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Information on EC 5.3.1.9 - glucose-6-phosphate isomerase and Organism(s) Oryctolagus cuniculus and UniProt Accession Q9N1E2

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EC Tree
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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Oryctolagus cuniculus
UNIPROT: Q9N1E2
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Word Map
The taxonomic range for the selected organisms is: Oryctolagus cuniculus
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
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6-Phosphoglucose isomerase
-
-
-
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D-Glucose-6-phosphate isomerase
-
-
-
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D-glucose-6-phosphate ketol-isomerase
-
-
-
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Glucose 6-phosphate isomerase
-
-
-
-
Glucose phosphate isomerase
-
-
-
-
Glucose phosphoisomerase
-
-
-
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Glucosephosphate isomerase 2
-
-
-
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GPI
-
-
-
-
Hexose 6-phosphate isomerase
-
-
-
-
Hexose isomerase
-
-
-
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Hexose monophosphate isomerase
-
-
-
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Hexose phosphate isomerase
-
-
-
-
Hexosephosphate isomerase
-
-
-
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Isomerase, glucose phosphate
-
-
-
-
Neuroleukin
-
-
-
-
NLK
-
-
-
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Oxoisomerase
-
-
-
-
PGI
-
-
-
-
PGI2
-
-
-
-
PGI3
-
-
-
-
PHI
-
-
-
-
Phosphoglucoisomerase
-
-
-
-
Phosphoglucose isomerase
-
-
-
-
Phosphohexoisomerase
-
-
-
-
Phosphohexomutase
-
-
-
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Phosphohexose isomerase
-
-
-
-
Phosphosaccharomutase
-
-
-
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SA-36
-
-
-
-
Sperm antigen-36
-
-
-
-
VEG54
-
-
-
-
Vegetative protein 54
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
show the reaction diagram
multistep catalytic mechanism, model including catalytically active amino acids
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
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
Fructose 6-phosphate
Glucose 6-phosphate
show the reaction diagram
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
D-glucose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
in the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-gluconate 6-phosphate
-
6-phosphogluconate
-
-
D-Glucal 6-phosphate
-
-
fructose 1,6-diphosphate
-
-
fructose 1-phosphate
-
-
suramin
-
no inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.74
fructose 6-phosphate
0.03 - 0.8
glucose 6-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
soluble and immobilized enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
pH 6.0: about 70% of maximal activity of soluble enzyme, about 30% of maximal activity of immobilized enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
immobilized enzyme
50 - 55
-
soluble enzyme
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
G6PI_RABIT
558
0
62747
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000 - 140000
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
the enzyme is a dimer with two alpha/beta-sandwich domains in each subunit
dimer
-
2 * 60000-70000, SDS-PAGE, SDS velocity centrifugation, maleic anhydride velocity and equilibrium sedimentation, urea velocity sedimentation, propionic acid velocity sedimentation guanidine-HCl velocity and equilibrium sedimentation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with the competitive inhibitor D-gluconate 6-phosphate, X-ray crystallography at 2.5 A resolution
hanging drop vapor diffusion method, X-ray crystal structure of the enzyme complexed with the cyclic form of its substrate, D-fructose 6-phosphate, at 2.1 A resolution
in complex with D-sorbitol 6-phosphate
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
immobilized enzyme: no marked change in the first few hours at different pH levels from pH 6.0-9.0, after a longer incubation the highest stability is measured at pH 6.0
2849
8
-
highest stability of soluble enzyme
2849
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
soluble enzyme, t1/2: 42 min. Immobilized enzyme, t1/2: 82 min
50
-
soluble enzyme, t1/2: 12 min. Immobilized enzyme, t1/2: 10 min
55
-
soluble enzyme, t1/2: 2 min. Immobilized enzyme, t1/2: 1 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
immobilization increases the stability against urea
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
8-10°C, storage stability of enzyme immobilized on different carriers, overview
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Noltmann, E.A.
Aldose-ketose isomerases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
271-354
1972
Apis mellifera, Aspergillus niger, Bos taurus, Canis lupus familiaris, Entamoeba sp., Escherichia coli, Homo sapiens, Klebsiella aerogenes, Mycobacterium tuberculosis, Oryctolagus cuniculus, Pisum sativum, Rattus norvegicus, Saccharomyces cerevisiae, Schistosoma mansoni, Sus scrofa, Trypanosoma sp.
-
Manually annotated by BRENDA team
Simon, L.M.; Kotorman, M.; Szajani, B.; Boross, L.
Preparation and characterization of immobilized glucose-phosphate isomerase
Enzyme Microb. Technol.
8
222-226
1986
Oryctolagus cuniculus
-
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
Chenault, H.K.; Mandes, R.F.
Selective inhibition of metabolic enzymes by enzymatically synthesized D-glucal-6-phosphate
Bioorg. Med. Chem.
2
627-629
1994
Oryctolagus cuniculus
Manually annotated by BRENDA team
Jeffery, C.J.; Bahnson, B.J.; Chien, W.; Ringe, D.; Petsko, G.A.
Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukin, autocrine motility factor, and differentiation mediator
Biochemistry
39
955-964
2000
Oryctolagus cuniculus (Q9N1E2), Oryctolagus cuniculus
Manually annotated by BRENDA team
Lee, J.H.; Chang, K.Z.; Patel, V.; Jeffery, C.J.
Crystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate
Biochemistry
40
7799-7805
2001
Oryctolagus cuniculus (Q9N1E2), Oryctolagus cuniculus
Manually annotated by BRENDA team
Lee, J.H.; Jeffery, C.J.
The crystal structure of rabbit phosphoglucose isomerase complexed with D-sorbitol-6-phosphate, an analog of the open chain form of D-glucose-6-phosphate
Protein Sci.
14
727-734
2005
Oryctolagus cuniculus (Q9N1E2), Oryctolagus cuniculus
Manually annotated by BRENDA team