2.7.2.3: phosphoglycerate kinase
This is an abbreviated version!
For detailed information about phosphoglycerate kinase, go to the full flat file.
Word Map on EC 2.7.2.3
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2.7.2.3
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glyceraldehyde-3-phosphate
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x-linked
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aldolase
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enolase
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x-chromosome
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hexokinase
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erythrocyte
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phosphofructokinase
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glucose-6-phosphate
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gapdh
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marrow
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lentiviral
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anemia
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trypanosoma
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hypoxanthine
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triosephosphate
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hematopoietic
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mutase
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glyceraldehyde
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brucei
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hypoxia-inducible
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hemolytic
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phosphoribosyltransferase
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cytomegalovirus
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glycosomal
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triose
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x-chromosome-linked
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tpi
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x-inactivation
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methylation-sensitive
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myoglobinuria
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n-domain
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genorm
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calvin
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hif-1alpha
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hpaii
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mgadp
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fructose-1,6-bisphosphate
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fructose-bisphosphate
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2,3-diphosphoglycerate
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myeloproliferative
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self-inactivating
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phosphoglucose
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microbody
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ligation-mediated
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atp-generating
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glucosephosphate
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alpha-enolase
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medicine
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phosphoribulokinase
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allozyme
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analysis
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biofuel production
- 2.7.2.3
- glyceraldehyde-3-phosphate
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x-linked
- aldolase
- enolase
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x-chromosome
- hexokinase
- erythrocyte
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phosphofructokinase
- glucose-6-phosphate
- gapdh
- marrow
-
lentiviral
- anemia
- trypanosoma
- hypoxanthine
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triosephosphate
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hematopoietic
- mutase
- glyceraldehyde
- brucei
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hypoxia-inducible
-
hemolytic
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phosphoribosyltransferase
- cytomegalovirus
- glycosomal
- triose
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x-chromosome-linked
- tpi
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x-inactivation
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methylation-sensitive
- myoglobinuria
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n-domain
-
genorm
-
calvin
- hif-1alpha
- hpaii
- mgadp
- fructose-1,6-bisphosphate
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fructose-bisphosphate
- 2,3-diphosphoglycerate
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myeloproliferative
-
self-inactivating
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phosphoglucose
- microbody
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ligation-mediated
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atp-generating
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glucosephosphate
- alpha-enolase
- medicine
- phosphoribulokinase
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allozyme
- analysis
- biofuel production
Reaction
Synonyms
3-PGK, 3-phosphoglycerate 1-phosphotransferase, 3-phosphoglycerate kinase, 3-phosphoglycerate phosphokinase, 3-phosphoglyceric acid kinase, 3-phosphoglyceric acid phosphokinase, 3-phosphoglyceric kinase, AbPGK, ATP-3-phospho-D-glycerate-1-phosphotransferase, ATP:3-phospho-D-glycerate 1-phosphotransferase, ATP:D-3-phosphoglycerate 1-phosphotransferase, chl-PGK, glycerate 3-phosphate kinase, glycerophosphate kinase, HacPGK1, HacPGK2, HapPGK, hPGK, HsPGK, human 3-phosphoglycerate kinase, kinase (phosphorylating), phosphoglycerate, Mfer_0156, OsPGK2, P-glycerate kinase, PAS-PGK, PfPGK, PGK, PGK 1, PGK-1, PGK-2, pgk-B, PGK1, PGK2, Pgk3, Pgk5, PGKA, PGKase-1, PGKB, PGKC, pgkp1, pgkp2, phosphoglycerate kinase, phosphoglycerate kinase 1, phosphoglycerate kinase 2, phosphoglycerate kinase B, phosphoglycerate kinase-1, phosphoglyceric acid kinase, phosphoglyceric kinase, phosphoglycerokinase, PwPGK, SjPGK, SSO0527, testis-specific phosphoglycerate kinase 2, TRSC58_02767, X chromosome-linked phosphoglycerate kinase-1
ECTree
2.7.2.3 phosphoglycerate kinaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 2.7.2.3 - phosphoglycerate kinase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1,3-bis(difluoro)-1,3-diphospho-2-dihydroxypropane
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phosphonate analogues of 1,3-diphosphoglycerate
1,4-bis(difluoro)-1,4-diphospho-diethylether
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phosphonate analogues of 1,3-diphosphoglycerate
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-diphosphate
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2-(p-Sulfophenylazo)-1,8-dihydroxy-3,6-naphthalene disulfonic acid
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competitive against MgATP2- and 3-phospho-D-glycerate
AMP2-
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competitive to MgATP2-, noncompetitive to 3-phospho-D-glycerate
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
Guanidinium chloride
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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
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competitive against 3-phospho-D-glycerate and noncompetitive against MgATP2-
hydroxyethylidene bisphosphonic acid
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competitive against MgATP2- and 3-phospho-D-glycerate
NaNO2
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inhibition at high concentration, activation at low concentrations
Naphthalene-1,3,6-trisulfonic acid
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competitive against 3-phospho-D-glycerate and noncompetitive against MgATP2-, binding structure
shRNA
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knockdown of PGK, followed by a reduced cytotoxicity of beta-L-dioxolane-cytidine approximately 1.4- and 1.8fold under normoxic and hypoxic conditions, respectively
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Sodium citrate
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inhibition at high concentration, activation at low concentrations
Sodium selenate
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inhibition at high concentration, activation at low concentrations
Sodium succinate
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inhibition at high concentration, activation at low concentrations
(NH4)2SO4
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inhibition at high concentration, activation at low concentrations
2,3-diphosphoglycerate
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competitive to 3-phospho-D-glycerate and MgATP2-
5,5'-dithiobis(2-nitrobenzoic acid)
nucleotide ligands protect, e.g. MgATP2-, MgADP-, Mg-beta,gamma-methylene-adenosine-5'-triphosphate, Mg-beta,gamma-imido-adenosine-5'-triphosphate
ADP
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0.1 mM, 63.1% activity; 0.1 mM, 85% activity; 0.1 mM, 86% activity; 1 mM, 31% activity; 1 mM, 32% activity
ADP
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noncompetitive to ATP and competitive to 3-phospho-D-glycerate
AMP
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0.625 mM, 95% activity; 0.625 mM, 98% activity; 10 mM, 40% activity; 10 mM, 44% activity; 10 mM, 50% activity
AMP
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noncompetitive with respect to 1,3-diphosphoglycerate, ADP and Mg2+, inhibition kinetics
AMP
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above 0.5 mM noncompetitive and below 0.5 mM competitive to 3-phospho-D-glycerate, competitive to MgATP2-
ATP
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very high concentrations of ATP (more than 1 mM) inhibit the enzyme activity
ATP
isoform PGKC is inhibited at concentrations higher than 0.23 mM ATP
ATP4-
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binds to the free enzyme as an inhibitor, when binding to the enzyme-MgATP2-(3-phospho-D-glycerate)complex, ATP4- acts as an activator
ATP4-
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inhibition at high concentration, acceleration of activity at low concentrations
glycerol 3-phosphate
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10 mM, 92% activity; 10 mM, 95% activity; 10 mM, 97% activity
iodoacetamide
nucleotide ligands protect, e.g. MgATP2-, MgADP-, Mg-beta,gamma-methylene-adenosine-5'-triphosphate, Mg-beta,gamma-imido-adenosine-5'-triphosphate
KH2PO4
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inhibition at high concentration, activation at low concentrations
Mg2+
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at pH 7.5, the catalytic activity of full-length enzyme is decreased with increasing concentration of Mg2+
NaCl
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inhibition at high concentration, acceleration of activity at low concentrations
NaCl
the enzyme is negatively affected by NaCl at concentrations above 150 mM; the enzyme is negatively affected by NaCl at concentrations above 150 mM
nucleoside diphosphates
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inhibition of ADP formation in decreasing order: GDP, ADP, IDP
nucleoside diphosphates
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inhibition of ADP formation in decreasing order: GDP, ADP, IDP
nucleoside diphosphates
Esox sp.
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inhibition of ADP formation in decreasing order: GDP, ADP, IDP
nucleoside diphosphates
Frog
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inhibition of ADP formation in decreasing order: GDP, ADP, IDP
nucleoside diphosphates
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inhibition of ADP formation in decreasing order: GDP, ADP, IDP
nucleoside diphosphates
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inhibition of ADP formation in decreasing order: GDP, ADP, IDP
nucleoside diphosphates
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inhibition of ADP formation in decreasing order: GDP, ADP, IDP
nucleoside diphosphates
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inhibition of ADP formation in decreasing order: GDP, ADP, IDP
nucleoside diphosphates
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inhibition of ADP formation in decreasing order: GDP, ADP, IDP
SO42-
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behaves as an inhibitor at MgATP2- and 3-phospho-D-glycerate concentration below 0.5-1 mM, as an activator at higher substrate concentrations
Zn2+
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ZnATP2- is an alternative substrate to MgATP2-, free metal ions strongly inhibit
Zn2+
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ZnATP2- is an alternative substrate to MgATP2-, free metal ions strongly inhibit
Zn2+
Esox sp.
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ZnATP2- is an alternative substrate to MgATP2-, free metal ions strongly inhibit
Zn2+
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ZnATP2- is an alternative substrate to MgATP2-, free metal ions strongly inhibit
Zn2+
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ZnATP2- is an alternative substrate to MgATP2-, free metal ions strongly inhibit
Zn2+
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ZnATP2- is an alternative substrate to MgATP2-, free metal ions strongly inhibit
Zn2+
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ZnATP2- is an alternative substrate to MgATP2-, free metal ions strongly inhibit
Zn2+
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ZnATP2- is an alternative substrate to MgATP2-, free metal ions strongly inhibit
additional information
PGK1 activity is inhibited by the formation of a single regulatory disulfide bond Cys227-Cys361 with a low midpoint redox potential
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additional information
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PGK1 activity is inhibited by the formation of a single regulatory disulfide bond Cys227-Cys361 with a low midpoint redox potential
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additional information
no effects by glycerol-2-phosphate, glycerol-3-phosphate, glucose-6-phosphate, fructose-6-phosphate, fructose-1, 6-bisphosphate, phosphoenolpyruvate, pyruvate, acetate, L-lysine, L-alanine, L-glutamate, GTP, and AMP on the enzyme activity
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additional information
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no effects by glycerol-2-phosphate, glycerol-3-phosphate, glucose-6-phosphate, fructose-6-phosphate, fructose-1, 6-bisphosphate, phosphoenolpyruvate, pyruvate, acetate, L-lysine, L-alanine, L-glutamate, GTP, and AMP on the enzyme activity
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additional information
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Mg2+ binding through PAS domain inhibits the enzyme activity at pH 7.5. This inhibition is withdrawn at pH 5.5
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additional information
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no effect by glucose 6-phosphate, fructose 6-phosphate, fructose 1,6-phosphate, pyruvate, phosphoenolpyruvate and lactate
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additional information
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the KH-type splicing regulatory protein, KSRP, serves as a decay-promoting factor for Pgk2 mRNA in male germ cells. KSRP binds to to a 93-nt sequence (the F1 region) of the 3'-UTR of the Pgk2 mRNA and destabilizes Pgk2 mRNA constructs in testis extracts and in transfected cells. Destabilization of Pgk2 mRNA occurs when t-KSRP and the Pgk2 mRNA-stabilizing protein, polypyrimidine tract binding protein 2 (PTBP2), are present together in complexes bound to the 3'-UTR of Pgk2 mRNA
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additional information
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yeast enzyme is insensitive to thiol reagents
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additional information
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yeast enzyme is insensitive to thiol reagents
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additional information
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inhibitory effect of phosphonate analogues of 1,3-diphosphoglycerate, overview
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additional information
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double-inhibition studies, kinetics, modeling of inhibitor binding, e.g. phosphate; enzyme is regulated by multivalent anions, overview
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additional information
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addition of sinefungin prior to actinomycin D is the best protocol for complete and rapid inhibition of mRNA synthesis, thus in bloodstream forms, inhibition of both trans splicing and transcription results in immediate exponential decay of PGKC mRNA with a half-life of 46 min. Inhibition of transcription alone gives non-exponential kinetics and inhibition of splicing alone results in a longer apparent half-life
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