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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 .
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,
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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
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Glucose phosphate isomerase
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Glucose phosphoisomerase
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Glucosephosphate isomerase 2
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Hexose 6-phosphate isomerase
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Hexose monophosphate isomerase
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Hexose phosphate isomerase
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Hexosephosphate isomerase
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Isomerase, glucose phosphate
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Phosphoglucoisomerase
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Phosphoglucose isomerase
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Phosphohexoisomerase
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Phosphohexomutase
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Phosphohexose isomerase
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Phosphosaccharomutase
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Vegetative protein 54
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alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
multistep catalytic mechanism, model including catalytically active amino acids
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intramolecular oxidoreduction
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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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].
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D-glucose 6-phosphate
D-fructose 6-phosphate
Fructose 6-phosphate
Glucose 6-phosphate
Glucose 6-phosphate
Fructose 6-phosphate
additional information
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D-glucose 6-phosphate
D-fructose 6-phosphate
multistep catalytic mechanism is proposed: first the enzyme catalyzes ring opening to yield the open chain form of the substrate. Then isomerization proceeds via proton transfer between C2 and C1 of a cis-enediol(ate) intermediate to yield the open chain form of the product. His388 promotes ring opening by protonating the ring oxygen. Glu216 helps to position His388, and a water molecule that is held in position by Lys518 and Thr214 accepts a proton from the hydroxyl group at C2
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r
D-glucose 6-phosphate
D-fructose 6-phosphate
the active site residues Lys58 and His388 might be involved in catalytic mechanism
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D-glucose 6-phosphate
D-fructose 6-phosphate
in the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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Fructose 6-phosphate
Glucose 6-phosphate
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r
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Glucose 6-phosphate
Fructose 6-phosphate
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Glucose 6-phosphate
Fructose 6-phosphate
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r
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additional information
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the enzyme plays important roles in glycolysis and gluconeogenesis
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additional information
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the enzyme plays important roles in glycolysis and gluconeogenesis
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D-glucose 6-phosphate
D-fructose 6-phosphate
in the cytoplasm, it catalyzes the second step in glycolysis. Outside the cell, it serves as a nerve growth factor and cytokine
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additional information
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additional information
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the enzyme plays important roles in glycolysis and gluconeogenesis
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additional information
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the enzyme plays important roles in glycolysis and gluconeogenesis
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D-gluconate 6-phosphate
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fructose 1,6-diphosphate
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0.01 - 0.74
fructose 6-phosphate
0.03 - 0.8
glucose 6-phosphate
0.01 - 0.17
fructose 6-phosphate
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muscle enzyme, values of 0.01 mM, 0.12 mM and 0.17 mM are determined by different authors
0.1
fructose 6-phosphate
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0.1
fructose 6-phosphate
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glucose 6-phosphate, soluble enzyme
0.119
fructose 6-phosphate
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0.12
fructose 6-phosphate
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liver enzyme
0.2
fructose 6-phosphate
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glucose 6-phosphate, immobilized enzyme
0.21
fructose 6-phosphate
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erythrocyte enzyme, wild-type
0.74
fructose 6-phosphate
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erythrocyte enzyme, mutant B9
0.03 - 0.8
glucose 6-phosphate
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muscle enzyme, values of 0.03 mM, 0.31 mM and 0.8 mM are determined by different authors
0.6
glucose 6-phosphate
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liver enzyme
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8
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soluble and immobilized enzyme
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6 - 10
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pH 6.0: about 70% of maximal activity of soluble enzyme, about 30% of maximal activity of immobilized enzyme
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30 - 60
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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
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Uniprot
brenda
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brenda
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brenda
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skeletal
brenda
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brenda
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G6PI_RABIT
558
0
62747
Swiss-Prot
Mitochondrion (Reliability: 5 )
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dimer
the enzyme is a dimer with two alpha/beta-sandwich domains in each subunit
dimer
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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
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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
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6
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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
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highest stability of soluble enzyme
2849
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45
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soluble enzyme, t1/2: 42 min. Immobilized enzyme, t1/2: 82 min
50
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soluble enzyme, t1/2: 12 min. Immobilized enzyme, t1/2: 10 min
55
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soluble enzyme, t1/2: 2 min. Immobilized enzyme, t1/2: 1 min
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immobilization increases the stability against urea
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8-10°C, storage stability of enzyme immobilized on different carriers, overview
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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.
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brenda
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
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brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda