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Information on EC 5.3.1.9 - glucose-6-phosphate isomerase and Organism(s) Geobacillus stearothermophilus and UniProt Accession P13376

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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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Geobacillus stearothermophilus
UNIPROT: P13376
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Word Map
The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
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
autocrine motility factor
-
6-Phosphoglucose isomerase
-
-
-
-
D-Glucose-6-phosphate isomerase
-
-
-
-
D-glucose-6-phosphate ketol-isomerase
-
-
-
-
Glucose 6-phosphate isomerase
-
-
-
-
Glucose phosphate isomerase
-
-
-
-
Glucose phosphoisomerase
-
-
-
-
Glucosephosphate isomerase 2
-
-
-
-
GPI
-
-
-
-
Hexose 6-phosphate isomerase
-
-
-
-
Hexose isomerase
-
-
-
-
Hexose monophosphate isomerase
-
-
-
-
Hexose phosphate isomerase
-
-
-
-
Hexosephosphate isomerase
-
-
-
-
Isomerase, glucose phosphate
-
-
-
-
Neuroleukin
-
-
-
-
NLK
-
-
-
-
Oxoisomerase
-
-
-
-
PGI
-
-
-
-
PGI2
-
-
-
-
PGI3
-
-
-
-
PHI
-
-
-
-
Phosphoglucoisomerase
-
-
-
-
Phosphoglucose isomerase
-
-
-
-
Phosphohexoisomerase
-
-
-
-
Phosphohexomutase
-
-
-
-
Phosphohexose isomerase
-
-
-
-
Phosphosaccharomutase
-
-
-
-
SA-36
-
-
-
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Sperm antigen-36
-
-
-
-
VEG54
-
-
-
-
Vegetative protein 54
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
intramolecular oxidoreduction
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Glucose 6-phosphate
Fructose 6-phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-phospho-D-arabinonate
-
N-bromoacetylethanolamine phosphate
-
6-phosphogluconate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.048
fructose 6-phosphate
-
-
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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?
G6PI2_GEOSE
445
0
50141
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
172000
-
sedimentation equilibrium analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal strcuture at 2.3 A resolution
hanging drop vapor diffusion method, crystal structure of the enzyme complexed with 5-phospho-D-arabinonate and N-bromoacetylethanolamine phosphate at 2.5 A and 2.3 A resolution, respectively. The inhibitors bind to a region within the domains interface and interact with His306 from the other subunit
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
25% loss of activity after 1 h
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C or -20°C, 20 mM Tris-acetate buffer, pH 8.0, stable for 1 month
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozyme A and B overexpressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nosoh, Y.
Glucose-6-phosphate isomerase from Bacillus stearothermophilus
Methods Enzymol.
41B
383-387
1975
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Marchand, M.; Kooystra, U.; Wierenga, R.K.; Lambeir, A.M.; van Beeumen, J.; Opperdoes, F.R.; Michels, P.A.M.
Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of the enzyme
Eur. J. Biochem.
184
455-464
1989
Geobacillus stearothermophilus, Saccharomyces cerevisiae, Oryctolagus cuniculus, Trypanosoma brucei
Manually annotated by BRENDA team
Hsiao, C.D.; Chou, C.C.; Hsiao, Y.Y.; Sun, Y.J.; Meng, M.
Expression, purification, and crystallization of two isozymes of 6-phosphoglucose isomerase of Bacillus stearothermophilus
J. Struct. Biol.
120
196-200
1997
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Chou, C.C.; Sun, Y.J.; Meng, M.; Hsiao, C.D.
The crystal structure of phosphoglucose isomerase/autocrine motility factor/neuroleukin complexed with its carbohydrate phosphate inhibitors suggests its substrate/receptor recognition
J. Biol. Chem.
275
23154-23160
2000
Geobacillus stearothermophilus (P13376)
Manually annotated by BRENDA team
Sun, Y.J.; Chou, C.C.; Chen, W.S.; Wu, R.T.; Meng, M.; Hsiao, C.D.
The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin
Proc. Natl. Acad. Sci. USA
96
5412-5417
1999
Geobacillus stearothermophilus (P13376), Geobacillus stearothermophilus
Manually annotated by BRENDA team