Information on EC 5.3.1.9 - Glucose-6-phosphate isomerase

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The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria

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EC NUMBER
COMMENTARY hide
5.3.1.9
-
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RECOMMENDED NAME
GeneOntology No.
Glucose-6-phosphate isomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-Glucose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,3-propanediol biosynthesis (engineered)
-
-
1,5-anhydrofructose degradation
-
-
Amino sugar and nucleotide sugar metabolism
-
-
Bifidobacterium shunt
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
chitin biosynthesis
-
-
formaldehyde oxidation I
-
-
GDP-mannose biosynthesis
-
-
gluconeogenesis I
-
-
gluconeogenesis II (Methanobacterium thermoautotrophicum)
-
-
gluconeogenesis III
-
-
glycolysis
-
-
Glycolysis / Gluconeogenesis
-
-
glycolysis I (from glucose 6-phosphate)
-
-
glycolysis III (from glucose)
-
-
glycolysis V (Pyrococcus)
-
-
heterolactic fermentation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Pentose phosphate pathway
-
-
sorbitol biosynthesis I
-
-
Starch and sucrose metabolism
-
-
starch biosynthesis
-
-
sucrose biosynthesis I (from photosynthesis)
-
-
sucrose biosynthesis II
-
-
sucrose biosynthesis III
-
-
sucrose degradation II (sucrose synthase)
-
-
sucrose degradation III (sucrose invertase)
-
-
sucrose degradation IV (sucrose phosphorylase)
-
-
UDP-N-acetyl-D-galactosamine biosynthesis II
-
-
UDP-N-acetyl-D-glucosamine biosynthesis I
-
-
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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 hide
9001-41-6
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.
Swissprot
Manually annotated by BRENDA team
Spanish, Indian and American honeybee
-
-
Manually annotated by BRENDA team
syncytia induced by nematode Heterodera schachtii
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
plastid and cytosolic isoenzyme
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Cassia coluteoides
isoenzyme PGI I and II
-
-
Manually annotated by BRENDA team
collected from the Mar Menor coastal lagoon
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
guar
-
-
Manually annotated by BRENDA team
UTEX-LB-1644
UniProt
Manually annotated by BRENDA team
Dunaliella salina UTEX-LB-1644
UTEX-LB-1644
UniProt
Manually annotated by BRENDA team
H, Wey, and Wis strains
UniProt
Manually annotated by BRENDA team
Entamoeba sp.
-
-
-
Manually annotated by BRENDA team
K10
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
plastid and cytosolic isoenzyme
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8 resp.
Swissprot
Manually annotated by BRENDA team
Trypanosoma brucei Treu 927
strain Treu 927 GUTat 10.1
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
D-fructose 6-phosphate
D-mannose 6-phosphate
show the reaction diagram
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
D-Mannose 6-phosphate
D-Fructose 6-phosphate
show the reaction diagram
fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
r
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
L-talose
L-tagatose
show the reaction diagram
-
best aldose substrate
-
-
?
malonic dialdehyde
methylglyoxal
show the reaction diagram
-
-
-
-
r
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
additional information
?
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activates 5.2fold 1.5 mM
Cu2+
-
activates 1.3fold 1.5 mM
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
Ni2+
-
activates 4.5fold 1.5 mM
Zinc
wild-type enzyme contains 0.24 mol zinc per mol of dimer
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
-
3-phosphoglycerate
-
-
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-arabinonate
5-phospho-D-arabinonohydroxamate
-
competitive, stable analogue of putative cis-endiol intermediate
5-phospho-D-arabinonohydroxamic acid
-
-
5-phosphoarabinonate
-
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-phosphogluconate
6-Phosphomannonate
Cassia coluteoides
-
with glucose 6-phosphate as substrate
Agaricic acid
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-Fructose 1-phosphate
D-Glucal 6-phosphate
-
-
D-glucitol 6-phosphate
-
comparison with inhibition of Candida albicans D-glucosamine 6-phosphate synthase
D-gluconate 6-phosphate
D-mannose 6-phosphate
dihydroxyacetone phosphate
-
-
Erythritol 4-phosphate
-
-
erythrose 4-phosphate
erythrose-4-phosphate
-
-
fructose 1,6-diphosphate
fructose 1-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
Maleic anhydride
-
-
malonate
-
10 mM, 15% inhibition
mannitol 1-phosphate
Cassia coluteoides
-
glucose 6-phosphate as substrate
mannitol 6-phosphate
-
-
mannose 6-phosphate
-
-
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
phosphate
ribose 5-phosphate
ribulose 5-phosphate
sedoheptulose 7-phosphate
sorbitol 6-phosphate
-
-
sorbitol-6-phosphate
suramin
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
IMAGE
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003 - 650
D-fructose 6-phosphate
0.04 - 2765
D-glucose 6-phosphate
3330
fructose 6-phosphate
Homo sapiens
-
isomerase a
475.5
L-talose
Pyrococcus furiosus
-
pH 7.0, 95°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02 - 162
D-fructose 6-phosphate
2.7 - 1700
D-glucose 6-phosphate
3.58
L-talose
Pyrococcus furiosus
-
pH 7.0, 95°C
6883
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.3
2-amino-2-deoxy-D-glucitol 6-phosphate
-
pH 8.0
17.2
2-amino-2-deoxy-D-mannitol 6-phosphate
-
pH 8.0
0.68
2-Deoxy-D-glucitol 6-phosphate
-
pH 8.0
0.0046
5-phospho-D-arabinoamide
-
pH 8.0
0.0022
5-phospho-D-arabinoate
-
pH 8.0
0.27
5-phospho-D-arabinonate
-
50°C
0.005
5-phospho-D-arabinonohydroxamate
-
50°C
0.00023
5-phospho-D-arabinonohydroxamic acid
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.148
6-phospho-D-gluconate
-
pH 8.0
0.56
6-phospho-D-gluconoamide
-
pH 8.0
0.02 - 58
6-phosphogluconate
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
0.04
D-glucitol 6-phosphate
-
pH 8.0
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
2 - 120
EDTA
0.035 - 1.8
erythrose 4-phosphate
0.0014
erythrose-4-phosphate
-
pH 7.4, 50°C
0.8
gluconate 6-phosphate
-
pH 7.6, 22°C
10
Maleate
-
-
5.54
N,2,3,4,5-pentahydroxypentanamide
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
0.076
N-acetyl-2-amino-2-deoxy-D-glucitol 6-phosphate
-
pH 8.0
0.03 - 0.7
sorbitol-6-phosphate
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.29
5-deoxy-5-malonate-D-arabinonohydroxamic acid
Saccharomyces cerevisiae
-
in 50 mM HEPES buffer, pH 7.1, at 25°C
-
0.00005 - 0.0002
5-phosphoarabinonhydroxamic acid
0.01
Agaricic acid
Trypanosoma brucei
P13377
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.009
-
pH 7.5, 37°C, activity in undialyzed cell extracts
0.06
-
substrate: D-fructose 6-phosphate, 80°C, pH not specified in the publication
0.39
-
purified native enzyme
7.7
-
50°C, pH 7.0
12
-
70°C, pH 7.0
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
43
-
with D-fructose 6-phosphate as substrate, at 90°C and pH 6.0
47.3
formation of D-glucose 6-phosphate
48.5
purified recombinant His-tagged enzyme
140
-
purified enzyme, substrate fructose 6-phosphate, reverse reaction
212.6
-
22°C, pH 7.4
500
-
D-glucose 6-phosphate formation, isomerase c
520
-
-
600
-
D-glucose 6-phosphate formation, isomerase b
617.7
-
pH 7.6, 22°C
870
-
D-glucose 6-phosphate formation, isomerase a
1470
-
fructose 6-phosphate formation
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
ribose 5-phosphate, enzyme form A
6 - 11
Cassia coluteoides
-
isoenzyme PGI I
7 - 11
Cassia coluteoides
-
isoenzyme PGI II
7
-
ribose 5-phosphate, enzyme form B
7 - 9.5
8
-
assay at, reverse reaction
8.3
-
-
9.5
-
in glycine-NaCl-NaOH buffer
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3 - 7
-
50% of maximal activity at pH 6.3 and pH 7.0
6 - 10
-
pH 6.0: about 70% of maximal activity of soluble enzyme, about 30% of maximal activity of immobilized enzyme
6 - 8
-
about 50% of maximal activity above pH 6.0 and below pH 8.0
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
6.3 - 8.8
-
more than 50% of maximum activity in this range
6.5 - 8.5
-
pH profile, overview
7 - 10
-
about 50% of maximal activity at pH 7 and at pH 10
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 RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
40 - 98
-
temperature profile, overview
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 hide
LITERATURE
5.1
-
calculated from amino acid sequence
6.22
-
sequence calculation
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
colon carcinomas show increased PGI expression compared to control cells, overview
Manually annotated by BRENDA team
-
3 enzyme variants are due to a specific intracellular cleavage of the enzyme in the malignant cells
Manually annotated by BRENDA team
-
enzyme localizes to actively growing hyphal tips
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
PGI activity in vesicle fluid
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
peripheral blood mononuclear cell
Manually annotated by BRENDA team
Cassia coluteoides
-
developing and germinating
Manually annotated by BRENDA team
-
synovial fluid
Manually annotated by BRENDA team
-
peroxisome/plasmalogen-deficient variant of the CHO-K1 cell line
Manually annotated by BRENDA team
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Escherichia coli (strain K12)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)