Information on EC 2.7.2.10 - phosphoglycerate kinase (GTP)

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The expected taxonomic range for this enzyme is: Entamoeba histolytica

EC NUMBER
COMMENTARY hide
2.7.2.10
-
RECOMMENDED NAME
GeneOntology No.
phosphoglycerate kinase (GTP)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + 3-phospho-D-glycerate = GDP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
GTP:3-phospho-D-glycerate 1-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
62213-34-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
HM1:IMSS
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
show the reaction diagram
-
in glycolytic direction selectivity for GDP over ADP is 150-fold, selectivity for GTP over ATP is about 50fold
-
-
r
GDP + 3-phospho-D-glyceroyl 1-phosphate
GTP + 3-phospho-D-glycerate
show the reaction diagram
GTP + 3-phospho-D-glycerate
GDP + 3-phospho-D-glyceroyl 1-phosphate
show the reaction diagram
ITP + 3-phospho-D-glycerate
IDP + 3-phospho-D-glyceroyl 1-phosphate
show the reaction diagram
-
in glycolytic direction 40% of the activity with GDP, 30% of the activity with GTP
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-
r
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GDP + 3-phospho-D-glyceroyl 1-phosphate
GTP + 3-phospho-D-glycerate
show the reaction diagram
-
production of GTP
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GDP
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displays higher activity with GDP/GTP and lower affinities for the adenine nucleotides
GTP
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displays higher activity with GDP/GTP and lower affinities for the adenine nucleotides
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
3-phosphoglycerate
-
pH 7, 30C
10
ADP
-
pH 7, 30C
1.2
ATP
-
pH 7, 30C
0.07 - 0.802
GDP
0.016 - 0.348
GTP
0.7
IDP
-
pH 7, 30C
0.8
ITP
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pH 7, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52
-
GDP + 3-phospho-D-glyceroyl phosphate
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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wild-type, mutants V311L and Y239F/E309Q incubated for 1-12 min do not show drastic reductions in activity at 50C. 30% of their initial activities decay after 1 min incubation at 60C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
upon concentration by vacuum dialysis against 20 mM imidazole buffer, pH 7, a loss of about 40% of activity occurs
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-22C, 50% glycerol (v/v), 4-7 months
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4C, concentrated enzyme solution, 10% loss of activity per week
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and mutants purified by metal-affinity chromatography, mutants purified more than 98%
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mutant proteins cloned into the pGEM-T-easy vector, further cloned into the pET28 expression vector, wild-type and mutants overexpressed as N-terminal histidine-tailed recombinant proteins in Escherichia coli BL21DE3pLysS cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E309M
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increases catalytic efficiency (Vm/Km) with ADP/ATP as a result of both, increased Vm and decreased Km values
E309Q
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increases catalytic efficiency (Vm/Km) with ADP/ATP as a result of both, increased Vm and decreased Km values
V311L
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increases catalytic efficiency (Vm/Km) with ADP/ATP as a result of both, increased Vm and decreased Km values. Is monomeric as the wild-type
Y239F
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increases catalytic efficiency (Vm/Km) with ADP/ATP as a result of both, increased Vm and decreased Km values
Y239F/E309M
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higher catalytic efficiency in the double mutant is achieved mainly due to an increased affinity for ADP/ATP with a concomitant diminished affinity for GDP/GTP. Is monomeric as the wild-type