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Enzyme Nomenclature
Information on EC 5.3.1.9 - glucose-6-phosphate isomerase
for references in articles please use BRENDA:EC5.3.1.9
Word Map on EC 5.3.1.9
- 5.3.1.9
- gpi
- hexokinase
- phosphoglucomutase
- lactate
- fructose
-
aldolase
- malate
-
phosphofructokinase
- 6-phosphogluconate
- arthritis
- erythrocyte
- metastasis
- pentose
- starch
-
allozyme
- phosphoglycerate
-
rheumatoid
- glyceraldehyde-3-phosphate
- enolase
- isocitrate
- glucose-6-phosphatase
- fructose-6-phosphate
-
triosephosphate
- triose
-
hemolytic
-
isomerases
- infestans
- glucokinase
- phytophthora
-
malic
- 1,6-bisphosphate
- chimaera
-
embden-meyerhof
- fructose-1,6-bisphosphate
- autotaxin
-
starch-gel
-
1.1.1.49
- butterfly
-
monomorphic
-
gluconeogenic
-
zymodeme
-
2.7.1.1
- fructokinase
- glycosome
-
fructose-6-p
- erythrose
-
phosphomannose
- medicine
-
nonspherocytic
- drug development
- analysis
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The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
5.3.1.9
-
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RECOMMENDED NAME
GeneOntology No.
glucose-6-phosphate isomerase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-Glucose 6-phosphate = D-fructose 6-phosphate
-
-
-
-
D-Glucose 6-phosphate = D-fructose 6-phosphate
push-pull mechanism of ring opening in which H388 breaks the O5-C1 bond by donating a proton, and simultaneously, K518 abstracts a proton from the C1 hydroxyl group
D-Glucose 6-phosphate = D-fructose 6-phosphate
mechanism is based on an enediol intermediate
-
D-Glucose 6-phosphate = D-fructose 6-phosphate
multistep catalytic mechanism, model including catalytically active amino acids
-
D-Glucose 6-phosphate = D-fructose 6-phosphate
cis-endiol intermediate based mechanism with Glu97 acting as the catalytic base responsible for isomerization
-
D-Glucose 6-phosphate = D-fructose 6-phosphate
on the basis of the calculations and simulations, a zwitterionic intermediate mechanism for the low-energy enzymatic reaction is proposed, involving both proton and hydride transfers
-
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
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
isomerization
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
D-glucose-6-phosphate aldose-ketose-isomerase
Also catalyses the anomerization of D-glucose 6-phosphate.
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CAS REGISTRY NUMBER
COMMENTARY
9001-41-6
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
Swissprot
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8 resp.
Swissprot
phosphoglucose isomerase-like activity associated with the carboxy-terminal domains of glucosamine-6-phosphate synthase
-
-
native enzyme and mutant enzymes Thr5 to Ile, Thr224 to Met, Gln343 to Arg, and Asp539 to Asn
-
-
bifunctional phosphoglucose isomerase/phosphomannose isomerase, EC 5.3.1.9 and 5.3.1.8, resp.
Uniprot
bifunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.8 and EC5.3.1.9, overexpression in Escherichia coli
-
-
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
-
-
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
Uniprot
enzyme additionally acts as an aldehyde isomerase converting malondialdehyde to methylglyoxal
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
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
metabolism
-
PGI is a key enzyme in glycolysis and glycogenesis catalyzing the second step of glycolysis
metabolism
-
phosphoglucose isomerase is a key enzyme in the glycolysis and glycogenesis pathways
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
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-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
-
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
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
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
?
-
-
enzyme of the oxidative pentose phosphate cycle
-
-
-
additional information
?
-
-
probable role of the enzyme in starch biosynthesis in amyloplasts
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
the enzyme is involved in the modified Embden-Meyerhof pathway
-
-
?
D-glucose 6-phosphate
D-fructose 6-phosphate
Q9N1E2
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
P13377
-
-
-
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 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
?
-
P06744
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
?
-
-
enzyme of the oxidative pentose phosphate cycle
-
-
-
additional information
?
-
-
probable role of the enzyme in starch biosynthesis in amyloplasts
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
wild-type enzyme contains 1.25 mol iron per mol of dimer, mutant enzymes H89A, H91A, E98V and H137A do not contain iron or zinc
Mg2+
Mn2+
Zn2+
additional information
Fe2+
-
bound to the enzyme. Catalytic activity is not strongly influenced either by the replacement of Fe2+ by a range of transition metals or by the presence or absence of the bound metal ion. The metal may not directly involved in catalysis but rather may be implicated in substrate recognition
Fe2+
-
Fe2+ also enhances the enzyme activity but to a lesser extent than Zn2+
Fe2+
10 mM, 37°C, 156% enhancement of the activity of the wild-type enzyme, mutant enzymes H89A, H91A, E98V and H137A do not contain iron or zinc
Mn2+
-
Mn2+ also enhances the enzyme activity but to a lesser extent than Zn2+
Zn2+
-
addition of Zn2+ ions remarkably enhances the enzyme activity (more than 3fold at 0.2 mM)
Zn2+
meta-dependent phosphoglucose isomerase which requires Zn2+ for its activity. 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
additional information
-
activity is not affected by addition of Mg2+ or Mn2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
Co2+
10 mM, 59% inhibition, D-fructose 6-phosphate as substrate
Cu2+
10 mM, 96% inhibition, D-fructose 6-phosphate as substrate
D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
insulin-like growth factor binding protein-3
-
both glycosylated and unglycosylated, binding and inhibition of enzyme
-
N-acetyl-2-amino-2-deoxy-D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
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-phosphate
-
; 2 mM, residual activities are 50% and 69% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively
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
-
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
-
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
Mn2+
10 mM, 18% inhibition, D-fructose 6-phosphate as substrate
Ni2+
10 mM, 84% inhibition, D-fructose 6-phosphate as substrate
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
-
screening for thiazolide inhibitors, diverse compounds, mode of action of thiazolides and structure-activity relationship, overview
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Zn2+
-
the coordination shell of Zn2+ changes significantly from the initial static crystal conformation to the equilibrated state of the enzyme-D-fructose 6-phosphate complex. Although Zn2+ is not directly involved in the reaction, the metal ion as a structural anchor constructs a hydrogen bond wire to connect the substrate to the outer region, providing a potential channel for hydrogen exchange between the substrate and solvent
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.038
D-fructose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant R347H; pH 7.5, 30°C, recombinant mutant R75G
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
0.063
D-fructose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant T195I; pH 7.5, 30°C, recombinant mutant V101M
2
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme G79L; pH 7.4, 70°C, mutant enzyme H82A
0.084
D-glucose 6-phosphate
-
in 50 mM HEPES buffer, pH 7.1, at 25°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)
0.29
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)
0.5
D-glucose 6-phosphate
-
mutant enzyme Q388A, at 21°C in 20 mM HEPES buffer (pH 7.5)
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)
1.02
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
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 37°C
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
2.89
D-glucose 6-phosphate
-
free enzyme, in 100 mM HEPES, 10 mM Mg2+ and 0.5 mM Mn2+, pH 7.5, 60°C
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
0.11 - 0.23
fructose 6-phosphate
-
values of 0.11 mM, 0.15 mM and 0.23 mM are determined by different autors
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
0.3 - 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
8
glucose 6-phosphate
-
glucose 6-phosphate, cytosolic and chloroplastic isoenzyme
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
190
D-fructose 6-phosphate
-
pH 7.5, 30°C, recombinant mutant R472H; pH 7.5, 30°C, recombinant mutant R83W
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)
0.6
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)
21
D-glucose 6-phosphate
-
mutant enzyme H396L, at 21°C in 20 mM HEPES buffer (pH 7.5)
240
D-glucose 6-phosphate
-
mutant enzyme Y274F, at 21°C in 20 mM HEPES buffer (pH 7.5)
340
D-glucose 6-phosphate
-
mutant enzyme Y341F, at 21°C in 20 mM HEPES buffer (pH 7.5)
360
D-glucose 6-phosphate
-
mutant enzyme S185A, at 21°C in 20 mM HEPES buffer (pH 7.5)
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
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
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.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
D-fructose 6-phosphate
pH 7.4, 70°C, mutant enzyme E93D; pH 7.4, 70°C, mutant enzyme H80A
2.7
D-glucose 6-phosphate
-
mutant enzyme H100L, at 21°C in 20 mM HEPES buffer (pH 7.5)
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)
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)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00023
5-phospho-D-arabinonohydroxamic acid
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
12
D-fructose 1,6-bisphosphate
50°C, pH 7.5, D-fructose 6-phosphate as substrate
4
D-Fructose 1-phosphate
50°C, pH 7.5, D-fructose 6-phosphate as substrate
0.38
D-gluconate 6-phosphate
50°C, pH 7.5, D-fructose 6-phosphate as substrate
2.3
D-mannose 6-phosphate
50°C, pH 7.5, D-fructose 6-phosphate as substrate
5.54
N,2,3,4,5-pentahydroxypentanamide
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.29
5-deoxy-5-malonate-D-arabinonohydroxamic acid
Saccharomyces cerevisiae
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.06
-
substrate: D-fructose 6-phosphate, 80°C, pH not specified in the publication
14.5
-
50°C, pH 7.0, reaction with D-fructose 6-phosphate; pH 7.0, 50°C, substrate: D-fructose 6-phosphate
29.1
-
50°C, pH 7.0, reaction with D-glucose 6-phosphate; pH 7.0, 50°C, substrate: D-glucose 6-phosphate
620
additional information
additional information
-
mass spectrometry based method for the direct determination of kinetic konstants of enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.5
7.4
7.5
7.6
8.1
8.5
8.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
-
pH 6.0: about 70% of maximal activity of soluble enzyme, about 30% of maximal activity of immobilized enzyme
6 - 8.5
-
the enzyme shows reversible isomerization activity with fructose 6-phosphate and glucose 6-phosphate between pH 6.0 and pH 8.5
7 - 9
-
free and immobilized enzymes have approximately 75% and 40% of their maximum activity at pH 7.0 and pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
57
70
90
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
-
30°C: about 45% of maximal activity of immobilized enzyme, about 35% of maximal activity of soluble enzyme, 60°C: about 60% of maximal activity of immobilized enzyme, about 65% of maximal activity of immobilized enzyme
50 - 70
-
free and immobilized enzymes retain about 90% of their maximum activity at 50°C and 70°C, but only about 40% of optimum activity is exhibited at 30°C
60 - 95
-
60°C: about 30% of maximal activity, 95°C: about 30% of maximal activity
70 - 110
-
70°C: about 40% of maximal activity, 110°C: about 35% of maximal activity
70 - 115
-
70°C: about 40% of maximal activity, 115°C: about 50% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
colon carcinomas show increased PGI expression compared to control cells, overview
-
3 enzyme variants are due to a specific intracellular cleavage of the enzyme in the malignant cells
-
peroxisome/plasmalogen-deficient variant of the CHO-K1 cell line
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE