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Information on EC 5.3.1.9 - glucose-6-phosphate isomerase and Organism(s) Pyrococcus furiosus and UniProt Accession P83194
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5.3.1.9 glucose-6-phosphate isomeraseIUBMB 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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Word Map
- 5.3.1.9
- gpi
- hexokinase
- phosphoglucomutase
- fructose
- aldolase
-
phosphofructokinase
- malate
- 6-phosphogluconate
- arthritis
- pentose
- erythrocyte
- metastasis
-
allozyme
- starch
-
rheumatoid
- isocitrate
- enolase
- phosphoglycerate
- infestans
- phytophthora
- glyceraldehyde-3-phosphate
-
mating
- glucokinase
-
triosephosphate
- fructose-6-phosphate
-
hemolytic
- isomerases
-
malic
- blight
- triose
- chimaera
- glucose-6-phosphatase
- butterfly
-
monomorphic
- fructose-1,6-bisphosphate
-
zymodeme
- autotaxin
- 1,6-bisphosphate
- fructokinase
-
starch-gel
- drug development
-
nonspherocytic
-
1.1.1.49
-
embden-meyerhof
-
sporangia
-
2.7.1.1
-
tumor-secreted
- erythrose
-
fructose-6-p
-
phosphomannose
- analysis
- medicine
The taxonomic range for the selected organisms is: Pyrococcus furiosus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-Phosphoglucose isomerase
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-
-
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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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-
-
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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
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-
-
-
Neuroleukin
-
-
-
-
NLK
-
-
-
-
Oxoisomerase
-
-
-
-
PGI
PGI2
-
-
-
-
PGI3
-
-
-
-
PHI
-
-
-
-
Phosphoglucoisomerase
-
-
-
-
Phosphoglucose isomerase
Phosphohexoisomerase
-
-
-
-
Phosphohexomutase
-
-
-
-
Phosphohexose isomerase
-
-
-
-
Phosphosaccharomutase
-
-
-
-
SA-36
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-
-
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Sperm antigen-36
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-
-
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VEG54
-
-
-
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Vegetative protein 54
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-
-
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PGI
-
-
-
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Phosphoglucose isomerase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
on the basis of the calculations and simulations, a zwitterionic intermediate mechanism for the low-energy enzymatic reaction is proposed, involving both proton and hydride transfers
-
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
mechanism is based on an enediol intermediate
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
cis-endiol intermediate based mechanism with Glu97 acting as the catalytic base responsible for isomerization
alpha-D-glucose 6-phosphate = beta-D-fructofuranose 6-phosphate
in hydride shift mechanism of catalysis Fe2+ is responsible for proton transfer between O1 and O2, and the hydride shift between C1 and C2 is favored by a markedly hydrophobic environment in the active site. The absence of any obvious enzymatic machinery for catalyzing ring opening of the sugar substrates suggests that the pyrococcal enzyme has a preference for straight chain substrates
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
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-
-
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intramolecular oxidoreduction
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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
9001-41-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glucose 6-phosphate
D-fructose 6-phosphate
in hydride shift mechanism of catalysis Fe2+ is responsible for proton transfer between O1 and O2, and the hydride shift between C1 and C2 is favored by a markedly hydrophobic environment in the active site. The absence of any obvious enzymatic machinery for catalyzing ring opening of the sugar substrates suggests that the pyrococcal enzyme has a preference for straight chain substrates. The metabolism in extreme thermophiles may use sugars in both ring and straight chain forms. At the extreme temperatures in which Pyrococcus furiosus exists, the equilibrium would increasingly favor the open chain forms
-
-
?
additional information
?
-
glucose-6-phosphate isomerase catalyzes the interconversion between two different aldoses and ketose for pentoses and hexoses via two isomerization reactions. Activity order as follows: aldose substrates with hydroxyl groups oriented in the same direction at C2, C3, and C4 better than C2 and C4 better than C2 and C3 better than C3 and C4. L-Talose and D-ribulose exhibit the most preferred substrates among the aldoses and ketoses, respectively, substrate specificity, overview
-
-
?
additional information
?
-
-
glucose-6-phosphate isomerase catalyzes the interconversion between two different aldoses and ketose for pentoses and hexoses via two isomerization reactions. Activity order as follows: aldose substrates with hydroxyl groups oriented in the same direction at C2, C3, and C4 better than C2 and C4 better than C2 and C3 better than C3 and C4. L-Talose and D-ribulose exhibit the most preferred substrates among the aldoses and ketoses, respectively, substrate specificity, overview
-
-
?
additional information
?
-
enzyme does not convert mannose 6-phosphate to fructose 6-phosphate
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-
?
additional information
?
-
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enzyme does not convert mannose 6-phosphate to fructose 6-phosphate
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-
?
additional information
?
-
-
the enzyme is part of the glycolytic pathway
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme is part of the glycolytic pathway
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Fe2+
-
bound to the enzyme. Catalytic activity is not strongly influenced either by the replacement of Fe2+ by a range of transition metals or by the presence or absence of the bound metal ion. The metal may not directly involved in catalysis but rather may be implicated in substrate recognition
additional information
additional information
activity is not affected by addition of Mg2+ or Mn2+
additional information
-
activity is not affected by addition of Mg2+ or Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-phospho-D-arabinonohydroxamate
competitive, stable analogue of putative cis-endiol intermediate
D-fructose 1,6-bisphosphate
10 mM, residual activities are 41% and 53% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively
D-Fructose 1-phosphate
2 mM, residual activities are 50% and 69% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively
D-mannose 6-phosphate
1.25 mM, residual activities are 18% and 38% in the direction of fructose 6-phosphate and glucose 6-phosphate formation, respectively
EDTA
100fold excess, complete loss of activity within 10 min. 93% of activity may be recovered by additon of 1000fold excess of Zn2+
additional information
activity is not affected by addition of 10 mM EDTA. The addition of fructose, glucose, mannose, galactose (10 mM), pyruvate, phosphoenolpyruvate (10 mM), AMP, ADP, or ATP (3.5 mM), does not show any effect on the activity neither in the fructose 6-phosphate formation, nor in the glucose 6-phosphate formation
-
additional information
-
activity is not affected by addition of 10 mM EDTA. The addition of fructose, glucose, mannose, galactose (10 mM), pyruvate, phosphoenolpyruvate (10 mM), AMP, ADP, or ATP (3.5 mM), does not show any effect on the activity neither in the fructose 6-phosphate formation, nor in the glucose 6-phosphate formation
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
IMAGE
additional information
additional information
kinetics for aldose substrates, overview
-
additional information
additional information
-
kinetics for aldose substrates, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14.5
29.1
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 110
70°C: about 40% of maximal activity, 110°C: about 35% of maximal activity
70 - 115
70°C: about 40% of maximal activity, 115°C: about 50% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is part of the Pyrococcus furiosus variant of the Embden-Meyerhof pathway
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21476
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in presence of bound zinc, substrate D-fructose 6-phosphate and several competitive inhibitors
native form and in comlex with 5-phospho-D-arabinonate, in presence and absence of Mn2+
vapor diffusion using the hanging drop method, crystal structure of the enzyme in native form and in complex with two active site ligands, 5-phosphoarabinonate and gluconate 6-phosphate
hanging-drop method of vapour diffusion using 1.6 M sodium citrate as the precipitant at pH 6.5. Maximum resolution of 1.92 A on a single selenomethionine-incorporated crystal. Crystal belongs to space group C2, with approximate unit-cell parameters a = 84.7, b = 42.4, c = 57.3 A, beta = 120.6° and a monomer in the asymmetric unit
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90
additional information
additional information
thermal inactivation follows first-order kinetics
additional information
-
thermal inactivation follows first-order kinetics
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 20fold by heat treatment and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
activity of EDTA-inhibited enzyme is completely restored by addition of manganese
enzyme inactivated by 100fold excess of EDTA can be reactivated by 1000fold excess of of Zn2+
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hansen, T.; Oehlmann, M.; Schonheit, P.
Novel type of glucose-6-phosphate isomerase in the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
183
3428-3435
2001
Pyrococcus furiosus
Verhees, C.H.; Huynen, M.A.; Ward, D.E.; Schiltz, E.; De Vos, W.M.; van der Oost, J.
The phosphoglucose isomerase from the hyperthermophilic archaeon Pyrococcus furiosus is a unique glycolytic enzyme that belongs to the cupin superfamily
J. Biol. Chem.
276
40926-40932
2001
Pyrococcus furiosus (P83194), Pyrococcus furiosus
Berrisford, J.M.; Akerboom, J.; Turnbull, A.P.; de Geus, D.; Sedelnikova, S.E.; Staton, I.; McLeod, C.W.; Verhees, C.H.; Van der Oost, J.; Rice, D.W.; Baker, P.J.
Crystal structure of Pyrococcus furiosus phosphoglucose isomerase: implications for substrate binding and catalysis
J. Biol. Chem.
278
33290-33297
2003
Pyrococcus furiosus
Berrisford, J.M.; Akerboom, J.; Brouns, S.; Sedelnikova, S.E.; Turnbull, A.P.; van der Oost, J.; Salmon, L.; Hardre, R.; Murray, I.A.; Blackburn, G.M.; Rice, D.W.; Baker, P.J.
The structures of inhibitor complexes of Pyrococcus furiosus phosphoglucose isomerase provide insights into substrate binding and catalysis
J. Mol. Biol.
343
649-657
2004
Pyrococcus furiosus (P83194), Pyrococcus furiosus
Berrisford, J.M.; Hounslow, A.M.; Akerboom, J.; Hagen, W.R.; Brouns, S.J.; van der Oost, J.; Murray, I.A.; Michael Blackburn, G.; Waltho, J.P.; Rice, D.W.; Baker, P.J.
Evidence supporting a cis-enediol-based mechanism for Pyrococcus furiosus phosphoglucose isomerase
J. Mol. Biol.
358
1353-1366
2006
Pyrococcus furiosus (P83194), Pyrococcus furiosus
Yoon, R.Y.; Yeom, S.J.; Park, C.S.; Oh, D.K.
Substrate specificity of a glucose-6-phosphate isomerase from Pyrococcus furiosus for monosaccharides
Appl. Microbiol. Biotechnol.
83
295-303
2009
Pyrococcus furiosus (P83194), Pyrococcus furiosus
Akerboom, J.; Turnbull, A.P.; Hargreaves, D.; Fisher, M.; de Geus, D.; Sedelnikova, S.E.; Berrisford, J.M.; Baker, P.J.; Verhees, C.H.; van der Oost, J.; Rice, D.W.
Purification, crystallization and preliminary crystallographic analysis of phosphoglucose isomerase from the hyperthermophilic archaeon Pyrococcus furiosus
Acta Crystallogr. Sect. D
59
1822-1823
2003
Pyrococcus furiosus
Wu, R.; Xie, H.; Cao, Z.; Mo, Y.
Combined quantum mechanics/molecular mechanics study on the reversible isomerization of glucose and fructose catalyzed by Pyrococcus furiosus phosphoglucose isomerase
J. Am. Chem. Soc.
130
7022-7031
2008
Pyrococcus furiosus
Kengen, S.W.; de Bok, F.A.; van Loo, N.D.; Dijkema, C.; Stams, A.J.; de Vos, W.M.
Evidence for the operation of a novel Embden-Meyerhof pathway that involves ADP-dependent kinases during sugar fermentation by Pyrococcus furiosus
J. Biol. Chem.
269
17537-17541
1994
Pyrococcus furiosus
Swan, M.K.; Solomons, J.T.; Beeson, C.C.; Hansen, T.; Schoenheit, P.; Davies, C.
Structural evidence for a hydride transfer mechanism of catalysis in phosphoglucose isomerase from Pyrococcus furiosus
J. Biol. Chem.
278
47261-47268
2003
Pyrococcus furiosus (P83194), Pyrococcus furiosus
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