Information on EC 2.7.2.3 - phosphoglycerate kinase and Organism(s) Sus scrofa

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Sus scrofa


The taxonomic range for the selected organisms is: Sus scrofa

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.2.3
-
RECOMMENDED NAME
GeneOntology No.
phosphoglycerate kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1-butanol autotrophic biosynthesis (engineered)
-
-
Bifidobacterium shunt
-
-
Calvin-Benson-Bassham cycle
-
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formaldehyde assimilation III (dihydroxyacetone cycle)
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-
gluconeogenesis I
-
-
gluconeogenesis III
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glycerol degradation to butanol
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glycolysis I (from glucose 6-phosphate)
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glycolysis II (from fructose 6-phosphate)
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glycolysis III (from glucose)
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glycolysis IV (plant cytosol)
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heterolactic fermentation
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sucrose biosynthesis I (from photosynthesis)
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superpathway of glucose and xylose degradation
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glycolysis
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photosynthesis
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Glycolysis / Gluconeogenesis
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Carbon fixation in photosynthetic organisms
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
ATP:3-phospho-D-glycerate 1-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9001-83-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
show the reaction diagram
-
only traces of activity
-
-
?
additional information
?
-
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
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dATP
-
-
dGTP
-
-
GTP
-
-
ITP
-
-
UTP
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
CaATP2- is the true substrate; can partially replace Mg2+ in activation
Cd2+
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can partially replace Mg2+ in activation; CdATP2- is the true substrate
Co2+
-
can partially replace Mg2+ in activation; CoATP2- is the true substrate
divalent cation
-
absolute requirement
K+
-
slightly activating
Ni2+
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can partially replace Mg2+ in activation; NiATP2- is the true substrate; poor activator
Zn2+
-
can partially replace Mg2+ in activation; ZnATP2- is the true substrate, free metal ions inhibit
additional information
-
no activation by Be2+; no activation by Fe2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-bisphosphoglycerate
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-
1,5-Bisphosphonopentane
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competitive
2,3-diphosphoglycerate
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-
2-Phosphoglycolate
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competitive
3-phospho-D-glycerate
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5,5'-dithiobis(2-nitrobenzoic acid)
adenosine
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-
ATP4-
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beta,gamma-imido-adenosine-5'-triphosphate
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binding structure; i.e. AMP-PNP, an ATP analogue
beta,gamma-methylene-adenosine-5'-triphosphate
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binding structure; i.e. AMP-PCP, an ATP analogue
Co2+
-
CoATP2- is the true substrate
gallic acid
-
-
Glycerol 2-phosphate
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competitive
glycerol 3-phosphate
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competitive
inositol triphosphate
-
-
iodoacetamide
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nucleotide ligands protect, e.g. MgATP2-, MgADP-, Mg-beta,gamma-methylene-adenosine-5'-triphosphate, Mg-beta,gamma-imido-adenosine-5'-triphosphate
Mg-beta,gamma-imido-adenosine-5'-triphosphate
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Mg-beta,gamma-methylene-adenosine-5'-triphosphate
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MgADP-
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MK-401
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nucleoside diphosphates
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inhibition of ADP formation in decreasing order: GDP, ADP, IDP
nucleoside monophosphates
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p-chloromercuribenzoate
-
-
phosphate
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Sulphasalazine
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Zn2+
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ZnATP2- is an alternative substrate to MgATP2-, free metal ions strongly inhibit
[Co(CN)6]3-
-
-
[Fe(CN)6]3-
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[Fe(CN)6]4-
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
enzyme is regulated by multivalent anions, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26
1,5-Bisphosphonopentane
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pH 7.5, 20C, versus 3-phospho-D-glycerate
0.35
2,3-diphosphoglycerate
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pH 7.5, 20C, versus 3-phospho-D-glycerate
4
2-Phosphoglycolate
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pH 7.5, 20C, versus 3-phospho-D-glycerate
9.6
Glycerol 2-phosphate
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pH 7.5, 20C, versus 3-phospho-D-glycerate
0.7
glycerol 3-phosphate
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pH 7.5, 20C, versus 3-phospho-D-glycerate
0.58
Mg-beta,gamma-imido-adenosine-5'-triphosphate
-
pH 7.5, 20C
1.21
Mg-beta,gamma-methylene-adenosine-5'-triphosphate
-
pH 7.5, 20C
0.039
MgADP-
-
pH 7.5, 20C
8.3
phosphate
-
pH 7.5, 20C, versus 3-phospho-D-glycerate
14
sulfate
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pH 7.5, 20C, versus 3-phospho-D-glycerate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
700
-
purified enzyme
1000
-
about, purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000 - 48000
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gel filtration
48000
-
x * 48000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 48000, SDS-PAGE
monomer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme in ternary complex with Mg2+-bound ATP analogue inhibitors Mg-beta,gamma-methylene-adenosine-5'-triphosphate and Mg-beta,gamma-imido-adenosine-5'-triphosphate, and substrate 3-phospho-D-glycerate, hanging drop vapour diffusion method, reservoir solution: 10 mM beta,gamma-methylene-adenosine-5'-triphosphate, 12 mM MgCl2, 10 mM 3-phospho-D-glycerate, 27-28% w/w polyethylene glycol 8000, pH 7.0, 15C, a few weeks, X-ray structure determination and analysis
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enzyme in ternary complex with MgADP and 3-phospho-D-glycerate, X-ray structure determination and analysis of the open and closed conformation during substrate binding
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single crystals of the binary complexes with ATP (at 1.9 A resolution) and MgATP2- (at 2.1 A resolution) are grown in hanging drops, at 15C, within about 2 weeks
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47
-
midpoint temperature Tm, without a ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
48
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midpoint temperature Tm, with MgATP2- as ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
49
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midpoint temperature Tm, with MgADP- as ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
51
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midpoint temperature Tm, with 3-phosphoglycerate and MgADP- as ligand, carboxamidomethylated enzyme
52
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midpoint temperature Tm, with 3-phosphoglycerate as ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
53
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midpoint temperature Tm, without a ligand, unmodified enzyme, value determined by differential scanning calometry
55
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midpoint temperature Tm, with MgATP2- as ligand, unmodified enzyme, value determined by differential scanning calometry
57
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midpoint temperature Tm, with MgADP- as ligand, unmodified enzyme, value determined by differential scanning calometry
58
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midpoint temperature Tm, with 3-phosphoglycerate as ligand, unmodified enzyme, value determined by differential scanning calometry
59
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midpoint temperature Tm, with 3-phosphoglycerate and MgADP- as ligand, unmodified enzyme, value determined by differential scanning calometry
additional information
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-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme shows highest thermal stability in ternary complex with 3-phosphoglycerate and MgADP-, due to domain closure
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE