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D-fructose 6-phosphate
D-glucose 6-phosphate
D-fructose 6-phosphate
D-mannose 6-phosphate
D-galactose
D-tagatose
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
D-Mannose 6-phosphate
D-Fructose 6-phosphate
fructose 6-phosphate
D-glucose 6-phosphate
-
-
r
Fructose 6-phosphate
Glucose 6-phosphate
Glucose 6-phosphate
Fructose 6-phosphate
L-talose
L-tagatose
best aldose substrate
-
-
?
malonic dialdehyde
methylglyoxal
-
-
-
-
r
additional information
?
-
D-fructose 6-phosphate

D-glucose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
Cassia coluteoides
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
?
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
the isomerization occurrs by a cis-enediol intermediate involving C-1 pro-R hydrogen of D-fructose 6-phosphate. The presence of metal electrophile to activate the carbonyl group is required not only for the hydride shift mechanism but also for the operation of an enediol process
-
-
r
D-fructose 6-phosphate
D-glucose 6-phosphate
-
-
-
r
D-fructose 6-phosphate

D-mannose 6-phosphate
-
-
-
r
D-fructose 6-phosphate
D-mannose 6-phosphate
-
-
-
r
D-glucose 6-phosphate

D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
Cassia coluteoides
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
multistep catalytic mechanism is proposed: first the enzyme catalyzes ring opening to yield the open chain form of the substrate. Then isomerization proceeds via proton transfer between C2 and C1 of a cis-enediol(ate) intermediate to yield the open chain form of the product. His388 promotes ring opening by protonating the ring oxygen. Glu216 helps to position His388, and a water molecule that is held in position by Lys518 and Thr214 accepts a proton from the hydroxyl group at C2
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
the active site residues Lys58 and His388 might be involved in catalytic mechanism
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
in the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
in hydride shift mechanism of catalysis Fe2+ is responsible for proton transfer between O1 and O2, and the hydride shift between C1 and C2 is favored by a markedly hydrophobic environment in the active site. The absence of any obvious enzymatic machinery for catalyzing ring opening of the sugar substrates suggests that the pyrococcal enzyme has a preference for straight chain substrates. The metabolism in extreme thermophiles may use sugars in both ring and straight chain forms. At the extreme temperatures in which Pyrococcus furiosus exists, the equilibrium would increasingly favor the open chain forms
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
the glucose 6-phosphate molecule is bound in an extended conformation in the active site of PGI, substrate binding structure, overview
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
the glucose 6-phosphate molecule is bound in an extended conformation in the active site of PGI, substrate binding structure, overview
-
-
r
D-Mannose 6-phosphate

D-Fructose 6-phosphate
-
-
-
r
D-Mannose 6-phosphate
D-Fructose 6-phosphate
-
-
-
r
Fructose 6-phosphate

Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
r
-
?
Fructose 6-phosphate
Glucose 6-phosphate
-
-
-
?
Glucose 6-phosphate

Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
Glucose 6-phosphate
Fructose 6-phosphate
-
r
-
?
additional information

?
-
-
the multifunctional protein GPI shows specific and competitive inhibitory activity toward a myofibril-bound serine proteinase, MBSP, from Carassius auratus with a Ki of 320 nM, inhibition kinetics, while no inhibitory activity is identified toward other serine proteinases, such as white croaker MBSP and crucian carp trypsin, overview
-
-
?
additional information
?
-
-
the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
-
-
?
additional information
?
-
-
the formation of phosphoglucose isomerase is under respiratory control, during anaerobiosis the enzyme is derepressed parallely with other glycolytic enzymes
-
-
?
additional information
?
-
the enzyme has cell-motility-stimulating activity on mouse colon cancer cells
-
?
additional information
?
-
-
the enzyme has cell-motility-stimulating activity on mouse colon cancer cells
-
?
additional information
?
-
the enzyme plays a central role in both the glycolysis and the gluconeogenesis pathways
-
?
additional information
?
-
-
the enzyme plays a central role in both the glycolysis and the gluconeogenesis pathways
-
?
additional information
?
-
-
PGI/AMF stimulates beta-catenin expression and is involved in E-cadherin and beta-catenin expression regulation, overview
-
-
?
additional information
?
-
the enzyme can also act as an autocrine motility factor, neuroleukin, and maturation factor
-
-
?
additional information
?
-
-
the enzyme can also act as an autocrine motility factor, neuroleukin, and maturation factor
-
-
?
additional information
?
-
the enzyme plays important roles in glycolysis and gluconeogenesis
-
?
additional information
?
-
-
the enzyme plays important roles in glycolysis and gluconeogenesis
-
?
additional information
?
-
-
the enzyme is part of the glycolytic pathway
-
?
additional information
?
-
glucose-6-phosphate isomerase catalyzes the interconversion between two different aldoses and ketose for pentoses and hexoses via two isomerization reactions. Activity order as follows: aldose substrates with hydroxyl groups oriented in the same direction at C2, C3, and C4 better than C2 and C4 better than C2 and C3 better than C3 and C4. L-Talose and D-ribulose exhibit the most preferred substrates among the aldoses and ketoses, respectively, substrate specificity, overview
-
-
?
additional information
?
-
-
glucose-6-phosphate isomerase catalyzes the interconversion between two different aldoses and ketose for pentoses and hexoses via two isomerization reactions. Activity order as follows: aldose substrates with hydroxyl groups oriented in the same direction at C2, C3, and C4 better than C2 and C4 better than C2 and C3 better than C3 and C4. L-Talose and D-ribulose exhibit the most preferred substrates among the aldoses and ketoses, respectively, substrate specificity, overview
-
-
?
additional information
?
-
enzyme does not convert mannose 6-phosphate to fructose 6-phosphate
-
-
?
additional information
?
-
-
enzyme does not convert mannose 6-phosphate to fructose 6-phosphate
-
-
?
additional information
?
-
-
glycolytic enzyme
-
-
?
additional information
?
-
-
enzyme of the oxidative pentose phosphate cycle
-
-
?
additional information
?
-
-
the isomerization occurs by a cis-enediol intermediate involving the C-1 pro-R hydrogen atom of fructose 6-phosphate. The presence of a metal electrophile to activate the carbonyl group is required not only for the hydride shift mechanism but also for the operation of an enediol process
-
-
?
additional information
?
-
the isomerization occurs by a cis-enediol intermediate involving the C-1 pro-R hydrogen atom of fructose 6-phosphate. The presence of a metal electrophile to activate the carbonyl group is required not only for the hydride shift mechanism but also for the operation of an enediol process
-
-
?
additional information
?
-
-
probable role of the enzyme in starch biosynthesis in amyloplasts
-
-
?
additional information
?
-
-
glycolytic enzyme
-
-
?
additional information
?
-
-
glycolytic enzyme
-
-
?
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1,5-Anhydroglucitol 6-phosphate
-
-
2-amino-2-deoxy-D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-amino-2-deoxy-D-glucitol 6-phosphate dimethyl ester
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-amino-2-deoxy-D-mannitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-Deoxy-D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
2-deoxyglucose 6-phosphate
-
-
5-deoxy-5-malonate-D-arabinonohydroxamic acid
-
-
5-phospho-D-arabinoamide
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinoate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinohydroxamate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
5-phospho-D-arabinonohydroxamate
competitive, stable analogue of putative cis-endiol intermediate
5-phospho-D-arabinonohydroxamic acid
-
-
5-phosphoarabinonhydroxamic acid
6-phospho-2-deoxygluconate
Cassia coluteoides
-
glucose 6-phosphate as substrate
6-phospho-D-gluconate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
6-phospho-D-gluconoamide
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
6-Phosphomannonate
Cassia coluteoides
-
with glucose 6-phosphate as substrate
Ca2+
slight inhibition at 1.5 mM
Co2+
10 mM, 59% inhibition, D-fructose 6-phosphate as substrate
D-fructose 1,6-bisphosphate
D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
dihydroxyacetone phosphate
-
-
Erythritol 4-phosphate
-
-
erythrose-4-phosphate
-
-
gluconate 6-phosphate
-
-
glyceraldehyde 3-phosphate
-
-
GTP
-
competitive inhibitor, also compromises the autocrine motility factor function of the enzyme. The GTP-binding site partially overlaps with the catalytic site. In addition,GTP stabilizes the structure of PGI against heat- and detergent-induced denaturation. GTP is bound in a syn-conformation with the gamma-phosphate group located near the phosphate-binding loop and the ribose moiety positioned away from the active-site residues
insulin-like growth factor binding protein-3
-
both glycosylated and unglycosylated, binding and inhibition of enzyme
-
K+
10 mM, 18% inhibition, D-fructose 6-phosphate as substrate
L-Sorbose 6-phosphate
-
-
L-xylulose 5-phosphate
-
-
Maleate
-
10 mM, 50% inhibition
malonate
-
10 mM, 15% inhibition
mannitol 1-phosphate
Cassia coluteoides
-
glucose 6-phosphate as substrate
N,2,3,4,5-pentahydroxypentanamide
-
-
N-acetyl-2-amino-2-deoxy-D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
N-bromoacetylethanolamine phosphate
-
oxaloacetate
-
10 mM, 25% inhibition
oxoglutarate
-
10 mM, 20% inhibition
sedoheptulose 7-phosphate
5-phospho-D-arabinonate

-
5-phospho-D-arabinonate
-
5-phospho-D-arabinonate
competitive
5-phosphoarabinonhydroxamic acid

-
-
5-phosphoarabinonhydroxamic acid
competitive inhibition
6-phosphogluconate

-
6-phosphogluconate
Cassia coluteoides
-
glucose 6-phosphate as substrate
6-phosphogluconate
-
0.2 mM, 52% inhibition
6-phosphogluconate
-
competitive
6-phosphogluconate
-
pH 7.6, 25ưC
6-phosphogluconate
-
competitive
Agaricic acid

-
-
Agaricic acid
irreversible inhibition
Cd2+

10 mM, 96% inhibition, D-fructose 6-phosphate as substrate
Cu2+

-
1 mM, about 40% inhibition
Cu2+
10 mM, 96% inhibition, D-fructose 6-phosphate as substrate
D-fructose 1,6-bisphosphate

10 mM, residual activities are 41% and 53% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively
D-fructose 1,6-bisphosphate
-
D-Fructose 1-phosphate

2 mM, residual activities are 50% and 69% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively
D-gluconate 6-phosphate

-
D-gluconate 6-phosphate
-
D-mannose 6-phosphate

1.25 mM, residual activities are 18% and 38% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively
EDTA

-
-
EDTA
100fold excess, complete loss of activity within 10 min. 93% of activity may be recovered by additon of 1000fold excess of Zn2+
EDTA
-
the enzyme activity is completely diminished when the enzyme is heated at 70ưC in the presence of 10 mM EDTA. Complete restoration of the enzyme activity is observed when the enzyme is incubated at room temperature in the presence of Zn2+
EDTA
10 mM, 78% inhibition, D-fructose 6-phosphate as substrate
erythrose 4-phosphate

-
erythrose 4-phosphate
Cassia coluteoides
-
glucose 6-phosphate as substrate
erythrose 4-phosphate
-
0.02 mM, 58% inhibition
erythrose 4-phosphate
-
activates enzyme form B with ribose 5-phosphate as substrate, inhibits activity of enzyme form A and B with glucose 6-phosphate as substrate, inhibits activity of enzyme form A with glucose 6-phosphate as substrate
erythrose 4-phosphate
-
competitive
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
-
erythrose 4-phosphate
-
competitive
fructose 1,6-diphosphate

-
1 mM, 4% inhibition
fructose 1,6-diphosphate
-
-
fructose 1-phosphate

-
1 mM, 10% inhibition
Hg2+

-
1 mM, about 50% inhibition
Mn2+

10 mM, 18% inhibition, D-fructose 6-phosphate as substrate
Ni2+

10 mM, 84% inhibition, D-fructose 6-phosphate as substrate
phosphate

-
-
ribose 5-phosphate

-
1 mM, 12% inhibition
ribulose 5-phosphate

-
0.5 mM, 48% inhibition
sedoheptulose 7-phosphate

-
1 mM, 10% inhibition
sedoheptulose 7-phosphate
-
-
sorbitol-6-phosphate

-
-
suramin

-
no inhibition
suramin
an anti-trypanosomal drug
Zn2+

-
plastid enzyme is completely inhibited by 5 mM, activity of cytosolic isoenzyme is reduced to 49% of untreated control
Zn2+
10 mM, 89% inhibition, D-fructose 6-phosphate as substrate
additional information

-
no inhibition by PCMB and iodoacetate
-
additional information
-
screening for thiazolide inhibitors, diverse compounds, mode of action of thiazolides and structure-activity relationship, overview
-
additional information
-
not inhibitory: EDTA
-
additional information
activity is not affected by addition of 10 mM EDTA. The addition of fructose, glucose, mannose, galactose (10 mM), pyruvate, phosphoenolpyruvate (10 mM), AMP, ADP, or ATP (3.5 mM), does not show any effect on the activity neither in the fructose 6-phosphate formation, nor in the glucose 6-phosphate formation
-
additional information
-
activity is not affected by addition of 10 mM EDTA. The addition of fructose, glucose, mannose, galactose (10 mM), pyruvate, phosphoenolpyruvate (10 mM), AMP, ADP, or ATP (3.5 mM), does not show any effect on the activity neither in the fructose 6-phosphate formation, nor in the glucose 6-phosphate formation
-
additional information
-
no inhibition by suramin, an anti-trypanosomal drug, and agaricic acid
-
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0.031 - 170
D-fructose 6-phosphate
1.029
D-galactose
-
pH 8.0, 40ưC
0.084 - 267.4
D-glucose 6-phosphate
0.25 - 1.1
D-mannose 6-phosphate
0.01 - 0.74
fructose 6-phosphate
0.03 - 8
glucose 6-phosphate
133
L-talose
pH 7.0, 95ưC
additional information
additional information
-
0.031
D-fructose 6-phosphate

pH 7.5, 30ưC, recombinant mutant S278L
0.034
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant I525T
0.037
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant wild-type enzyme
0.038
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R347H
0.038
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R75G
0.039
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant L487F
0.04
D-fructose 6-phosphate
-
50ưC, pH 6.3
0.045
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant A300P
0.045
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant L339P
0.046
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R347C
0.046
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant T375R
0.05
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant E495K
0.06
D-fructose 6-phosphate
-
pH 7.4, 80ưC
0.061
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R83W
0.063
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant T195I
0.063
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant V101M
0.068
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R472H
0.14
D-fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from germinating seeds
0.1425
D-fructose 6-phosphate
-
-
0.147
D-fructose 6-phosphate
-
22ưC, pH 7.4
0.18
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme Y95K
0.19
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme H136A
0.2
D-fructose 6-phosphate
80ưC, pH 7.4
0.21
D-fructose 6-phosphate
50ưC, pH 7.4
0.22
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme T63A
0.23
D-fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from developing seeds
0.25
D-fructose 6-phosphate
pH 7.4, 70ưC, wild-type enzyme
0.27
D-fructose 6-phosphate
-
pH 7.6, 25ưC
0.3
D-fructose 6-phosphate
-
pH 7.4, 50ưC
0.318
D-fructose 6-phosphate
-
pH 7.6, 22ưC
0.35
D-fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from germinating seeds
0.36
D-fructose 6-phosphate
-
pH 8.0
0.36
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme Y95F
0.39
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme H80D
0.42
D-fructose 6-phosphate
50ưC, pH 7.0, recombinant enzyme
0.44
D-fructose 6-phosphate
80ưC, pH 7.4
0.46
D-fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from developing seeds
0.5
D-fructose 6-phosphate
50ưC
0.5
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme G79A
0.59
D-fructose 6-phosphate
50ưC, pH 7.5, mutant enzyme E89V
0.6
D-fructose 6-phosphate
-
pH 7.4, 50ưC
0.6 - 3
D-fructose 6-phosphate
pH 7.0, 50ưC
0.63
D-fructose 6-phosphate
50ưC, pH 7.0, native enzyme
0.7
D-fructose 6-phosphate
-
pH 7.6, 37ưC
0.8
D-fructose 6-phosphate
-
pH 7.4, 50ưC
1
D-fructose 6-phosphate
-
80ưC, pH 7.0, native enzyme
1.2
D-fructose 6-phosphate
-
80ưC, pH 7.0, recombinant enzyme
1.4
D-fructose 6-phosphate
50ưC, pH 7.5, mutant enzyme H137A
1.4
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme Y160F
1.7
D-fructose 6-phosphate
50ưC, pH 7.5, wild-type enzyme
2
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme G79L
2
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme H82A
2.1
D-fructose 6-phosphate
50ưC, pH 7.5, mutant enzyme H91A
2.2
D-fructose 6-phosphate
-
at pH 6.0 and 37ưC
2.9
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme E93D
3
D-fructose 6-phosphate
-
pH 7.2, 37ưC
3.5
D-fructose 6-phosphate
50ưC, pH 7.5, mutant enzyme H89A
4
D-fructose 6-phosphate
-
80ưC, pH not specified in the publication
20.3
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme H80A
169
D-fructose 6-phosphate
-
wild-type, 37ưC, pH 8.0
170
D-fructose 6-phosphate
-
mutant A346H, 37ưC, pH 8.0
0.084
D-glucose 6-phosphate

-
in 50 mM HEPES buffer, pH 7.1, at 25ưC
0.11
D-glucose 6-phosphate
-
ZR-82 cells, 22ưC
0.18
D-glucose 6-phosphate
mutant enzyme D511N, at 21ưC in 20 mM HEPES buffer (pH 7.5)
0.2 - 1
D-glucose 6-phosphate
mutant enzyme H100L, at 21ưC in 20 mM HEPES buffer (pH 7.5)
0.23
D-glucose 6-phosphate
mutant enzyme E495Q, at 21ưC in 20 mM HEPES buffer (pH 7.5)
0.28
D-glucose 6-phosphate
-
22ưC, pH 7.4
0.29
D-glucose 6-phosphate
mutant enzyme H396L, at 21ưC in 20 mM HEPES buffer (pH 7.5)
0.29
D-glucose 6-phosphate
wild type enzyme, at 21ưC in 20 mM HEPES buffer (pH 7.5)
0.3
D-glucose 6-phosphate
mutant enzyme Y274F, at 21ưC in 20 mM HEPES buffer (pH 7.5)
0.3
D-glucose 6-phosphate
mutant enzyme Y341F, at 21ưC in 20 mM HEPES buffer (pH 7.5)
0.4
D-glucose 6-phosphate
-
pH 7.4, 50ưC
0.5
D-glucose 6-phosphate
mutant enzyme Q388A, at 21ưC in 20 mM HEPES buffer (pH 7.5)
0.6
D-glucose 6-phosphate
-
pH 7.4, 50ưC
0.72
D-glucose 6-phosphate
80ưC, pH 7.4
0.73
D-glucose 6-phosphate
mutant enzyme S185A, at 21ưC in 20 mM HEPES buffer (pH 7.5)
0.78
D-glucose 6-phosphate
mutant enzyme N386A, at 21ưC in 20 mM HEPES buffer (pH 7.5)
0.83
D-glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from germinating seeds
1
D-glucose 6-phosphate
-
pH 7.6, 37ưC
1
D-glucose 6-phosphate
-
pH 7.2, 37ưC
1
D-glucose 6-phosphate
-
50ưC, pH 6.3
1.02
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37ưC
1.04
D-glucose 6-phosphate
mutant enzyme N154Q, at 21ưC in 20 mM HEPES buffer (pH 7.5)
1.1
D-glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from germinating seeds
1.3
D-glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from developing seeds
1.5
D-glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from developing seeds
1.53
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37ưC
1.65
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60ưC
1.86
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60ưC
1.9
D-glucose 6-phosphate
-
pH 7.4, 80ưC
1.9
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37ưC
1.99
D-glucose 6-phosphate
pH 7.0, 50ưC
1.99
D-glucose 6-phosphate
50ưC, pH 7.0, native enzyme
2
D-glucose 6-phosphate
50ưC, pH 7.0, recombinant enzyme
2.11
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37ưC
2.43
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60ưC
2.58
D-glucose 6-phosphate
-
mutant GroD1 cells, 22ưC
2.7
D-glucose 6-phosphate
-
pH 7.4, 50ưC
2.89
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60ưC
3.5
D-glucose 6-phosphate
80ưC, pH 7.4
7.9
D-glucose 6-phosphate
-
80ưC, pH 7.0, recombinant enzyme
8.7
D-glucose 6-phosphate
-
80ưC, pH 7.0, native enzyme
11.7
D-glucose 6-phosphate
50ưC, pH 7.5, wild-type enzyme
221
D-glucose 6-phosphate
-
wild-type, 37ưC, pH 8.0
267.4
D-glucose 6-phosphate
-
mutant A346H, 37ưC, pH 8.0
0.25
D-mannose 6-phosphate

80ưC, pH 7.4
1.1
D-mannose 6-phosphate
80ưC, pH 7.4
0.01 - 0.17
fructose 6-phosphate

-
muscle enzyme, values of 0.01 mM, 0.12 mM and 0.17 mM are determined by different authors
0.0186
fructose 6-phosphate
-
isomerase a
0.0205
fructose 6-phosphate
-
isomerase c
0.0213
fructose 6-phosphate
-
isomerase b
0.048
fructose 6-phosphate
-
-
0.0596
fructose 6-phosphate
-
mutant enzyme Thr224 to Met
0.0635
fructose 6-phosphate
-
native enzyme
0.0657
fructose 6-phosphate
-
mutant enzyme Thr5 to Ile
0.07
fructose 6-phosphate
-
mammary gland enzyme
0.071
fructose 6-phosphate
-
-
0.0734
fructose 6-phosphate
-
mutant enzyme Asp539 to Asn
0.0769
fructose 6-phosphate
-
mutant enzyme Gln343 to Arg
0.09
fructose 6-phosphate
-
isozyme 1 and isozyme 2
0.1
fructose 6-phosphate
-
-
0.1
fructose 6-phosphate
-
-
0.1
fructose 6-phosphate
-
-
0.1
fructose 6-phosphate
-
-
0.1
fructose 6-phosphate
-
fructose 6-phosphate, isozyme 4
0.1
fructose 6-phosphate
-
glucose 6-phosphate, soluble enzyme
0.11
fructose 6-phosphate
-
isozyme 3
0.11 - 0.23
fructose 6-phosphate
-
values of 0.11 mM, 0.15 mM and 0.23 mM are determined by different autors
0.116
fructose 6-phosphate
-
-
0.119
fructose 6-phosphate
-
-
0.12
fructose 6-phosphate
-
-
0.12
fructose 6-phosphate
-
liver enzyme
0.12
fructose 6-phosphate
-
fructose 6-phosphate, enzyme form PGI II
0.12
fructose 6-phosphate
-
fructose 6-phosphate, at pH 8.6
0.12
fructose 6-phosphate
-
glucose 6-phosphate
0.122
fructose 6-phosphate
-
-
0.167
fructose 6-phosphate
-
-
0.17
fructose 6-phosphate
-
enzyme form PGI I
0.18
fructose 6-phosphate
-
-
0.2
fructose 6-phosphate
-
glucose 6-phosphate, immobilized enzyme
0.2
fructose 6-phosphate
-
enzyme forms PGI I and PGI II
0.21
fructose 6-phosphate
-
erythrocyte enzyme, wild-type
0.228 - 0.278
fructose 6-phosphate
-
-
0.3
fructose 6-phosphate
-
isozyme 1 and 2
0.46
fructose 6-phosphate
-
glucose 6-phosphate, isozyme 2
0.48
fructose 6-phosphate
-
chloroplastic isoenzyme
0.74
fructose 6-phosphate
-
erythrocyte enzyme, mutant B9
0.03 - 0.8
glucose 6-phosphate

-
muscle enzyme, values of 0.03 mM, 0.31 mM and 0.8 mM are determined by different authors
0.12 - 0.57
glucose 6-phosphate
-
mammary gland enzyme, values of 0.12 mM and 0.57 mM are determined by different authors
0.25
glucose 6-phosphate
-
-
0.27
glucose 6-phosphate
-
-
0.3 - 1.5
glucose 6-phosphate
-
values of 0.27 mM, 0.3 mM, 0.7 mM, 0.8 mM and 1.5 mM are determined by different authors
0.351
glucose 6-phosphate
-
mutant enzyme Thr224 to Met
0.36
glucose 6-phosphate
-
-
0.44
glucose 6-phosphate
-
glucose 6-phosphate
0.44
glucose 6-phosphate
-
glucose 6-phosphate, enzyme form PGI I and PGI II
0.44
glucose 6-phosphate
-
at pH 8.6
0.445
glucose 6-phosphate
-
native enzyme
0.449
glucose 6-phosphate
-
mutant enzyme Thr5 to Ile
0.45
glucose 6-phosphate
-
isozyme 4
0.505
glucose 6-phosphate
-
mutant enzyme Asp539 to Asn
0.51
glucose 6-phosphate
-
isozyme 1
0.573
glucose 6-phosphate
-
mutant enzyme Gln343 to Arg
0.58
glucose 6-phosphate
-
isozyme 3
0.58
glucose 6-phosphate
-
fructose 6-phosphate, cytosolic isoenzame
0.6
glucose 6-phosphate
-
liver enzyme
2
glucose 6-phosphate
-
-
2
glucose 6-phosphate
-
-
5.9
glucose 6-phosphate
-
isozyme 2
8
glucose 6-phosphate
-
isozyme 1
8
glucose 6-phosphate
-
glucose 6-phosphate, cytosolic and chloroplastic isoenzyme
additional information
additional information

-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
the pH-value has a great influence on the Km-value for fructose 6-phosphate
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
kinetics for aldose substrates, overview
-
additional information
additional information
-
kinetics for aldose substrates, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0003 - 650
D-fructose 6-phosphate
0.04 - 2765
D-glucose 6-phosphate
3330
fructose 6-phosphate
-
isomerase a
475.5
L-talose
pH 7.0, 95ưC
0.0003
D-fructose 6-phosphate

50ưC, pH 7.5, mutant enzyme E98V
0.021
D-fructose 6-phosphate
50ưC, pH 7.5, mutant enzyme H89A
0.06
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme E93D
0.07
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme G79L
0.22
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme Y95F
0.32
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme G79A
0.34
D-fructose 6-phosphate
50ưC, pH 7.5, mutant enzyme H137A
0.42
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme H80D
0.43
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme H80A
0.5
D-fructose 6-phosphate
50ưC, pH 7.5, mutant enzyme H91A
0.6
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant S278L
0.68
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme Y95K
1.9
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme T63A
5
D-fructose 6-phosphate
-
at pH 6.0 and 37ưC
8
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme H82A
8.4
D-fructose 6-phosphate
50ưC
11.6
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme Y160F
15
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant L339P
18
D-fructose 6-phosphate
-
pH 8.0
19
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant L487F
26
D-fructose 6-phosphate
50ưC, pH 7.5, wild-type enzyme
30.8
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme H136A
32.4
D-fructose 6-phosphate
pH 7.4, 70ưC, wild-type enzyme
42
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R347H
75
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant T375R
76
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant I525T
93
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R75G
100
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant A300P
150
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R347C
160
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant V101M
190
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R472H
190
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R83W
300
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant T195I
420
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant mutant E495K
650
D-fructose 6-phosphate
pH 7.5, 30ưC, recombinant wild-type enzyme
0.04
D-glucose 6-phosphate

kcat below 0.04 s-1,mutant enzyme K362A, at 21ưC in 20 mM HEPES buffer (pH 7.5)
0.04
D-glucose 6-phosphate
kcat below 0.04 s-1mutant enzyme H389L, at 21ưC in 20 mM HEPES buffer (pH 7.5)
0.3
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant S278L
0.6
D-glucose 6-phosphate
mutant enzyme H100L, at 21ưC in 20 mM HEPES buffer (pH 7.5)
1.3
D-glucose 6-phosphate
mutant enzyme D511N, at 21ưC in 20 mM HEPES buffer (pH 7.5)
1.6
D-glucose 6-phosphate
mutant enzyme E495Q, at 21ưC in 20 mM HEPES buffer (pH 7.5)
4 - 5
D-glucose 6-phosphate
mutant enzyme Q388A, at 21ưC in 20 mM HEPES buffer (pH 7.5)
17
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant L487F
21
D-glucose 6-phosphate
mutant enzyme H396L, at 21ưC in 20 mM HEPES buffer (pH 7.5)
31
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant L339P
42
D-glucose 6-phosphate
50ưC, pH 7.5, wild-type enzyme
61
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant A300P
63
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R347H
80
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant T375R
110
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant I525T
120
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R83W
130
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R75G
140
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant V101M
240
D-glucose 6-phosphate
mutant enzyme Y274F, at 21ưC in 20 mM HEPES buffer (pH 7.5)
260
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R472H
340
D-glucose 6-phosphate
mutant enzyme Y341F, at 21ưC in 20 mM HEPES buffer (pH 7.5)
350
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant R347C
360
D-glucose 6-phosphate
mutant enzyme S185A, at 21ưC in 20 mM HEPES buffer (pH 7.5)
380
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant T195I
470
D-glucose 6-phosphate
mutant enzyme N154Q, at 21ưC in 20 mM HEPES buffer (pH 7.5)
470
D-glucose 6-phosphate
mutant enzyme N386A, at 21ưC in 20 mM HEPES buffer (pH 7.5)
500
D-glucose 6-phosphate
wild type enzyme, at 21ưC in 20 mM HEPES buffer (pH 7.5)
729
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37ưC
750
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant mutant E495K
929
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37ưC
946
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37ưC
1000
D-glucose 6-phosphate
pH 7.5, 30ưC, recombinant wild-type enzyme
1091
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37ưC
2009
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60ưC
2198
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60ưC
2433
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60ưC
2765
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60ưC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.02 - 162
D-fructose 6-phosphate
2.7 - 1700
D-glucose 6-phosphate
3.58
L-talose
pH 7.0, 95ưC
0.02
D-fructose 6-phosphate

pH 7.4, 70ưC, mutant enzyme E93D
0.02
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme H80A
0.035
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme G79L
0.61
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme Y95F
0.64
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme G79A
1.1
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme H80D
2.27
D-fructose 6-phosphate
-
at pH 6.0 and 37ưC
3.8
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme Y95K
4
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme H82A
8.3
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme Y160F
8.6
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme T63A
11.5
D-fructose 6-phosphate
pH 7.0, 50ưC, native enzyme
16.5
D-fructose 6-phosphate
pH 7.0, 50ưC, recombinant enzyme
130
D-fructose 6-phosphate
pH 7.4, 70ưC, wild-type enzyme
162
D-fructose 6-phosphate
pH 7.4, 70ưC, mutant enzyme H136A
2.7
D-glucose 6-phosphate

mutant enzyme H100L, at 21ưC in 20 mM HEPES buffer (pH 7.5)
6.2
D-glucose 6-phosphate
pH 7.0, 50ưC, native enzyme
6.7
D-glucose 6-phosphate
mutant enzyme E495Q, at 21ưC in 20 mM HEPES buffer (pH 7.5)
7.4
D-glucose 6-phosphate
mutant enzyme D511N, at 21ưC in 20 mM HEPES buffer (pH 7.5)
8.5
D-glucose 6-phosphate
pH 7.0, 50ưC, recombinant enzyme
72
D-glucose 6-phosphate
mutant enzyme H396L, at 21ưC in 20 mM HEPES buffer (pH 7.5)
90
D-glucose 6-phosphate
mutant enzyme Q388A, at 21ưC in 20 mM HEPES buffer (pH 7.5)
450
D-glucose 6-phosphate
mutant enzyme N154Q, at 21ưC in 20 mM HEPES buffer (pH 7.5)
489
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37ưC
490
D-glucose 6-phosphate
mutant enzyme S185A, at 21ưC in 20 mM HEPES buffer (pH 7.5)
517
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37ưC
610
D-glucose 6-phosphate
mutant enzyme N386A, at 21ưC in 20 mM HEPES buffer (pH 7.5)
618
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37ưC
715
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37ưC
790
D-glucose 6-phosphate
mutant enzyme Y274F, at 21ưC in 20 mM HEPES buffer (pH 7.5)
906
D-glucose 6-phosphate
-
immobilized-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60ưC
957
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60ưC
1100
D-glucose 6-phosphate
mutant enzyme Y341F, at 21ưC in 20 mM HEPES buffer (pH 7.5)
1218
D-glucose 6-phosphate
-
avicel-cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60ưC
1308
D-glucose 6-phosphate
-
cellulose-binding module-phosphoglucose isomerase, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60ưC
1700
D-glucose 6-phosphate
wild type enzyme, at 21ưC in 20 mM HEPES buffer (pH 7.5)
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