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

EC NUMBER
COMMENTARY hide
5.3.1.9
-
RECOMMENDED NAME
GeneOntology No.
Glucose-6-phosphate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-Glucose 6-phosphate = D-fructose 6-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
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
-
-
SYSTEMATIC NAME
IUBMB Comments
D-glucose-6-phosphate aldose-ketose-isomerase
Also catalyses the anomerization of D-glucose 6-phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-41-6
-
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
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
?
-
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
?
-
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
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
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
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, 95C
additional information
additional information
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, 95C
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, 95C
6883
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
-
50C
0.005
5-phospho-D-arabinonohydroxamate
-
50C
0.00023
5-phospho-D-arabinonohydroxamic acid
-
in 50 mM HEPES buffer, pH 7.1, at 25C
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
50C, pH 7.5, D-fructose 6-phosphate as substrate
4
D-Fructose 1-phosphate
50C, pH 7.5, D-fructose 6-phosphate as substrate
0.04
D-glucitol 6-phosphate
-
pH 8.0
0.38
D-gluconate 6-phosphate
50C, pH 7.5, D-fructose 6-phosphate as substrate
2.3
D-mannose 6-phosphate
50C, 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, 50C
0.8
gluconate 6-phosphate
-
pH 7.6, 22C
10
Maleate
-
-
5.54
N,2,3,4,5-pentahydroxypentanamide
-
in 50 mM HEPES buffer, pH 7.1, at 25C
0.076
N-acetyl-2-amino-2-deoxy-D-glucitol 6-phosphate
-
pH 8.0
0.03 - 0.7
sorbitol-6-phosphate
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 25C
-
0.00005 - 0.0002
5-phosphoarabinonhydroxamic acid
0.01
Agaricic acid
Trypanosoma brucei
P13377
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.009
-
pH 7.5, 37C, activity in undialyzed cell extracts
0.06
-
substrate: D-fructose 6-phosphate, 80C, pH not specified in the publication
0.39
-
purified native enzyme
7.7
-
50C, pH 7.0
12
-
70C, pH 7.0
14.5
-
50C, pH 7.0, reaction with D-fructose 6-phosphate; pH 7.0, 50C, substrate: D-fructose 6-phosphate
29.1
-
50C, pH 7.0, reaction with D-glucose 6-phosphate; pH 7.0, 50C, substrate: D-glucose 6-phosphate
43
-
with D-fructose 6-phosphate as substrate, at 90C 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
-
22C, 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, 22C
870
-
D-glucose 6-phosphate formation, isomerase a
1470
-
fructose 6-phosphate formation
additional information
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
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
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
-
30C: about 45% of maximal activity of immobilized enzyme, about 35% of maximal activity of soluble enzyme, 60C: 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 50C and 70C, but only about 40% of optimum activity is exhibited at 30C
60 - 95
-
60C: about 30% of maximal activity, 95C: about 30% of maximal activity
70 - 110
-
70C: about 40% of maximal activity, 110C: about 35% of maximal activity
70 - 115
-
70C: about 40% of maximal activity, 115C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
-
calculated from amino acid sequence
6.22
-
sequence calculation
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
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)