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

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Sus scrofa
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The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pgk, phosphoglycerate kinase, pgk-1, 3-phosphoglycerate kinase, phosphoglycerate kinase 1, pgk-2, phosphoglycerate kinase-1, phosphoglycerokinase, 3-pgk, phosphoglycerate kinase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-PGK
-
-
-
-
3-phosphoglycerate kinase
3-phosphoglycerate phosphokinase
-
-
-
-
3-phosphoglyceric acid kinase
-
-
-
-
3-phosphoglyceric acid phosphokinase
-
-
-
-
3-phosphoglyceric kinase
-
-
-
-
ATP-3-phospho-D-glycerate-1-phosphotransferase
-
-
-
-
ATP:D-3-phosphoglycerate 1-phosphotransferase
-
-
-
-
glycerate 3-phosphate kinase
-
-
-
-
glycerophosphate kinase
-
-
-
-
kinase (phosphorylating), phosphoglycerate
-
-
-
-
phosphoglycerate kinase 2
-
phosphoglyceric acid kinase
-
-
-
-
phosphoglyceric kinase
-
-
-
-
phosphoglycerokinase
-
-
-
-
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
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:3-phospho-D-glycerate 1-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9001-83-6
-
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 SUBSTRATE
NATURAL 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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dATP
-
-
dGTP
-
-
GTP
-
-
ITP
-
-
UTP
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
divalent cation
-
absolute requirement
K+
-
slightly activating
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-bisphosphoglycerate
-
-
1,5-Bisphosphonopentane
-
competitive
2,3-diphosphoglycerate
-
-
2-Phosphoglycolate
-
competitive
3-phospho-D-glycerate
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
adenosine
-
-
ATP4-
-
-
beta,gamma-imido-adenosine-5'-triphosphate
binding structure; i.e. AMP-PNP, an ATP analogue
beta,gamma-methylene-adenosine-5'-triphosphate
binding structure; i.e. AMP-PCP, an ATP analogue
Co2+
-
CoATP2- is the true substrate
gallic acid
-
-
Glycerol 2-phosphate
-
competitive
glycerol 3-phosphate
-
competitive
inositol triphosphate
-
-
iodoacetamide
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
-
Mg-beta,gamma-methylene-adenosine-5'-triphosphate
-
MK-401
-
-
nucleoside diphosphates
-
inhibition of ADP formation in decreasing order: GDP, ADP, IDP
nucleoside monophosphates
-
-
p-chloromercuribenzoate
-
-
phosphate
-
-
SO42-
-
-
sulphasalazine
-
-
Zn2+
-
ZnATP2- is an alternative substrate to MgATP2-, free metal ions strongly inhibit
[Co(CN)6]3-
-
-
[Fe(CN)6]3-
-
-
[Fe(CN)6]4-
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
enzyme is regulated by multivalent anions, overview
-
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
-
pH 7.5, 20°C, versus 3-phospho-D-glycerate
0.35
2,3-diphosphoglycerate
-
pH 7.5, 20°C, versus 3-phospho-D-glycerate
4
2-Phosphoglycolate
-
pH 7.5, 20°C, versus 3-phospho-D-glycerate
9.6
Glycerol 2-phosphate
-
pH 7.5, 20°C, versus 3-phospho-D-glycerate
0.7
glycerol 3-phosphate
-
pH 7.5, 20°C, versus 3-phospho-D-glycerate
0.58
Mg-beta,gamma-imido-adenosine-5'-triphosphate
pH 7.5, 20°C
1.21
Mg-beta,gamma-methylene-adenosine-5'-triphosphate
pH 7.5, 20°C
0.039
MgADP-
pH 7.5, 20°C
8.3
phosphate
-
pH 7.5, 20°C, versus 3-phospho-D-glycerate
14
sulfate
-
pH 7.5, 20°C, versus 3-phospho-D-glycerate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1000
-
about, purified enzyme
700
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
assay at
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
prepubertal and postpubertal testes of pigs
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PGK2_PIG
417
0
44895
Swiss-Prot
other Location (Reliability: 3)
PGK1_PIG
417
0
44559
Swiss-Prot
other Location (Reliability: 3)
A0A8D0IJ02_PIG
408
0
43518
TrEMBL
Mitochondrion (Reliability: 3)
D0G784_PIG
329
0
35390
TrEMBL
Mitochondrion (Reliability: 5)
A0A5G2R4C4_PIG
398
0
42385
TrEMBL
other Location (Reliability: 2)
Q6T4P4_PIG
95
0
10347
TrEMBL
other Location (Reliability: 2)
A0A8D0IHR8_PIG
387
0
40038
TrEMBL
other Location (Reliability: 1)
A0A8D0MKJ8_PIG
417
0
44846
TrEMBL
other Location (Reliability: 3)
F1RPH0_PIG
417
0
44575
TrEMBL
other Location (Reliability: 3)
A0A8D0S725_PIG
417
0
44873
TrEMBL
other Location (Reliability: 3)
A0A5G2QJC3_PIG
406
0
43478
TrEMBL
other Location (Reliability: 4)
A0A8D0LHN1_PIG
397
0
42348
TrEMBL
other Location (Reliability: 2)
A0A4X1W2A2_PIG
400
0
42560
TrEMBL
other Location (Reliability: 2)
A0A4X1W292_PIG
417
0
44575
TrEMBL
other Location (Reliability: 3)
A0A8D0IJ29_PIG
406
0
43478
TrEMBL
other Location (Reliability: 4)
K7GKJ8_PIG
400
0
42560
TrEMBL
other Location (Reliability: 2)
X4ZHK0_PIG
417
0
44895
TrEMBL
other Location (Reliability: 3)
A0A8D1GHS3_PIG
391
0
41548
TrEMBL
other Location (Reliability: 3)
Q6T4P3_PIG
112
0
12341
TrEMBL
other Location (Reliability: 3)
A0A8D0I7M4_PIG
395
0
41297
TrEMBL
other Location (Reliability: 2)
A0A4X1VWX9_PIG
398
0
42385
TrEMBL
other Location (Reliability: 2)
A0A8D1WAY0_PIG
282
0
31839
TrEMBL
Mitochondrion (Reliability: 2)
A0A8D0I5X0_PIG
409
0
43809
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8D1W8J4_PIG
265
0
29784
TrEMBL
other Location (Reliability: 3)
X4ZFQ2_PIG
417
0
44846
TrEMBL
other Location (Reliability: 3)
Q6T4P2_PIG
88
0
9448
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000 - 48000
-
gel filtration
48000
-
x * 48000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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, 15°C, a few weeks, X-ray structure determination and analysis
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
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 15°C, 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
-
midpoint temperature Tm, with MgATP2- as ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
49
-
midpoint temperature Tm, with MgADP- as ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
51
-
midpoint temperature Tm, with 3-phosphoglycerate and MgADP- as ligand, carboxamidomethylated enzyme
52
-
midpoint temperature Tm, with 3-phosphoglycerate as ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
53
-
midpoint temperature Tm, without a ligand, unmodified enzyme, value determined by differential scanning calometry
55
-
midpoint temperature Tm, with MgATP2- as ligand, unmodified enzyme, value determined by differential scanning calometry
57
-
midpoint temperature Tm, with MgADP- as ligand, unmodified enzyme, value determined by differential scanning calometry
58
-
midpoint temperature Tm, with 3-phosphoglycerate as ligand, unmodified enzyme, value determined by differential scanning calometry
59
-
midpoint temperature Tm, with 3-phosphoglycerate and MgADP- as ligand, unmodified enzyme, value determined by differential scanning calometry
additional information
-
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Scopes, R.K.
3-Phosphoglycerate kinase
The Enzymes, 3rd. Ed. (Boyer, P. D. , ed. )
8
335-351
1973
Saccharomyces cerevisiae, Cyprinus carpio, Oryctolagus cuniculus, Equus caballus, Esox sp., Frog, Homo sapiens, Pisum sativum, Sus scrofa, Testudinidae
-
Manually annotated by BRENDA team
Joao, H.C.; Williams, R.J.P.
The anatomy of a kinase and the control of phosphate transfer
Eur. J. Biochem.
216
1-18
1993
Saccharomyces cerevisiae, Equus caballus, Sus scrofa
Manually annotated by BRENDA team
Scopes, R.K.
3-phosphoglycerate kinase of skeletal muscle
Methods Enzymol.
42C
127-134
1975
Bos taurus, Oryctolagus cuniculus, Equus caballus, Ovis aries, Sus scrofa, Trichosurus vulpecula, Vombatus sp.
-
Manually annotated by BRENDA team
Fifis, T.; Scopes, R.K.
Purification of 3-phosphoglycerate kinase from diverse sources by affinity elution chromatography
Biochem. J.
175
311-319
1978
Abramis brama, Beta vulgaris, Bos taurus, Saccharomyces cerevisiae, Bufo vulgaris, Cyprinus carpio, Gallus gallus, Chrysophrys guttulatus, Columba sp., Oryctolagus cuniculus, Dromaius novaehollandiae, Escherichia coli, Equus caballus, Ovis aries, Macropus fuliginosus, Macropus giganteus, Oncorhynchus mykiss, Pseudocheirus peregrinus, Rattus norvegicus, Salmo trutta, Spinacia oleracea, Sus scrofa, Thylogale billardierii, Trichosurus vulpecula, Vombatus ursinus
Manually annotated by BRENDA team
Szilagyi, A.N.; Vas, M.
Anion activation of 3-phosphoglycerate kinase requires domain closure
Biochemistry
37
8551-8563
1998
Sus scrofa
Manually annotated by BRENDA team
Kovari, Z.; Flachner, B.; Naray-Szabo, G.; Vas, M.
Crystallographic and thiol-reactivity studies on the complex of pig muscle phosphoglycerate kinase with ATP analogues: correlation between nucleotide binding mode and helix flexibility
Biochemistry
41
8796-8806
2002
Sus scrofa (Q7SIB7), Sus scrofa
Manually annotated by BRENDA team
Szilagyi, A.N.; Ghosh, M.; Garman, E.; Vas, M.
A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: new insight into the role of the nucleotide in domain closure
J. Mol. Biol.
306
499-511
2001
Sus scrofa (Q7SIB7), Sus scrofa
Manually annotated by BRENDA team
Flachner, B.; Kovari, Z.; Varga, A.; Gugolya, Z.; Vonderviszt, F.; Naray-Szabo, G.; Vas, M.
Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP
Biochemistry
43
3436-3449
2004
Sus scrofa
Manually annotated by BRENDA team
Varga, A.; Flachner, B.; Graczer, E.; Osvath, S.; Szilagyi, A.N.; Vas, M.
Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase
FEBS J.
272
1867-1885
2005
Saccharomyces cerevisiae, Sus scrofa
Manually annotated by BRENDA team
Park, H.J.; Lee, W.Y.; Park, C.; Hong, K.H.; Kim, J.H.; Song, H.
Species-specific expression of phosphoglycerate kinase 2 (PGK2) in the developing porcine testis
Theriogenology
110
158-167
2018
Mus musculus (P09041), Mus musculus, Sus scrofa (Q6RI85), Sus scrofa
Manually annotated by BRENDA team