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Information on EC 5.3.1.9 - glucose-6-phosphate isomerase and Organism(s) Thermococcus litoralis and UniProt Accession P84140

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IUBMB Comments
The enzyme from yeast catalyses the reversible conversion specifically between the alpha-D-glucose 6-phosphate and beta-D-fructofuranose 6-phosphate. The enzyme also catalyses the anomerization of both D-hexose 6-phosphates .
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Thermococcus litoralis
UNIPROT: P84140
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Word Map
The taxonomic range for the selected organisms is: Thermococcus litoralis
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphoglucose isomerase, glucose-6-phosphate isomerase, glucose phosphate isomerase, autocrine motility factor, phosphoglucoisomerase, phosphohexose isomerase, neuroleukin, pgi/amf, amf/pgi, glucose 6-phosphate isomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6-Phosphoglucose isomerase
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-
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D-Glucose-6-phosphate isomerase
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-
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D-glucose-6-phosphate ketol-isomerase
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-
-
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Glucose 6-phosphate isomerase
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-
-
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Glucose phosphate isomerase
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-
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Glucose phosphoisomerase
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-
-
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Glucosephosphate isomerase 2
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-
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GPI
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-
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Hexose 6-phosphate isomerase
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-
-
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Hexose isomerase
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-
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Hexose monophosphate isomerase
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-
-
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Hexose phosphate isomerase
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-
-
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Hexosephosphate isomerase
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-
-
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Isomerase, glucose phosphate
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-
-
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Neuroleukin
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-
-
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NLK
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-
-
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Oxoisomerase
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-
-
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PGI
-
-
-
-
PGI2
-
-
-
-
PGI3
-
-
-
-
PHI
-
-
-
-
Phosphoglucoisomerase
-
-
-
-
Phosphoglucose isomerase
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-
-
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Phosphohexoisomerase
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-
-
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Phosphohexomutase
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-
-
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Phosphohexose isomerase
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-
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Phosphosaccharomutase
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-
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SA-36
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Sperm antigen-36
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-
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VEG54
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-
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Vegetative protein 54
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
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intramolecular oxidoreduction
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucose-6-phosphate aldose-ketose-isomerase (configuration-inverting)
The enzyme from yeast catalyses the reversible conversion specifically between the alpha-D-glucose 6-phosphate and beta-D-fructofuranose 6-phosphate. The enzyme also catalyses the anomerization of both D-hexose 6-phosphates [7].
CAS REGISTRY NUMBER
COMMENTARY hide
9001-41-6
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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
fructose 6-phosphate
D-glucose 6-phosphate
show the reaction diagram
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
Zinc
wild-type enzyme contains 0.24 mol zinc per mol of dimer
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cd2+
10 mM, 96% inhibition, D-fructose 6-phosphate as substrate
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
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D-gluconate 6-phosphate
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D-mannose 6-phosphate
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EDTA
10 mM, 78% inhibition, D-fructose 6-phosphate as substrate
K+
10 mM, 18% inhibition, D-fructose 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+
10 mM, 89% inhibition, D-fructose 6-phosphate as substrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.59 - 3.5
D-fructose 6-phosphate
11.7
D-glucose 6-phosphate
50°C, pH 7.5, wild-type enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003 - 26
D-fructose 6-phosphate
42
D-glucose 6-phosphate
50°C, pH 7.5, wild-type enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47.3
formation of D-glucose 6-phosphate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
G6PI_THELI
190
0
21720
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E98V
the ratio of turnover number and Km-value is 31373fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H137A
the ratio of turnover number and Km-value is 66.7fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H89A
the ratio of turnover number and Km-value is 2712fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
H91A
the ratio of turnover number and Km-value is 66.7fold lower than that of the wild-type enzyme. The absorption maximum at 420 nm as found in wild-type enzyme is completely lost. Mutant enzyme does not contain iron or zinc or other metal
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jeong, J.J.; Fushinobu, S.; Ito, S.; Jeon, B.S.; Shoun, H.; Wakagi, T.
Characterization of the cupin-type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralis
FEBS Lett.
535
200-204
2003
Thermococcus litoralis (P84140), Thermococcus litoralis
Manually annotated by BRENDA team