional it functions beyond its housekeeping role in central metabolism. Fructose-1,6-bisphosphate aldolase is immunogenic in Streptococcus suis SS9
-
physiological function
-
fructose-1,6-bisphosphate aldolase B catalyses the reversible reaction of glyceraldehyde-3-phosphate (G3-P) and dihydroxyacetone phosphate (DHAP) to form fructose 1,6-bisphosphate and participates in both gluconeogenesis and glycolysis. In vitro protein-protein interaction analysis between liver fructose 1,6-bisphosphate aldolase B and liver fructose 1,6-bisphosphatase (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. FBPase-1 guides the cellular localization of aldolase B
-
physiological function
-
conserved glycolytic enzyme with virulence functions in bacteria. It is involved in the Embden-Meyerhof-Parnas (EMP) glycolytic pathway and in gluconeogenesis. Additional it functions beyond its housekeeping role in central metabolism. The Pneumococcal enzyme is an immunogenic adhesin which binds Flamingo cadherin receptor
-
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
physiological function
-
during invasion of the apicomplexan parasite Toxoplasma gondii into host cells, the enzyme serves in the role of a structural bridging protein, as opposed to its normal enzymatic role in the glycolysis pathway
-
physiological function
-
the enzyme has an anabolic function catalyzing fructose-1,6-bisphosphate formation in the course of gluconeogenesis. The enzyme is essential for growth on fructose
-
physiological function
-
isoform FbaC acts as major aldolase in glycolysis, whereas isoform FbaP acts as major aldolase in gluconeogenesis in Bacillus methanolicus. The aldolase-negative Corynebacterium glutamicum mutant Dfda can be complemented by the FbaC gene
-
physiological function
-
conserved enzyme in the glycolytic pathway. The enzyme also has protection efficacy
-
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
-
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
-
the active site of enzyme Pcal_0111 contains a lysine residue which makes Schiff base with carbonyl group of the substrate
-
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