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Information on EC 2.7.2.3 - phosphoglycerate kinase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P00560

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Saccharomyces cerevisiae
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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, phosphoglycerate kinase 2, 3-pgk, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP:3-phospho-D-glycerate 1-phosphotransferase
-
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
-
-
phosphoglycerate kinase 1
-
-
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
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
show the reaction diagram
2'-deoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2'-deoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
show the reaction diagram
-
isozyme PGK1
-
-
?
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
show the reaction diagram
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
-
-
-
r
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
beta-L(-)-dioxolanecytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L(-)-dioxolanecytidine 5'-diphosphate + 1,3-diphosphoglycerate
show the reaction diagram
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L-2',3'-dideoxy-3'-thiacytidine 5'-diphosphate + 1,3-diphosphoglycerate
show the reaction diagram
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
show the reaction diagram
-
no activity
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
r
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dITP + 3-phospho-D-glycerate
dIDP + 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
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
enzyme is identical with the socalled host factor, which activates RNA transcription in Sendai virus, when bound in a complex with host tubulin and a complementary factor
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
required as phosphate donor
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required for activity
divalent cation
KH2PO4
-
inhibition at high concentration, acceleration of activity at low concentrations
Mn2+
-
can partially replace Mg2+ in activation
NaCl
-
inhibition at high concentration, acceleration of activity at low concentrations
NaNO2
-
inhibition at high concentration, acceleration of activity at low concentrations
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
-
inhibition at high concentration, activation at low concentrations
1,3-bis(difluoro)-1,3-diphospho-2-dihydroxypropane
-
phosphonate analogues of 1,3-diphosphoglycerate
1,3-bisphosphoglycerate
-
-
1,4-bis(difluoro)-1,4-diphospho-diethylether
-
phosphonate analogues of 1,3-diphosphoglycerate
1,4-Bisphosphonobutane
-
-
1,5-Bisphosphonopentane
-
-
2-(p-Sulfophenylazo)-1,8-dihydroxy-3,6-naphthalene disulfonic acid
-
competitive against MgATP2- and 3-phospho-D-glycerate
2-Hydroxy-3,5-diiodobenzoate
-
-
2-Hydroxy-5-iodobenzoate
-
-
2-Oxo-1,4-bisphosphonobutane
-
-
2-Oxo-1,5-bisphosphonopentane
-
-
3-phospho-D-glycerate
-
-
4-Phosphonobutyronitrile
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
ADP3-
-
competitive to 3-phospho-D-glycerate
AMP2-
-
competitive to MgATP2-, noncompetitive to 3-phospho-D-glycerate
ATP4-
Co2+
-
CoATP2- is the true substrate
Guanidinium chloride
-
0.5 M, 30% loss of activity for the mutant P204H, 5% loss of activity for the wild-type, both are unfolded at 1 M
Hexametaphosphate
-
competitive against 3-phospho-D-glycerate and noncompetitive against MgATP2-
hydroxyethylidene bisphosphonic acid
-
competitive against MgATP2- and 3-phospho-D-glycerate
inositol triphosphate
-
-
KH2PO4
-
inhibition at high concentration, activation at low concentrations
MgADP-
-
competitive to 3-phospho-D-glycerate
NaCl
-
inhibition at high concentration, acceleration of activity at low concentrations
NaNO2
-
inhibition at high concentration, activation at low concentrations
Naphthalene-1,3,6-trisulfonic acid
-
competitive against 3-phospho-D-glycerate and noncompetitive against MgATP2-, binding structure
nucleoside diphosphates
-
inhibition of ADP formation in decreasing order: GDP, ADP, IDP
nucleoside monophosphates
-
-
p-chloromercuribenzoate
-
-
salicylate
-
i.e. 2-hydroxybenzoate
SO42-
Sodium citrate
-
inhibition at high concentration, activation at low concentrations
Sodium selenate
-
inhibition at high concentration, activation at low concentrations
Sodium succinate
-
inhibition at high concentration, activation at low concentrations
sulphasalazine
-
-
suramin
-
competitive against MgATP2- and 3-phospho-D-glycerate
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
-
inhibition at high concentration, acceleration of activity at low concentrations
ATP4-
SO42-
-
behaves as an inhibitor at MgATP2- and 3-phospho-D-glycerate concentration below 0.5-1 mM, as an activator at higher substrate concentrations
Sodium citrate
-
inhibition at high concentration, acceleration of activity at low concentrations
Sodium selenate
-
inhibition at high concentration, acceleration of activity at low concentrations
Sodium succinate
-
inhibition at high concentration, acceleration of activity at low concentrations
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.28
3-phospho-D-glycerate
pH and temperature not specified in the publication
0.1 - 0.18
ADP
0.48
ATP
pH and temperature not specified in the publication
0.146 - 2.5
3-phospho-D-glycerate
0.00438
3-phospho-D-glyceroyl phosphate
-
at pH 7.4, temperature not specified in the publication
0.2 - 0.5
ADP
0.04 - 1.25
ATP
3.45
dATP
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
963.1
ADP
enzymatic activity in bulk condition
3.4 - 354
3-phospho-D-glycerate
3.4 - 354
ATP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.44 - 1.5
1,3-bis(difluoro)-1,3-diphospho-2-dihydroxypropane
-
pH 7.5, 25°C
3.25 - 3.3
1,4-bis(difluoro)-1,4-diphospho-diethylether
-
pH 7.5, 25°C
0.56
1,4-Bisphosphonobutane
-
pH 8.5, 27°C
1.19
1,5-Bisphosphonopentane
-
pH 8.5, 27°C
0.1 - 0.15
2-(p-Sulfophenylazo)-1,8-dihydroxy-3,6-naphthalene disulfonic acid
0.065 - 0.075
2-Hydroxy-3,5-diiodobenzoate
0.06
2-Hydroxy-5-iodobenzoate
-
versus 3-phospho-D-glycerate, pH 7.8, 25°C
0.084
2-Oxo-1,4-bisphosphonobutane
-
pH 8.5, 27°C
0.2
2-Oxo-1,5-bisphosphonopentane
-
pH 8.5, 27°C
3.5
4-Phosphonobutyronitrile
-
pH 8.5, 27°C
0.17 - 0.22
ADP3-
1.5 - 2
AMP
1.5
AMP2-
-
pH 7.8, 25°C
1.28
Hexametaphosphate
-
pH 7.5, versus 3-phospho-D-glycerate
23 - 25
hydroxyethylidene bisphosphonic acid
5.5
Naphthalene-1,3,6-trisulfonic acid
-
pH 7.5, versus 3-phospho-D-glycerate
0.009 - 0.011
salicylate
0.13 - 0.16
suramin
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Saccharomyces cerevisiae
-
IC50 values are predicted within a factor of ca. 4 over a 2500x range in activity
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.4
-
purified mutant P204F
4.5
-
purified mutant P204H
468
-
purified wild-type enzyme
700
-
purified muscle enzyme
785
-
purified enzyme
850
-
purified enzyme
945
-
purified eenzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
calculated from amino acid sequence
4.3 - 4.4
-
thin-layer isoelectric focusing
4.8
-
thin-layer isoelectric focusing
5.3
-
thin-layer isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
commercial product
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
overexpression of PGK1 can restore normal ageing of cells and suppress other apoptotic phenotypes of the MCY4/313Kllsm4DELTA1 mutant strain, including chromatin fragmentation and sensitivity to acetic acid, H2O2 and caffeine
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000 - 47000
-
gel filtration, ultracentrifugation, amino acid analysis, tryptophan content
45000 - 48000
-
gel filtration
46000
-
x * 46000, SDS-PAGE
50000
-
1 * 50000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
monomer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization from ammonium sulfate precipitation, pH 7.0, room temperature, a few days, X-ray structure determination, in presence of 1% 1,4-dioxane and 68% ammonium sulfate, and analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P204F
-
site-directed mutagenesis, mutation in the hinge region of the enzyme, which plays a role in protein folding during catalysis, less well folded with considerable loss of secondary and tertiary structure, no activity
P204H
R203P
-
three-dimensional structure analysis, kcat is reduced by 10-20%, mostly unaltered kinetic parameter, decreased stability compared to the wild-type
W308F
-
mutant enzyme is fully active, thermal stability is slightly decreased with respect to wild-type enzyme
W308F/W333F
-
mutant enzyme is fully active, thermal stability is slightly decreased with respect to wild-type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24
-
two stable, folded conformers with an abrupt conformational transition occurring at 24°C. The transition state thermodynamics for the low- to high-temperature conformational change are calculated from slow-scan-rate differential scanning calorimetry measurements where it is found that the free energy barrier for the conversion is 90 kJ/mol and the transition state possesses a significant unfolding quality
48
-
midpoint temperature Tm, without a ligand, mutant enzyme W308F/W333F, value determined by differential scanning calometry
49
-
midpoint temperature Tm, with MgATP2- as ligand, mutant enzyme W308F/W333F, value determined by differential scanning calometry
51
-
midpoint temperature Tm, with 3-phosphoglycerate as ligand, mutant enzyme W308F/W333F, value determined by differential scanning calometry
52
-
midpoint temperature Tm, with MgADP- as ligand, mutant enzyme W308F/W333F, value determined by differential scanning calometry
53
-
midpoint temperature Tm, without a ligand, mutant enzyme W333F, value determined by differential scanning calometry
54
-
midpoint temperature Tm, mutant enzyme W308F/W333F, with 3-phosphoglycerate and MgADP- as ligand, value determined by differential scanning calometry
59
-
midpoint temperature Tm, mutant enzyme W333F, with 3-phosphoglycerate and MgADP- as ligand, value determined by differential scanning calometry
61
-
midpoint temperature Tm, with MgADP- as ligand, wild-type enzymne, value determined by differential scanning calometry
63
-
midpoint temperature Tm, with 3-phosphoglycerate and MgADP- as ligand, wild-type enzyme, value determined by differential scanning calometry
additional information
-
thermal analysis
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme shows highest thermal stability in ternary complex with 3-phosphoglycerate and MgADP-, due to domain closure
-
Pro204 is important for stability and catalytic mechanism of the enzyme
-
the extrapolated unfolding rate of Escherichia coli PGK is 100000 slower than that of the yeast homolog
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 50 mM phosphate buffer, pH 6.2
-
-80°C, 50 mM Tris buffer, 1 mM EDTA, 1 mM DTT, pH 7.8
-
as a precipitate in 3.3 M ammonium sulfate, stable for years
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Strep-Tactin Sepharose column chromatography
further purification of the commercial product
-
to homogeneity, by gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C41(DE3) pLysS cells
histidine-tagged PGK
-
into vector pET27b and expressed in Escherichia coli BL21 (DE3)pLysS cells
-
overexpression in Saccharomyces cerevisiae
-
pRS313/Kllsm4DELTA1 plasmid, carrying a truncated form of the KlLSM4 gene of Kluyveromyces lactis introduced into yeast strain MCY4. Overexpression of the glycolitic gene PGK1 in MCY4/313Kllsm4DELTA1
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
first quantitative analysis of the binding of alkyl bisphosphonates to yeast PGK, with activities being predicted within, on average, a factor of 4 over a 2500x overall range in activity
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Janson, C.A.; Cleland, W.W.
The inhibition of acetate, pyruvate, and 3-phosphogylcerate kinases by chromium adenosine triphosphate
J. Biol. Chem.
249
2567-2571
1974
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Watson, H.C.; Bryant, T.N.; Walker, N.P.C.; Shaw, P.J.; Wendell, P.L.
The active site of yeast phosphoglycerate kinase
Biochem. Soc. Trans.
5
652-654
1977
Saccharomyces cerevisiae, Equus caballus
Manually annotated by BRENDA team
Li, Y.K.; Byers, L.D.
Phosphonate inhibitors of glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase
Biochim. Biophys. Acta
1164
17-21
1993
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Larsson-Raznikiewicz, M.; Schierbeck, B.
Activation and inhibition of the phosphoglycerate kinase reaction by ATP
Biochim. Biophys. Acta
481
283-287
1977
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Khamis, M.M.; Larsson-Raznikiewicz, M.
Activation and inhibition of phosphoglycerate kinase by sulphate ion
Biochim. Biophys. Acta
657
190-194
1981
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Larsson-Raznikiewicz, M.; Arvidsson, L.
Inhibition of phosphoglycerate kinase by products and product homologues
Eur. J. Biochem.
22
506-512
1971
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Larsson-Raznikiewicz, M.; Wiksell, E.
Inhibition of phosphoglycerate kinase by salicylates
Biochim. Biophys. Acta
523
94-100
1978
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Boyle, H.A.; Fairbrother, W.J.; Williams, R.J.P.
An NMR analysis of the binding of inhibitors to yeast phosphoglycerate kinase
Eur. J. Biochem.
184
535-543
1989
Saccharomyces cerevisiae
Manually annotated by BRENDA team
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
Kuntz, G.W.K.; Krietsch, W.K.G.
Phosphoglycerate kinase from spinach, blue-green algae, and yeast
Methods Enzymol.
90
110-114
1982
Saccharomyces cerevisiae, Spinacia oleracea, Spirulina geitleri, Arthrospira platensis
-
Manually annotated by BRENDA team
Kulbe, K.D.; Bojanovski, M.
3-Phosphoglycerate kinase from bovine liver and yeast
Methods Enzymol.
90
115-120
1982
Bos taurus, Saccharomyces cerevisiae
-
Manually annotated by BRENDA team
Scopes, R.K.
3-Phosphoglycerate kinase of baker's yeast
Methods Enzymol.
42C
134-138
1975
Saccharomyces cerevisiae
-
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
Ritco-Vonsovici, M.; Mouratou, B.; Minard, P.; Desmadril, M.; Yon, J.M.; Andrieux, M.; Leroy, E.; Guittet, E.
Role of the C-terminal helix in the folding and stability of yeast phosphoglycerate kinase
Biochemistry
34
833-841
1995
Saccharomyces cerevisiae
Manually annotated by BRENDA team
McHarg, J.; Littlechild, J.A.
Studies with inhibitors of the glycolytic enzyme phosphoglycerate kinase for potential treatment of cardiovascular and respiratory disorders
J. Pharm. Pharmacol.
48
201-205
1996
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Sherman, M.A.; Chen, Y.; Mas, M.T.
An engineered amino-terminal domain of yeast phosphoglycerate kinase with native-like structure
Protein Sci.
6
882-891
1997
Saccharomyces cerevisiae
Manually annotated by BRENDA team
McHarg, J.; Kelly, S.M.; Price, N.C.; Cooper, A.; Littlechild, J.A.
Site-directed mutagenesis of proline 204 in the 'hinge' region of yeast phosphoglycerate kinase
Eur. J. Biochem.
259
939-945
1999
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Ogino, T.; Iwama, M.; Kinouchi, J.; Shibagaki, Y.; Tsukamoto, T.; Mizumoto, K.
Involvement of a cellular glycolytic enzyme, phosphoglycerate kinase, in Sendai virus transcription
J. Biol. Chem.
274
35999-36008
1999
Bos taurus, Saccharomyces cerevisiae, Oryctolagus cuniculus, Homo sapiens (P00558), Homo sapiens
Manually annotated by BRENDA team
Tougard, P.; Bizebard, T.; Ritco-Vonsovici, M.; Minard, P.; Desmadril, M.
Structure of a circularly permuted phosphoglycerate kinase
Acta Crystallogr. Sect. D
58
2018-2023
2002
Saccharomyces cerevisiae (P00560), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Tougard, P.; Le, T.H.; Minard, P.; Desmadril, M.; Yon, J.M.; Bizebard, T.; Lebras, G.; Dumas, C.
Structural and functional properties of mutant Arg203Pro from yeast phosphoglycerate kinase, as a model of phosphoglycerate kinase-Uppsala
Protein Eng.
9
181-187
1996
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Krishnan, P.; Fu, Q.; Lam, W.; Liou, J.Y.; Dutschman, G.; Cheng, Y.C.
Phosphorylation of pyrimidine deoxynucleoside analog diphosphates: selective phosphorylation of L-nucleoside analog diphosphates by 3-phosphoglycerate kinase
J. Biol. Chem.
277
5453-5459
2002
Saccharomyces cerevisiae, Homo sapiens
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
Balog, E.; Laberge, M.; Fidy, J.
The influence of interdomain interactions on the intradomain motions in yeast phosphoglycerate kinase: a molecular dynamics study
Biophys. J.
92
1709-1716
2007
Saccharomyces cerevisiae (P00560), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Hurth, C.; Tassius, C.; Talbot, J.C.; Maali, A.; Moskalenko, C.; Minard, P.; Aime, J.P.; Argoul, F.
Enzymatic activity of immobilized yeast phosphoglycerate kinase
Biosens. Bioelectron.
22
2449-2455
2007
Saccharomyces cerevisiae (P00560), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Osvath, S.; Herenyi, L.; Zavodszky, P.; Fidy, J.; Koehler, G.
Hierarchic finite level energy landscape model: to describe the refolding kinetics of phosphoglycerate kinase
J. Biol. Chem.
281
24375-24380
2006
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Kotsikorou, E.; Sahota, G.; Oldfield, E.
Bisphosphonate inhibition of phosphoglycerate kinase: quantitative structure-activity relationship and pharmacophore modeling investigation
J. Med. Chem.
49
6692-6703
2006
Saccharomyces cerevisiae, Homo sapiens, Trypanosoma brucei (P07378)
Manually annotated by BRENDA team
Young, T.A.; Skordalakes, E.; Marqusee, S.
Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: modulation of conformational ensembles without altering structure or stability
J. Mol. Biol.
368
1438-1447
2007
Saccharomyces cerevisiae, Escherichia coli, Escherichia coli (P0A799)
Manually annotated by BRENDA team
Osvath, S.; Jackel, M.; Agocs, G.; Zavodszky, P.; Kohler, G.; Fidy, J.
Domain interactions direct misfolding and amyloid formation of yeast phosphoglycerate kinase
Proteins Struct. Funct. Bioinform.
62
909-917
2006
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Ijeoma, O.; Hollowell, H.N.; Bodnar, M.A.; Britt, B.M.
Thermodynamic analysis of the nondenaturational conformational change of bakers yeast phosphoglycerate kinase at 24C
Arch. Biochem. Biophys.
478
206-211
2008
Saccharomyces cerevisiae
Manually annotated by BRENDA team
White, E.M.; Holland, A.R.; MacDonald, G.
Infrared studies reveal unique vibrations associated with the PGK-ATP-3-PG ternary complex
Biochemistry
47
84-91
2008
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Osvath, S.; Quynh, L.M.; Smeller, L.
Thermodynamics and kinetics of the pressure unfolding of phosphoglycerate kinase
Biochemistry
48
10146-10150
2009
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Encalada, R.; Rojo-Dominguez, A.; Rodriguez-Zavala, J.S.; Pardo, J.P.; Quezada, H.; Moreno-Sanchez, R.; Saavedra, E.
Molecular basis of the unusual catalytic preference for GDP/GTP in Entamoeba histolytica 3-phosphoglycerate kinase
FEBS J.
276
2037-2047
2009
Entamoeba histolytica, Entamoeba histolytica HM1:IMSS, Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Manually annotated by BRENDA team
Mazzoni, C.; Torella, M.; Petrera, A.; Palermo, V.; Falcone, C.
PGK1, the gene encoding the glycolitic enzyme phosphoglycerate kinase, acts as a multicopy suppressor of apoptotic phenotypes in S. cerevisiae
Yeast
26
31-37
2009
Saccharomyces cerevisiae
Manually annotated by BRENDA team
McCormick, N.E.; Forget, S.M.; Syvitski, R.T.; Jakeman, D.L.
MgF3- and AlF4- transition state analogue complexes of yeast phosphoglycerate kinase
Biochem. Cell Biol.
95
295-303
2017
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Li, Q.; Scholl, Z.N.; Marszalek, P.E.
Unraveling the mechanical unfolding pathways of a multidomain protein phosphoglycerate kinase
Biophys. J.
115
46-58
2018
Saccharomyces cerevisiae (P00560), Saccharomyces cerevisiae, Escherichia coli (P0A799), Escherichia coli
Manually annotated by BRENDA team
Jin, C.; Zhu, X.; Wu, H.; Wang, Y.; Hu, X.
Perturbation of phosphoglycerate kinase 1 (PGK1) only marginally affects glycolysis in cancer cells
J. Biol. Chem.
295
6425-6446
2020
Saccharomyces cerevisiae, Homo sapiens (P00558), Homo sapiens
Manually annotated by BRENDA team
Kouril, T.; Eicher, J.J.; Siebers, B.; Snoep, J.L.
Phosphoglycerate kinase acts as a futile cycle at high temperature
Microbiology
163
1604-1612
2017
Saccharomyces cerevisiae, Saccharolobus solfataricus
Manually annotated by BRENDA team
Rojas-Pirela, M.; Andrade-Alviarez, D.; Rojas, V.; Kemmerling, U.; Caceres, A.J.; Michels, P.A.; Concepcion, J.L.; Quinones, W.
Phosphoglycerate kinase structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea
Open Biology
10
200302
2020
Geobacillus stearothermophilus, Corynebacterium glutamicum, Oryctolagus cuniculus, Leishmania mexicana mexicana, Phaeodactylum tricornutum, Spinacia oleracea, Spirulina geitleri, Synechocystis sp. PCC 6803, Thermotoga maritima, Zymomonas mobilis, Trypanosoma rangeli (A0A061J5A1), Trypanosoma rangeli (A0A061J9D5), Entamoeba histolytica (N9V9W5), Homo sapiens (P00558), Saccharomyces cerevisiae (P00560), Trypanosoma brucei brucei (P07377), Trypanosoma brucei brucei (P07378), Thermus thermophilus (P09403), Leishmania major (Q27683), Trypanosoma cruzi (Q4D192), Trypanosoma cruzi (Q4D193), Trypanosoma cruzi, Pseudomonas sp. 'TAC II 18' (Q9RBS3), Entamoeba histolytica HM-1:IMSS-A (N9V9W5), Trypanosoma cruzi CL-Brener (Q4D192), Trypanosoma cruzi CL-Brener (Q4D193), Trypanosoma rangeli SC58 (A0A061J5A1), Trypanosoma rangeli SC58 (A0A061J9D5)
Manually annotated by BRENDA team