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malfunction

-
deficiency of the enzymatic activity in red blood cells causes nonspherocytic hemolytic anemia
malfunction
-
PGI/AMF is correlated with breast cancer and poor prognosis in breast cancer. Inhibition of PGI/AMF expression triggers mesenchymal-to-epithelial transition in aggressive mesenchymal-type breast cancer MD-MB-231 cells
malfunction
-
neuromuscular symptoms are associated with inherited GPI deficiency
malfunction
-
enzyme deficiency leads to nonspherocytic hemolytic anemia
metabolism

-
PGI is a key enzyme in glycolysis and glycogenesis catalyzing the second step of glycolysis
metabolism
-
key enzyme in the AMF signaling pathway, overview
metabolism
-
GPI plays an important role in glycolysis
metabolism
-
PGI is the second enzyme of glycolysis
metabolism
PGI is the second enzyme of glycolysis
metabolism
-
phosphoglucose isomerase is a key enzyme in the glycolysis and glycogenesis pathways
metabolism
Trypanosoma brucei brucei Treu 927
-
PGI is the second enzyme of glycolysis
-
physiological function

-
the enzyme is part of the Pyrococcus furiosus variant of the Embden-Meyerhof pathway
physiological function
-
PGI/AMF is a housekeeping gene product/cytokine that catalyzes a step in glycolysis and gluconeogenesis, and acts as a multifunctional cytokine associated with aggessive tumors. PGI/AMF induces a mesenchymal-like morphologic conversion being a key enzyme for both epithelial-to-mesenchymal transition in the initiating step of cancer metastasis and mesenchymal-to-epithelial transition in the late stage of metastasis during breast cancer progression, overview
physiological function
-
multifunctional protein GPI is an endogenous inhibitor to myofibril-bound serine proteinase, and may play a significant role in the regulation of muscular protein metabolism in vivo
physiological function
-
AMF is critical for the migration, invasion, metastasis, and anti-apoptotic effects of malignant tumor cells, and its multiple roles in tumor progression may be mediated by certain downstream pathways and effectors. Phosphoglucose isomerase/autocrine motility factor promotes melanoma cell migration through ERK activation dependent on autocrine production of interleukin-8, overview
physiological function
phosphoglucose isomerase plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. The enzyme also acts as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator
physiological function
-
the Pgi activity is limiting in the control BL310 strain during growth on lactose or galactose. The level of Pgi enzyme activity controls the level of production of those UDP-glucose and UDP-galactose in galactose
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
physiological function
-
autocrine motility factor/phosphoglucose isomerase (AMF/PGI) regulates endoplasmic reticulm (ER) stress and cell death through control of ER calcium release. AMF/PGI also protects against thapsigargin- and tunicamycin-induced ER stress and apoptosis and suppresses cytosolic Ca2+ homeostasis
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
physiological function
-
phosphoglucose isomerase plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. The enzyme also acts as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator
-
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D-fructose 6-phosphate
D-glucose 6-phosphate
D-fructose 6-phosphate
D-mannose 6-phosphate
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
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
-
-
-
-
?
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
Trypanosoma brucei brucei Treu 927
-
-
-
r
D-glucose 6-phosphate
D-fructose 6-phosphate
Trypanosoma brucei brucei Treu 927
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
-
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 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 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
?
-
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
?
-
-
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
Cu2+
10 mM, 96% 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
-
-
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, 25°C
6-phosphogluconate
-
competitive
Agaricic acid

-
-
Agaricic acid
irreversible inhibition
Cd2+

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
-
complete inhibition
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 70°C 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
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
-
no inhibition by suramin, an anti-trypanosomal drug, and agaricic acid
-
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0.031 - 170
D-fructose 6-phosphate
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, 95°C
additional information
additional information
-
0.031
D-fructose 6-phosphate

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

-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.11
D-glucose 6-phosphate
-
ZR-82 cells, 22°C
0.18
D-glucose 6-phosphate
-
mutant enzyme D511N, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.2 - 1
D-glucose 6-phosphate
-
mutant enzyme H100L, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.23
D-glucose 6-phosphate
-
mutant enzyme E495Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.28
D-glucose 6-phosphate
-
22°C, pH 7.4
0.29
D-glucose 6-phosphate
-
mutant enzyme H396L, at 21°C in 20 mM HEPES buffer (pH 7.5); wild type enzyme, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.3
D-glucose 6-phosphate
-
mutant enzyme Y274F, at 21°C in 20 mM HEPES buffer (pH 7.5); mutant enzyme Y341F, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.4
D-glucose 6-phosphate
-
pH 7.4, 50°C
0.5
D-glucose 6-phosphate
-
mutant enzyme Q388A, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.6
D-glucose 6-phosphate
-
pH 7.4, 50°C
0.72
D-glucose 6-phosphate
80°C, pH 7.4
0.73
D-glucose 6-phosphate
-
mutant enzyme S185A, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.78
D-glucose 6-phosphate
-
mutant enzyme N386A, at 21°C in 20 mM HEPES buffer (pH 7.5)
1
D-glucose 6-phosphate
-
50°C, pH 6.3
1
D-glucose 6-phosphate
-
pH 7.6, 37°C
1
D-glucose 6-phosphate
-
pH 7.2, 37°C
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, 37°C
1.04
D-glucose 6-phosphate
-
mutant enzyme N154Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
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, 37°C
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, 60°C
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, 60°C
1.9
D-glucose 6-phosphate
-
pH 7.4, 80°C
1.9
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
1.99
D-glucose 6-phosphate
-
50°C, pH 7.0, native enzyme; pH 7.0, 50°C
2
D-glucose 6-phosphate
-
50°C, 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, 37°C
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, 60°C
2.58
D-glucose 6-phosphate
-
mutant GroD1 cells, 22°C
2.7
D-glucose 6-phosphate
-
pH 7.4, 50°C
2.89
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
3.5
D-glucose 6-phosphate
80°C, pH 7.4
7.9
D-glucose 6-phosphate
-
80°C, pH 7.0, recombinant enzyme
8.7
D-glucose 6-phosphate
-
80°C, pH 7.0, native enzyme
11.7
D-glucose 6-phosphate
50°C, pH 7.5, wild-type enzyme
221
D-glucose 6-phosphate
-
wild-type, 37°C, pH 8.0
267.4
D-glucose 6-phosphate
-
mutant A346H, 37°C, pH 8.0
0.25
D-mannose 6-phosphate

80°C, pH 7.4
1.1
D-mannose 6-phosphate
80°C, 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
-
glucose 6-phosphate, soluble enzyme
0.1
fructose 6-phosphate
-
fructose 6-phosphate, isozyme 4
0.11 - 0.23
fructose 6-phosphate
-
values of 0.11 mM, 0.15 mM and 0.23 mM are determined by different autors
0.11
fructose 6-phosphate
-
isozyme 3
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
-
glucose 6-phosphate
0.12
fructose 6-phosphate
-
fructose 6-phosphate, at pH 8.6
0.12
fructose 6-phosphate
-
fructose 6-phosphate, enzyme form PGI II
0.122
fructose 6-phosphate
-
-
0.14
fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from germinating seeds
0.1425
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
-
enzyme forms PGI I and PGI II
0.2
fructose 6-phosphate
-
glucose 6-phosphate, immobilized enzyme
0.21
fructose 6-phosphate
-
erythrocyte enzyme, wild-type
0.228 - 0.278
fructose 6-phosphate
-
-
0.23
fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from developing seeds
0.3
fructose 6-phosphate
-
isozyme 1 and 2
0.35
fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from germinating seeds
0.46
fructose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from developing seeds
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
-
at pH 8.6
0.44
glucose 6-phosphate
-
glucose 6-phosphate, enzyme form PGI I and PGI II
0.44
glucose 6-phosphate
-
glucose 6-phosphate
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
0.83
glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from germinating seeds
1.1
glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from germinating seeds
1.3
glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI II from developing seeds
1.5
glucose 6-phosphate
Cassia coluteoides
-
isoenzyme PGI I from developing seeds
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
-
kinetics for aldose substrates, overview
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0003 - 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, 95°C
0.0003
D-fructose 6-phosphate

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

-
kcat below 0.04 s-1mutant enzyme H389L, at 21°C in 20 mM HEPES buffer (pH 7.5); kcat below 0.04 s-1,mutant enzyme K362A, at 21°C in 20 mM HEPES buffer (pH 7.5)
0.3
D-glucose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant S278L
0.6
D-glucose 6-phosphate
-
mutant enzyme H100L, at 21°C in 20 mM HEPES buffer (pH 7.5)
1.3
D-glucose 6-phosphate
-
mutant enzyme D511N, at 21°C in 20 mM HEPES buffer (pH 7.5)
1.6
D-glucose 6-phosphate
-
mutant enzyme E495Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
4 - 5
D-glucose 6-phosphate
-
mutant enzyme Q388A, at 21°C in 20 mM HEPES buffer (pH 7.5)
17
D-glucose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant L487F
21
D-glucose 6-phosphate
-
mutant enzyme H396L, at 21°C in 20 mM HEPES buffer (pH 7.5)
31
D-glucose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant L339P
42
D-glucose 6-phosphate
50°C, pH 7.5, wild-type enzyme
61
D-glucose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant A300P
63
D-glucose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant R347H
80
D-glucose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant T375R
110
D-glucose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant I525T
120
D-glucose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant R83W
130
D-glucose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant R75G
140
D-glucose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant V101M
240
D-glucose 6-phosphate
-
mutant enzyme Y274F, at 21°C in 20 mM HEPES buffer (pH 7.5)
260
D-glucose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant R472H
340
D-glucose 6-phosphate
-
mutant enzyme Y341F, at 21°C in 20 mM HEPES buffer (pH 7.5)
350
D-glucose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant R347C
360
D-glucose 6-phosphate
-
mutant enzyme S185A, at 21°C in 20 mM HEPES buffer (pH 7.5)
380
D-glucose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant T195I
470
D-glucose 6-phosphate
-
mutant enzyme N154Q, at 21°C in 20 mM HEPES buffer (pH 7.5); mutant enzyme N386A, at 21°C in 20 mM HEPES buffer (pH 7.5)
500
D-glucose 6-phosphate
-
wild type enzyme, at 21°C 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, 37°C
750
D-glucose 6-phosphate
-
pH 7.5, 30°C, 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, 37°C
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, 37°C
1000
D-glucose 6-phosphate
-
pH 7.5, 30°C, 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, 37°C
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, 60°C
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, 60°C
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, 60°C
2765
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
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, 95°C
0.02
D-fructose 6-phosphate

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

-
mutant enzyme H100L, at 21°C in 20 mM HEPES buffer (pH 7.5)
6.2
D-glucose 6-phosphate
-
pH 7.0, 50°C, native enzyme
6.7
D-glucose 6-phosphate
-
mutant enzyme E495Q, at 21°C in 20 mM HEPES buffer (pH 7.5)
7.4
D-glucose 6-phosphate
-
mutant enzyme D511N, at 21°C in 20 mM HEPES buffer (pH 7.5)
8.5
D-glucose 6-phosphate
-
pH 7.0, 50°C, recombinant enzyme
72
D-glucose 6-phosphate
-
mutant enzyme H396L, at 21°C in 20 mM HEPES buffer (pH 7.5)
90
D-glucose 6-phosphate
-
mutant enzyme Q388A, at 21°C in 20 mM HEPES buffer (pH 7.5)
450
D-glucose 6-phosphate
-
mutant enzyme N154Q, at 21°C 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, 37°C
490
D-glucose 6-phosphate
-
mutant enzyme S185A, at 21°C 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, 37°C
610
D-glucose 6-phosphate
-
mutant enzyme N386A, at 21°C 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, 37°C
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, 37°C
790
D-glucose 6-phosphate
-
mutant enzyme Y274F, at 21°C 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, 60°C
957
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
1100
D-glucose 6-phosphate
-
mutant enzyme Y341F, at 21°C 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, 60°C
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, 60°C
1700
D-glucose 6-phosphate
-
wild type enzyme, at 21°C in 20 mM HEPES buffer (pH 7.5)
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