Information on EC 2.7.2.3 - phosphoglycerate kinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
2.7.2.3
-
RECOMMENDED NAME
GeneOntology No.
phosphoglycerate kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
mechanism
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
mechanism
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
mechanism
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
mechanism
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
mechanism
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
mechanism
Frog
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
mechanism
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
mechanism
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
sequential mechanism
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
random sequential mechanism
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
rapid equilibrium random mechanism
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
mechanism, substrate-induced effects combine synergistically to induce major conformational changes of the active site to catalytic status
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
C-terminal part is important for full activity
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
residues engaged in 3-phospho-D-glycerate binding: R22, D24, R144, E149, E150, H191, R192, residues engaged in ATP binding: G236, G237, G263, G371, G375, P372, E277, E377, G407, G408, G429-431
P61884
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
substrate binding conformations of the 2 enzyme domains
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
Pro204 is important for stability and catalytic mechanism of the enzyme
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
substrate binding
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
substrate binding
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
active site structure containing 2 tryptophan residues, substrate binding
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
small angle X-ray scattering (SAXS) data on complexes of human PGK (HsPGK) in solution. In combination with deformable elastic network (DEN) refinement a fully open conformation of the apoenzyme is defined, and details are revealed of the relative time spent by the enzyme in the open and closed conformations during catalytic turnover. Together with the crystal structures it is demonstrated that the enzyme strongly favors the open conformation
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
an ordered mechanism is assumed where 3-phospho-D-glycerate and 3-phospho-D-glyceroyl phosphate bind before ADP and ATP, respectively
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
residues engaged in 3-phospho-D-glycerate binding: R22, D24, R144, E149, E150, H191, R192, residues engaged in ATP binding: G236, G237, G263, G371, G375, P372, E277, E377, G407, G408, G429-431
Pyrococcus woesei Vul 4
-
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
an ordered mechanism is assumed where 3-phospho-D-glycerate and 3-phospho-D-glyceroyl phosphate bind before ADP and ATP, respectively
-
-
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
residues engaged in 3-phospho-D-glycerate binding: R22, D24, R144, E149, E150, H191, R192, residues engaged in ATP binding: G236, G237, G263, G371, G375, P372, E277, E377, G407, G408, G429-431
Pyrococcus woesei DSM 3773
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
1-butanol autotrophic biosynthesis
-
Bifidobacterium shunt
-
Biosynthesis of antibiotics
-
Biosynthesis of secondary metabolites
-
Calvin-Benson-Bassham cycle
-
Carbon fixation in photosynthetic organisms
-
formaldehyde assimilation III (dihydroxyacetone cycle)
-
gluconeogenesis I
-
gluconeogenesis III
-
glycerol degradation to butanol
-
glycolysis
BRENDA
BRENDA
BRENDA
Glycolysis / Gluconeogenesis
-
glycolysis I (from glucose 6-phosphate)
-
glycolysis II (from fructose 6-phosphate)
-
glycolysis III (from glucose)
-
glycolysis IV (plant cytosol)
-
glycolysis VI (metazoan)
-
heterolactic fermentation
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
photosynthesis
BRENDA
BRENDA
BRENDA
sucrose biosynthesis I (from photosynthesis)
-
superpathway of glucose and xylose degradation
-
SYSTEMATIC NAME
IUBMB Comments
ATP:3-phospho-D-glycerate 1-phosphotransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-PGK
-
-
-
-
3-phosphoglycerate kinase
-
-
-
-
3-phosphoglycerate kinase
-
-
3-phosphoglycerate kinase
Entamoeba histolytica HM1:IMSS
-
-
-
3-phosphoglycerate kinase
P00558
-
3-phosphoglycerate kinase
P20971
-
3-phosphoglycerate kinase
P20971
-
-
3-phosphoglycerate kinase
P09411
-
3-phosphoglycerate kinase
P61884
-
3-phosphoglycerate kinase
Pyrococcus woesei DSM 3773, Pyrococcus woesei Vul 4
P61884
-
-
3-phosphoglycerate kinase
-
-
3-phosphoglycerate kinase
-
-
-
3-phosphoglycerate kinase
-
-
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
-
-
-
-
hPGK
P00558
-
HsPGK
P00558
-
human 3-phosphoglycerate kinase
-
-
kinase (phosphorylating), phosphoglycerate
-
-
-
-
Mfer_0156
P20971
ordered locus name
Mfer_0156
P20971
ordered locus name
-
P-glycerate kinase
-
-
PfPGK
P27362
-
PGK
-
-
-
-
PGK
Entamoeba histolytica HM1:IMSS
-
-
-
PGK
-, P0A799
-
PGK
Escherichia coli K12
-
-
-
PGK 1
-
-
PGK-1
-
-
PGK1
P00558
-
PGK1
-
-
PGK1
P09411
-
PGK2
P09041
-
phosphoglycerate kinase
-
-
phosphoglycerate kinase
-
-
phosphoglycerate kinase
P00558
-
phosphoglycerate kinase
-
-
phosphoglycerate kinase
-
-
phosphoglycerate kinase 1
-
-
phosphoglycerate kinase 1
-
-
phosphoglycerate kinase 1
P09411
-
phosphoglycerate kinase 1
-
-
phosphoglycerate kinase 2
-
-
phosphoglycerate kinase 2
P09041
-
phosphoglycerate kinase-1
-
-
phosphoglyceric acid kinase
-
-
-
-
phosphoglyceric kinase
-
-
-
-
phosphoglycerokinase
-
-
-
-
PwPGK
P61884
-
SSO0527
P50317
locus name
SSO0527
P50317
locus name
-
X chromosome-linked phosphoglycerate kinase-1
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-83-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
bream
-
-
Manually annotated by BRENDA team
silver beet
-
-
Manually annotated by BRENDA team
silver beet; var. Fordhook giant
-
-
Manually annotated by BRENDA team
Bufo vulgaris
toad
-
-
Manually annotated by BRENDA team
gene PGK1; strain 3153A
SwissProt
Manually annotated by BRENDA team
strain 3153A
SwissProt
Manually annotated by BRENDA team
Chrysophrys guttulatus
red snapper
-
-
Manually annotated by BRENDA team
nubian mutant
-
-
Manually annotated by BRENDA team
Entamoeba histolytica HM1:IMSS
HM1:IMSS
-
-
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12
-
-
Manually annotated by BRENDA team
Esox sp.
-
-
-
Manually annotated by BRENDA team
Frog
-
-
-
Manually annotated by BRENDA team
Tibetan chicken and two lowland breeds (White Leghorn and Shouguang chicken)
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus NCA 1503
NCA 1503
-
-
Manually annotated by BRENDA team
Pacific halibut
-
-
Manually annotated by BRENDA team
isozyme PGK1
GenBank
Manually annotated by BRENDA team
isozyme PGK1
-
-
Manually annotated by BRENDA team
mutant pathological variant phosphoglycerate kinase-Uppsala with R206P
-
-
Manually annotated by BRENDA team
New Guinea human variant
-
-
Manually annotated by BRENDA team
recombinantly expressed in Escherichia coli
GenBank
Manually annotated by BRENDA team
2 isozymes, cytosolic and chloroplastic; cv. Golden Promise
-
-
Manually annotated by BRENDA team
Lactobacillus delbrueckii subsp. lactis NCC88
strain NCC88
-
-
Manually annotated by BRENDA team
Western grey kangaroo
-
-
Manually annotated by BRENDA team
Eastern grey kangaroo
-
-
Manually annotated by BRENDA team
2 isoforms PGK1 and PGK2, probably cytosolic and chloroplastic form
-
-
Manually annotated by BRENDA team
2 isozymes PGKA and PGKB; DBA/2J
-
-
Manually annotated by BRENDA team
2 isozymes: X-chromosome encoded PGK1 and chromosome 17 encoded PGK2, 3 genetic variants of PGK2: PGK2A, PGK2B, PGK2C
-
-
Manually annotated by BRENDA team
; 60-80 day old CD-1 mice
-
-
Manually annotated by BRENDA team
Swiss albino mice
-
-
Manually annotated by BRENDA team
Mus musculus DBA/2J
DBA/2J
-
-
Manually annotated by BRENDA team
ATCC 25978T
-
-
Manually annotated by BRENDA team
ram; testis-specific isozyme PGKB, isozyme PGKA
-
-
Manually annotated by BRENDA team
L. var. Little Marvel
-
-
Manually annotated by BRENDA team
2 isozymes; from human erythrocytes
-
-
Manually annotated by BRENDA team
ringtail possum
-
-
Manually annotated by BRENDA team
gene pgk, strain TACII18
SwissProt
Manually annotated by BRENDA team
TACII18
-
-
Manually annotated by BRENDA team
Pseudomonas sp. TACII18
TACII18
-
-
Manually annotated by BRENDA team
; strain Vul 4, DSM 3773
SwissProt
Manually annotated by BRENDA team
Pyrococcus woesei DSM 3773
-
SwissProt
Manually annotated by BRENDA team
Pyrococcus woesei Vul 4
strain Vul 4, DSM 3773
SwissProt
Manually annotated by BRENDA team
enzyme level in developing rat tissues
-
-
Manually annotated by BRENDA team
strain JCM2524
-
-
Manually annotated by BRENDA team
Rhodopseudomonas palustris JCM2524
strain JCM2524
-
-
Manually annotated by BRENDA team
normal and various site-specific mutant forms
-
-
Manually annotated by BRENDA team
strain BY4741
-
-
Manually annotated by BRENDA team
2 isozymes, cytosolic and chloroplastic; Sorte Noveto
-
-
Manually annotated by BRENDA team
Spirulina geitleri
-
-
-
Manually annotated by BRENDA team
formerly Thermoanaerobium brockii strain Rt8.G4; strain Rt8.G4
-
-
Manually annotated by BRENDA team
Thermoanaerobacter sp. Rt8.G4
strain Rt8.G4
-
-
Manually annotated by BRENDA team
brushtail possum
-
-
Manually annotated by BRENDA team
brushtail possum; vulepeculus
-
-
Manually annotated by BRENDA team
trout
-
-
-
Manually annotated by BRENDA team
bloodstream form, stock 427
-
-
Manually annotated by BRENDA team
cytoplasmic isozyme; glycosomal isozyme 56PGK, gene PGKA
-
-
Manually annotated by BRENDA team
from mammalian blood stream and the gut of tsetse fly; glycosomal PGKA and cytosolic PGKB isozymes
-
-
Manually annotated by BRENDA team
glycosomal PGKA and cytosolic PGKB isozymes
-
-
Manually annotated by BRENDA team
Vombatus sp.
-
-
-
Manually annotated by BRENDA team
ATCC 29191
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
targeted disruption of Pgk2 by homologous recombination eliminates PGK activity in sperm and testis, and severely impairs male fertility, but does not block spermatogenesis. Mating behavior, reproductive organ weights (testis, excurrent ducts, and seminal vesicles), testis histology, sperm counts, and sperm ultrastructure are indistinguishable between Pgk2(-/-) and wild-type mice. Sperm motility and ATP levels are markedly reduced in males lacking PGK2. Pgk2(-/-) males sire occasional pups. Alternative pathways that bypass the PGK step of glycolysis exist. One of these bypass enzymes, acylphosphatase, is active in mouse sperm, perhaps contributing to phenotypic differences between mice lacking GAPDHS or PGK2
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
physiological function
-
PGK1 helps support the interactions between cancer and its microenvironment. A direct and facilitating relationship between CXCL12 and PGK1 levels in the tumor stroma, overexpression of PGK1 increases expression of CXCL12 compared with controls, whereas reducing PGK1 expression decreases expression of CXCL12 levels by cancer-associated fibroblasts. Coimplantation of PGK1-overexpressing fibroblasts with prostate tumor cells promote tumor cell growth in vivo. PGK1 expression in normal fibroblasts stimulates PCalpha proliferation and invasion. Expression of PGK1 and CXCL12 by normal fibroblasts contributes to expression of cancer-associated fibroblast phenotype. Reduced CXCR4 levels in normal fibroblasts that overexpress PGK1
physiological function
-
PGK1 regulates the expression of CXCR4 and beta-catenin at the mRNA and protein levels. PGK1 and CXCR4 regulate their expression reciprocally. Overexpression of PGK1 dramatically increases the invasiveness of gastric cancer cells. Inhibition of CXCR4 in cells overexpressing PGK1 produces only a moderate reduction of invasiveness suggesting that, PGK1 itself has a critical role in tumor invasiveness. PGK1 may be a crucial enzyme in peritoneal dissemination, enhanced expression of PGK1 and its signaling targets CXCR4 and beta-catenin in gastric cancer cells promote peritoneal carcinomatosis
physiological function
P09411
Pgk1/EGFP expression in ovaries is effective in protecting the fecundity of the partial ovaries after ovary allotransplantation
physiological function
-
PGK2 is not required for completion of spermatogenesis, but is essential for sperm motility and male fertility
physiological function
-
phosphoglycerate kinase-1 and histone H4 elicit a significant differential humoral response in cancer sera compared with age- and sex-matched sera from normal patients and patients with chronic pancreatitis and diabetes
physiological function
-
Synechocystis phosphoglycerate kinase is inactivated by oxidation and the oxidized enzyme is easily reduced and reactivated by thioredoxin, suggesting a role for thioredoxin in the control of the redox state of this enzyme
physiological function
-
gluconeogenic pathway
physiological function
-
the enzyme is involved in glycogen catabolism
physiological function
-
gluconeogenic pathway
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2',3'-didehydro-2',3'-dideoxythymidine triphosphate + 3-phospho-D-glycerate
2',3'-didehydro-2',3'-dideoxythymidine diphosphate + 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
-
isozyme PGK1, 3.6fold higher activity compared to 2'-deoxycytidine
-
-
?
2',3'-dideoxy-GTP + 3-phospho-D-glycerate
2',3'-dideoxy-GDP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
2'-dATP + 3-phospho-D-glycerate
2'-dADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
2'-deoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2'-deoxycytidine 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
-
-
?
2'-dGTP + 3-phospho-D-glycerate
2'-dGDP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
2'-dTTP + 3-phospho-D-glycerate
2'-dTDP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
3'-deoxy-3'-azidothymidine triphosphate + 3-phospho-D-glycerate
3'-deoxy-3'-azidothymidine diphosphate + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
show the reaction diagram
-
-
-
-
?
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
show the reaction diagram
-
-
-
-
r
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
show the reaction diagram
-
-
-
-
r
acyclovir triphosphate + 3-phospho-D-glycerate
acyclovir diphosphate + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
ADP + 1,3-bisphosphoglycerate
ATP + 3-phosphoglycerate
show the reaction diagram
-
using the stopped-flow method it is shown that substrate binding kinetics that lead to the formation of the catalytic PGK-1,3-bisphosphoglycerate-ADP complexes are mutually antagonistic with D-ADP, but much less so with L-ADP. A situation that is similar to that for the formation of the abortive PGK-3-phosphoglycerate-ADP complexes
-
-
?
ADP + 3-phospho-D-glyceroyl 1-phosphate
3-phospho-D-glycerate
show the reaction diagram
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl 1-phosphate
3-phospho-D-glycerate
show the reaction diagram
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl 1-phosphate
3-phospho-D-glycerate
show the reaction diagram
-
molecular dynamics simulations reveal, that both in the absence and in the presence of ligands the enzyme exhibits a hinge bending type motion but the characteristics of this motion vary considerably. In the apo form, the enzyme exhibits a hinge bending motion of a relatively small amplitude with a time period around 20 ns while the time period of the complexed form is much longer than simulation time. In both cases there is a hinge at the C-terminal side of helix 7, but the hinge points which are near the substrate binding site change upon binding. The apo form is more flexible, there are more hinge points that contribute with similar significance to the hinge bending motion, while in the ternary complex there is only one dominant hinge point. This is located in the vicinity of the substrates, in loop K13. The binding of ADP rigidifies its binding site in the C-domain, while binding 1,3-diphosphoglycerate increases the flexibility of the binding range of the N-domain
-
-
?
ADP + 3-phospho-D-glyceroyl 1-phosphate
3-phospho-D-glycerate
show the reaction diagram
P18912
overall increases in amide protection from hydrogen exchange when the W290Y mutant protein binds the substrate and product ligands and an additional increase when the transition-state analogue complex containing a 3-phospho-D-glycerate-(AlF4-)-ADP moiety is formed. Communication between domains is manifested in the accessibility of higher-energy, exchange-competent states. For residue D33, chemical shifts only change significantly upon transition-state analogue binding. For residue S346, chemical shifts change significantly upon ADP and transition-state analogue binding. For residue S58, chemical shifts are affected by 3-phospho-D-glycerate and transition-state analogue binding
-
-
?
ADP + 3-phospho-D-glyceroyl 1-phosphate
3-phospho-D-glycerate
show the reaction diagram
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
Entamoeba histolytica, Entamoeba histolytica HM1:IMSS
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl 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
-
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
P00558
-
-
-
?
ADP + 3-phospho-D-glyceroyl 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
-
-
-
-
?
ADP + 3-phospho-D-glyceroyl 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
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
P07378
-
-
-
?
ADP + 3-phospho-D-glyceroyl 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
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-, P20971
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
P61884, -
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
key enzyme in glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
energy charge is the most important factor in regulating the 2 forms of PGK
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
key enzyme of anaerobic glycolysis in Plasmodium falciparum
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
Q08GC7
binding of 3-phospho-D-glycerate (or maybe 1,3-diphosphoglycerate) disrupts salt bridge between Arg148 and Glu375 and enables the formation of a new interdomain salt bridge between Arg60 and Asp197, which stabilizes the closed conformation
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
catalytic residue R38, which also binds the substrate 3-phosphoglycerate, is essential in inducing domain closure. Similarly, residues K219, N336, and E343 which interact with the nucleotide substrates are involved in the process of domain closure. The other catalytic residue, K215, covers a large distance during catalysis but has no direct role in domain closure
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
infrared studies reveal unique vibrations associated with the phosphoglycerate kinase-ATP-3-phosphoglycerate ternary complex
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
molecular modeling study show that the beta-phosphates of D- and L-ADP have different orientations when bound to the active site of human PGK. The difference is unexpected because L-ADP is almost as catalytically competent as D-ADP
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
Pyrococcus woesei Vul 4
P61884
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
Lactobacillus delbrueckii subsp. lactis NCC88
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
Pyrococcus woesei DSM 3773
P61884
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
Q7SIB7
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
P00560
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
P20971
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
trout
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
Vombatus sp.
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
P61884, -
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
P46273
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
P00558
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
P00558
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-, Q9RBS3
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-, P50311
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
specific for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
high specificity for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
high specificity for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
the isolated N-terminal domain is soluble, monomeric, compactly folded, native-like in structure, and capable of binding 3-phospho-D-glycerate with high affinity
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
absolute specificity for 3-phospho-D-glycerate
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
absolute specificity for 3-phospho-D-glycerate
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
absolute specificity for 3-phospho-D-glycerate
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
-
simultaneous binding of both substrates is essential for domain closure
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
Thermoanaerobacter sp. Rt8.G4
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
Mus musculus DBA/2J
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
Pyrococcus woesei Vul 4
P61884
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
Rhodopseudomonas palustris JCM2524
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
Geobacillus stearothermophilus NCA 1503
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
Geobacillus stearothermophilus NCA 1503
-
absolute specificity for 3-phospho-D-glycerate
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
Lactobacillus delbrueckii subsp. lactis NCC88
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
P46273
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
show the reaction diagram
Pyrococcus woesei DSM 3773
P61884
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
show the reaction diagram
Entamoeba histolytica, Entamoeba histolytica HM1:IMSS
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
P61884, -
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-, P20971
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
the enzyme is required for ATP generation in the terminal stage of the glycolytic pathway. Important role of PGK in synaptic transmission. Disrupted phosphoglycerate kinase in nubian mutants causes altered ATP generation in nubian animals. Brain extracts show a threefold reduction in resting ATP levels compared with controls. Disruption of ATP generation in nubian animals is accompanied by temperature-dependent defects in neuronal activity with initial seizure activity, followed by an activity-dependent loss of synaptic transmission. Nubian mutants also diaplay structural defects at the synapse, with larger varicosity size but normal varicosity number
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
the enzyme plays an essential role in energy production for movement via muscle contraction in Clonorchis sinensis
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
P20971
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
Pyrococcus woesei Vul 4
P61884
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
P50317
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
Pyrococcus woesei DSM 3773
P61884
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate.
show the reaction diagram
P61884, -
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate.
show the reaction diagram
Pyrococcus woesei Vul 4, Pyrococcus woesei DSM 3773
P61884
-
-
-
?
beta-L(-)-dioxolanecytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L(-)-dioxolanecytidine 5'-diphosphate + 1,3-diphosphoglycerate
show the reaction diagram
-
isozyme PGK1, 3fold higher activity compared to 2'-deoxycytidine
-
-
?
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
-
isozyme PGK1, 4fold higher activity compared to 2'-deoxycytidine
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
show the reaction diagram
-
no activity
-
-
-
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
show the reaction diagram
-
no activity
-
-
-
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
show the reaction diagram
-
no activity
-
-
-
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
show the reaction diagram
-
no activity
-
-
-
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
show the reaction diagram
-
no activity
-
-
-
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
show the reaction diagram
trout
-
no activity
-
-
-
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
show the reaction diagram
Spirulina geitleri
-
no activity
-
-
-
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
show the reaction diagram
-
low activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
show the reaction diagram
-
low activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
show the reaction diagram
Mus musculus, Mus musculus DBA/2J
-
1% of the activity with ATP
-
-
?
D-ADP + 1,3-bisphosphoglycerate
?
show the reaction diagram
-
-
-
-
?
D-ATP + 1,3-bisphospho-D-glycerate
?
show the reaction diagram
-
-
-
-
?
D-ATP + 3-phospho-D-glycerate
D-ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
D-CDP + 1,3-bisphospho-D-glycerate
?
show the reaction diagram
-
-
-
-
?
D-CTP + 3-phospho-D-glycerate
D-CDP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
D-GTP + 3-phospho-D-glycerate
D-GDP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
show the reaction diagram
Spirulina geitleri
-
low activity
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
show the reaction diagram
-
27% of the activity with ATP
-
-
-
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
show the reaction diagram
-
isozymes PGK2A, PGK2B, and PGK1 show low activity, isozyme PGK2C shows 119% of the activity with ATP
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
show the reaction diagram
Mus musculus DBA/2J
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
show the reaction diagram
Spirulina geitleri
-
no activity
-
-
-
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
show the reaction diagram
-
isozyme PGK2C with lower activity, all other isozymes show slightly lower activity compared to ATP
-
-
?
dITP + 3-phospho-D-glycerate
dIDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
dITP + 3-phospho-D-glycerate
dIDP + 1,3-diphosphoglycerate
show the reaction diagram
Spirulina geitleri
-
no activity
-
-
-
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
-
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
trout
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
Esox sp., Testudinidae
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
no activity
-
-
-
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
Spirulina geitleri
-
very low activity
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
36% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
low activity
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
low activity
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
60% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
60% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
-
27% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
Mus musculus DBA/2J
-
60% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
Geobacillus stearothermophilus NCA 1503
-
27% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
show the reaction diagram
Entamoeba histolytica HM1:IMSS
-
-
-
-
-
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
trout
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
Esox sp., Testudinidae
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
no activity
-
-
-
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
Spirulina geitleri
-
very low activity
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
low activity
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
42% of the activity with ATP
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
45% of the activity with ATP
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
-
64% of the activity with ATP
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
show the reaction diagram
Geobacillus stearothermophilus NCA 1503
-
42% of the activity with ATP
-
-
?
L-2'-dATP + 3-phospho-D-glycerate
L-2'-dADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
L-2'-dGTP + 3-phospho-D-glycerate
L-2'-dGDP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
L-2'-dTTP + 3-phospho-D-glycerate
L-2'-dTDP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
L-ADP + 1,3-bisphosphoglycerate
?
show the reaction diagram
-
with L-ADP, the transient burst phase of ATP is more clear-cut than with D-ADP, suggesting that the product release steps are slower with L-ADP than with D-ADP. This is in accordance with the lower kcat measured with L-ADP compared to D-ADP
-
-
?
L-ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
L-MgADP is almost as a good substrate for hPGK as the natural D-MgADP
-
-
?
L-ATP + 1,3-bisphospho-D-glycerate
?
show the reaction diagram
-
-
-
-
?
L-ATP + 3-phospho-D-glycerate
L-ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
L-CDP + 1,3-bisphospho-D-glycerate
?
show the reaction diagram
-
-
-
-
?
L-CTP + 3-phospho-D-glycerate
L-CDP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
L-GTP + 3-phospho-D-glycerate
L-GDP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
show the reaction diagram
-
-
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
show the reaction diagram
-
no activity
-
-
-
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
show the reaction diagram
-
no activity
-
-
-
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
show the reaction diagram
-
low activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
show the reaction diagram
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
show the reaction diagram
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
show the reaction diagram
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
show the reaction diagram
Mus musculus, Mus musculus DBA/2J
-
1% of the activity with ATP
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
L-UTP + 3-phospho-D-glycerate
L-UDP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
no activity with dCTP, dUTP, dTTP
-
-
-
additional information
?
-
-
2',3'-dideoxycytidine is a very poor substrate
-
-
-
additional information
?
-
-
no activity with pyrimidine nucleotides
-
-
-
additional information
?
-
-
the only analog of 3-phospho-D-glycerate that can replace the substrate is an artificial 3-phospho-D-glycerate in which the phosphate group-O-PO3H2 is replaced by the phosphomethyl group-CH2-PO3H2, i.e. 2-hydroxy-4-phospho-DL-butyric acid
-
-
-
additional information
?
-
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
-
additional information
?
-
-
nucleotide substrate specificity
-
-
-
additional information
?
-
-
no activity with dTTP
-
-
-
additional information
?
-
-
enzyme is regulated by multivalent anions, 2-domain hinge-binding enzyme
-
-
-
additional information
?
-
-
also catalyzes ADP-ATP exchange reaction
-
-
-
additional information
?
-
-
phylogenetic tree
-
-
-
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
-
-
-
additional information
?
-
P00558
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
-
-
-
additional information
?
-
-
enzyme acts as a disulfide reductase, e.g. plasmin reductase, in tumour angiogenesis
-
-
-
additional information
?
-
-
induction of multidrug resistance in cancer cell lines by overexpression of isozyme PGK1
-
-
-
additional information
?
-
-
the enzyme may be involved in the cellular activation of several antiviral nucleoside analogs including dideoxyinosine, acyclovir, L-2'-deoxycytosine and L-2'-deoxythymidine
-
-
-
additional information
?
-
-
PGKC 3'-UTR exerts strong regulatory effects in Trypanosoma brucei. The regulatory effects are exerted at the levels of both mRNA stability and translation
-
-
-
additional information
?
-
-
phosphoglycerate kinase 1 is induced by hydrogen peroxide in a dose-dependent manner, while its expression is suppressed by a co-treatment with delphinidin (antioxidant). Several antioxidants, including alpha-tocopherol, butylated hydroxytoluene, and Trolox, also inhibit the PGK1 induction caused by hydrogen peroxide
-
-
-
additional information
?
-
-
single-nucleotide polymorphisms is an adaptation to the external anoxic environment
-
-
-
additional information
?
-
-
Pgk1 plays some functional roles in the development of tooth germ and other embryonic organs by forming protein complex with glyceraldehyde-3-phosphate dehydrogenase
-
-
-
additional information
?
-
-
Mg-ADP or Mg-beta,gamma-imido-adenosine 5'-triphosphate substitute the substrate Mg-ATP in the ternary complexes, they cannot react with 3-phospho-D-glyceroyl phosphate. Domain closure and substrate antagonism are closely related phenomena for PGK. Conformational rearrangements in the hinge generated by binding of both substrates provide the main driving force for domain closure overcoming the slightly unfavourable contact interactions between the domains
-
-
-
additional information
?
-
-
phosphorylates beta-L-dioxolane-cytidine, a novel L-configuration deoxycytidine analogue, under clinical trials for treating cancer
-
-
-
additional information
?
-
-
pressure-jump unfolding kinetics of phosphoglycerate kinase at pressures between 50 and 150 MPa and time dependence of the conformational state of the protein followed by tryptophan fluorescence measurements from 30 s to 2 h: the activation volumes of the unfolding reaction are negative for the folded-intermediate, intermediate-unfolded, and unfolded-intermediate transitions
-
-
-
additional information
?
-
-
the oxidized PGK contains chloroplast-type thioredoxin (Trx)-accessible disulfide bond
-
-
?
additional information
?
-
-
molecular dynamics simulations are carried out with four different nucleotides (D-/L-ADP and D-/L-CDP) in complex with hPGK and 1,3-bisphospho-D-glycerate (bPG). The binding affinities of CDPs (both enantiomers) for hPGK are found very weak while D- and L-ADP are better substrates. The binding affinity of the bPG substrate is found to be lower in presence of D-ADP than L-ADP which indicates a potential antagonistic effect on one substrate to the other
-
-
-
additional information
?
-
Geobacillus stearothermophilus NCA 1503
-
no activity with pyrimidine nucleotides
-
-
-
additional information
?
-
Lactobacillus delbrueckii subsp. lactis NCC88
-
phylogenetic tree
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
ADP + 3-phospho-D-glyceroyl 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
-
-
-
r
ADP + 3-phospho-D-glyceroyl 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
-
-
-
r
ADP + 3-phospho-D-glyceroyl 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
-, P20971
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
P61884, -
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
key enzyme in glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
energy charge is the most important factor in regulating the 2 forms of PGK
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
-
key enzyme of anaerobic glycolysis in Plasmodium falciparum
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
Pyrococcus woesei Vul 4
P61884
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
Lactobacillus delbrueckii subsp. lactis NCC88
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
show the reaction diagram
Pyrococcus woesei DSM 3773
P61884
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
P61884, -
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-, P20971
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
the enzyme is required for ATP generation in the terminal stage of the glycolytic pathway. Important role of PGK in synaptic transmission. Disrupted phosphoglycerate kinase in nubian mutants causes altered ATP generation in nubian animals. Brain extracts show a threefold reduction in resting ATP levels compared with controls. Disruption of ATP generation in nubian animals is accompanied by temperature-dependent defects in neuronal activity with initial seizure activity, followed by an activity-dependent loss of synaptic transmission. Nubian mutants also diaplay structural defects at the synapse, with larger varicosity size but normal varicosity number
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
-
the enzyme plays an essential role in energy production for movement via muscle contraction in Clonorchis sinensis
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
P20971
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
show the reaction diagram
Pyrococcus woesei Vul 4, Pyrococcus woesei DSM 3773
P61884
-
-
-
?
additional information
?
-
-
phylogenetic tree
-
-
-
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
-
-
-
additional information
?
-
P00558
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
-
-
-
additional information
?
-
-
enzyme acts as a disulfide reductase, e.g. plasmin reductase, in tumour angiogenesis
-
-
-
additional information
?
-
-
induction of multidrug resistance in cancer cell lines by overexpression of isozyme PGK1
-
-
-
additional information
?
-
-
the enzyme may be involved in the cellular activation of several antiviral nucleoside analogs including dideoxyinosine, acyclovir, L-2'-deoxycytosine and L-2'-deoxythymidine
-
-
-
additional information
?
-
-
PGKC 3'-UTR exerts strong regulatory effects in Trypanosoma brucei. The regulatory effects are exerted at the levels of both mRNA stability and translation
-
-
-
additional information
?
-
-
phosphoglycerate kinase 1 is induced by hydrogen peroxide in a dose-dependent manner, while its expression is suppressed by a co-treatment with delphinidin (antioxidant). Several antioxidants, including alpha-tocopherol, butylated hydroxytoluene, and Trolox, also inhibit the PGK1 induction caused by hydrogen peroxide
-
-
-
additional information
?
-
-
single-nucleotide polymorphisms is an adaptation to the external anoxic environment
-
-
-
additional information
?
-
-
the oxidized PGK contains chloroplast-type thioredoxin (Trx)-accessible disulfide bond
-
-
?
additional information
?
-
Lactobacillus delbrueckii subsp. lactis NCC88
-
phylogenetic tree
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ADP
Esox sp., Frog, Pisum sativum, Testudinidae
-
-
ADP
-
true substrate is the magnesium complexes of ADP
ADP
trout
-
-
ADP
Arthrospira platensis, Spirulina geitleri
-
-
ADP
Vombatus sp.
-
-
ADP
Abramis brama, Bufo vulgaris, Chrysophrys guttulatus, Columba sp.
-
-
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor
ATP
Esox sp., Frog
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor
ATP
trout
-
required as phosphate donor
ATP
Arthrospira platensis, Spirulina geitleri
-
required as phosphate donor
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
Vombatus sp.
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
Bufo vulgaris, Chrysophrys guttulatus, Columba sp.
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
Na2ATP2-; required as phosphate donor
ATP
P20971
required as phosphate donor
ATP
P61884
required as phosphate donor
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
P46273
required as phosphate donor
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor; true substrate is the magnesium complexes of ATP
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor
ATP
P50311
required as phosphate donor
ATP
-
required as phosphate donor
ATP
Q9RBS3
required as phosphate donor
ATP
-
required as phosphate donor
ATP
-
required as phosphate donor
ATP
-
exhibits 2.5times higher activity with ATP compared with GTP
dATP
Spirulina geitleri
-
-
GTP
trout
-
-
GTP
Spinacia oleracea, Spirulina geitleri
-
-
ITP
trout
-
-
ITP
Spinacia oleracea, Spirulina geitleri
-
-
UTP
trout
-
-
additional information
-
in the presence of either beta,gamma-imido-adenosine 5'-triphosphate or ADP binding of 3-phospho-D-glycerate is weakened and the contribution of the entropy-factor to its binding is increased relative to the enthalpy factor
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
CaATP2- is the true substrate; can partially replace Mg2+ in activation
Ca2+
-
15% of the activity with Mg2+; can partially replace Mg2+ in activation
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
34% of the activity with Mg2+; can partially replace Mg2+ in activation
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
30% of the activity with Mg2+; can partially replace Mg2+ in activation
Ca2+
-
divalent metal ion required: Ca2+, Mg2+ or Mn2+. Mg2+ is the preferred cation
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation; CdATP2- is the true substrate
Cd2+
-
can partially replace Mg2+ in activation
Cd2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation; CoATP2- is the true substrate
Co2+
-
58% of the activity with Mg2+; can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
77% of the activity with Mg2+; can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Divalent cation
-
descending order of activation potential Mg2+,Mn2+, Zn2+, Co2+, Cd2+, Ca2+, isozyme PGK1 is more activated than PGK2
Divalent cation
-
-
Divalent cation
-
Mg2+ or Mn2+
Divalent cation
-
Mg2+ or Mn2+
Divalent cation
-
-
Divalent cation
-
Mg2+ or Mn2+
Divalent cation
-
requires Mg2+ or Ca2+
Divalent cation
-
Mg2+ or Mn2+
K+
-, P20971
monovalent cations are essential for the activity of the archaeal enzyme with K+ being significantly more efficient than Na+; monovalent cations are essential for the activity, with K+ being significantly more efficient than Na+.
K+
P61884
monovalent cations are essential for the activity of the archaeal enzyme with K+ being significantly more efficient than Na+. Non-cooperative K+ binding with an apparent Kd (K+) of 88 mM; monovalent cations are essential for the activity, with K+ being significantly more efficient than Na+. Non-cooperative K+ binding with an apparent Kd of 88 mM
KCl
-
maximal activation at 100 mM
KH2PO4
-
inhibition at high concentration, acceleration of activity at low concentrations
KH2PO4
-
maximal activation at 25-50 mM
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
-
above 10 mM inhibition of isozyme PGK1, not PGK2; Mg2+ most efficient activator; required
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
-
required; true substrate is the magnesium complexes of ATP
Mg2+
-
required; true substrate is the magnesium complexes of ATP
Mg2+
-
required; true substrate is the magnesium complexes of ATP
Mg2+
-
-
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
Trichosurus vulpecula, Vombatus sp.
-
true substrate is the magnesium complexes of ATP
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
-
required
Mg2+
-
5 mM Mg2+ or 10 mM Mn2+ required; required
Mg2+
-
optimum concentration: 8-16 mM; required
Mg2+
-
true substrate is the magnesium complexes of ATP
Mg2+
-
5 mM Mg2+ or 10 mM Mn2+ required
Mg2+
-
required
Mg2+
-, P20971
; Km: 1.1 mM
Mg2+
P61884
-
Mg2+
P46273
-
Mg2+
-
required
Mg2+
-
0.8 m Mg2+ and 0.5 mM Mn2+ are optimal
Mg2+
-
MgATP2- is the substrate. Mg2+ is liganded to both beta- and gamma-phosphates of ATP
Mg2+
-
divalent metal ion required: Ca2+, Mg2+ or Mn2+. Mg2+ is the preferred cation. Optimal concentration of Mg2+ is 5-15 mM
Mg2+
Q08GC7
-
Mn2+
-
can partially replace Mg2+ in activation; more effective for isoenzyme PGK1 than for PGK2
Mn2+
-
Mn2+ or Mg2+ required
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
67% of the activity with Mg2+; can partially replace Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
-
5 mM Mg2+ or 10 mM Mn2+ required; Mn2+ or Mg2+ required
Mn2+
-
0.8 mM Mg2+ and 0.5 mM Mn2+ are optimal
Na+
-, P20971
monovalent cations are essential for the activity of the archaeal enzyme with K+ being significantly more efficient than Na+; monovalent cations are essential for the activity, with K+ being significantly more efficient than Na+
Na+
P61884
monovalent cations are essential for the activity of the archaeal enzyme with K+ being significantly more efficient than Na+; monovalent cations are essential for the activity, with K+ being significantly more efficient than Na+
NaCl
-
inhibition at high concentration, acceleration of activity at low concentrations
NaCl
-
maximal activation at 100 mM
NaH2PO4
-
maximal activation at 25-50 mM
NaNO2
-
inhibition at high concentration, acceleration of activity at low concentrations
Ni2+
-
can partially replace Mg2+ in activation; NiATP2- is the true substrate; poor activator
Ni2+
-
no activation
Ni2+
-
can partially replace Mg2+ in activation
Ni2+
-
12% of the activity with Mg2+; can partially replace Mg2+ in activation
Zn2+
-
can partially replace Mg2+ in activation; more effective for isoenzyme PGK1 than for PGK2
Zn2+
-
can partially replace Mg2+ in activation; ZnATP2- is the true substrate, free metal ions inhibit
Zn2+
-
no activation
Zn2+
-
ZnATP2- is the true substrate, free metal ions inhibit
Zn2+
-
no activation
Mn2+
-
divalent metal ion required: Ca2+, Mg2+ or Mn2+. Mg2+ is the preferred cation
additional information
-
no activation by Be2+; no activation by Fe2+
additional information
-
no activation by Ba2+
additional information
-
no activation by: Sr2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
inhibition at high concentration, activation at low concentrations
(NH4)2SO4
-
strong
1,3-bis(difluoro)-1,3-diphospho-2-dihydroxypropane
-
phosphonate analogues of 1,3-diphosphoglycerate
-
1,4-bis(difluoro)-1,4-diphospho-diethylether
-
phosphonate analogues of 1,3-diphosphoglycerate
1,4-Bisphosphonobutane
-
-
1,5-Bisphosphonopentane
-
-
1,5-Bisphosphonopentane
-
competitive
1-beta-D-arabinofuranosylcytosine
-
-
1-beta-D-arabinofuranosylcytosine 5'-diphosphate
-
-
2',2'-difluorodeoxycytidine
-
-
2',2'-difluorodeoxycytidine 5'-diphosphate
-
i.e. gemcitabine
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine
-
-
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine 5'-diphosphate
-
-
2'-fluoro-5-methyl-beta-L-arabinofuranosyluracil
-
-
2'-fluoro-5-methyl-beta-L-arabinofuranosyluracil 5'-diphosphate
-
-
2,3-diphosphoglycerate
-
competitive to 3-phospho-D-glycerate and MgATP2-
2,3-diphosphoglycerate
-
-
2,3-diphosphoglycerate
-
noncompetitive with respect to 1,3-diphosphoglycerate
2,3-diphosphoglycerate
-
-
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
-
-
2-Phosphoglycolate
-
competitive
4-Phosphonobutyronitrile
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
reversible
5,5'-dithiobis(2-nitrobenzoic acid)
-
rabbit muscle enzyme
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
complete loss of activity
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
actinomycin D
-
blocks transcription
adenosine
-
-
ADP
-
noncompetitive with respect to ATP and 3-phospho-D-glycerate
ADP
-
noncompetitive to ATP and competitive to 3-phospho-D-glycerate
ADP
-
inhibitory in forward reaction
ADP
-
0.1 mM, 63.1% activity; 0.1 mM, 85% activity; 0.1 mM, 86% activity; 1 mM, 31% activity; 1 mM, 32% activity
ADP3-
-
competitive to 3-phospho-D-glycerate
AMP
-
above 0.5 mM noncompetitive and below 0.5 mM competitive to 3-phospho-D-glycerate, competitive to MgATP2-
AMP
-
noncompetitive with respect to 1,3-diphosphoglycerate, ADP and Mg2+, inhibition kinetics
AMP
-
0.625 mM, 95% activity; 0.625 mM, 98% activity; 10 mM, 40% activity; 10 mM, 44% activity; 10 mM, 50% activity
AMP2-
-
competitive to MgATP2-, noncompetitive to 3-phospho-D-glycerate
ATP4-
-
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-
-
inhibition at high concentration, acceleration of activity at low concentrations
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
beta-L-2',3'-dideoxy-3'-thiacytidine
-
-
beta-L-2',3'-dideoxy-3'-thiacytidine diphosphate
-
-
Ca2+
-
inhibition above 1 mM
Ca2+
-
partial inhibition in presence of Mg2+
citrate
-
40% inhibition at 50 mM
Co2+
-
77% of the activity with Mg2+
Co2+
-
inhibits at high concentrations
CTP
-
competitive to ATP
D-2',3'-dideoxycytidine
-
-
D-MgADP-
-
competitive inhibitor with respect to MgATP
diphosphate
-
-
Glycerol 2-phosphate
-
competitive
Glycerol 2-phosphate
-
10 mM, 97% activity
glycerol 3-phosphate
-
competitive
glycerol 3-phosphate
-
10 mM, 92% activity; 10 mM, 95% activity; 10 mM, 97% activity
GTP
-
competitive to ATP
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
Heavy metal ions
-
rabbit muscle enzyme
-
Hexametaphosphate
-
competitive against 3-phospho-D-glycerate and noncompetitive against MgATP2-
hydrogen peroxide
-
-
hydroxyethylidene bisphosphonic acid
-
competitive against MgATP2- and 3-phospho-D-glycerate
Ib1
-
isozymes are differntly sensitive
-
iodoacetamide
-
irreversible
iodoacetamide
-
nucleotide ligands protect, e.g. MgATP2-, MgADP-, Mg-beta,gamma-methylene-adenosine-5'-triphosphate, Mg-beta,gamma-imido-adenosine-5'-triphosphate
iodoacetate
-
-
ITP
-
weak competitive inhibitor
K+
-, P20971
activates
K+
P61884
activates
KH2PO4
-
inhibition at high concentration, activation at low concentrations
KH2PO4
-
above 50 mM
L-2',3'-dideoxycytidine
-
-
-
L-MgADP-
-
competitive inhibitor with respect to MgATP
Mg-beta,gamma-imido-adenosine-5'-triphosphate
-
-
Mg-beta,gamma-methylene-adenosine-5'-triphosphate
-
-
Mg2+
-
inhibition above 50 mM
MgADP-
-
competitive to 3-phospho-D-glycerate
N-ethylmaleimide
-
irreversible
N-ethylmaleimide
-
-
NaCl
-
inhibition at high concentration, acceleration of activity at low concentrations
NaH2PO4
-
above 50 mM
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 diphosphates
-
purine nucleotide diphosphates
nucleoside monophosphates
-
purine nucleotide monophosphates
p-chloromercuribenzoate
-
reversible
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
rabbit muscle enzyme
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
strong
phosphate
-
phosphate buffer
salicylate
-
i.e. 2-hydroxybenzoate
shRNA
-
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
-
sinefungin
-
blocks splicing
SO42-
-
activation with yeast PGK, inhibition with trypanosomal PGK
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
SO42-
-
above 50 mM
Sodium citrate
-
inhibition at high concentration, activation at low concentrations
sodium nitroprusside
-
-
Sodium selenate
-
inhibition at high concentration, activation at low concentrations
Sodium succinate
-
inhibition at high concentration, activation at low concentrations
suramin
-
competitive against MgATP2- and 3-phospho-D-glycerate
suramin
-
isozymes are differently sensitive
suramin
-
IC50: 0.007 mM
UDP
-
10 mM, 94.3% activity; 10 mM, 97% activity
Zn2+
-
ZnATP2- is an alternative substrate to MgATP2-, free metal ions strongly inhibit
Mn2+
-
inhibition above 50 mM
additional information
-
yeast enzyme is insensitive to thiol reagents
-
additional information
-
no inhibition by Hg2+
-
additional information
-
-
-
additional information
-
inhibitory effect of phosphonate analogues of 1,3-diphosphoglycerate, overview
-
additional information
-
double-inhibition studies, kinetics, modeling of inhibitor binding, e.g. phosphate; enzyme is regulated by multivalent anions, overview
-
additional information
-
no effect by glucose 6-phosphate, fructose 6-phosphate, fructose 1,6-phosphate, pyruvate, phosphoenolpyruvate and lactate
-
additional information
-
aromatic bisphosphonate inhibitors
-
additional information
-
aliphatic bisphosphonate inhibitors
-
additional information
P07378
aromatic and aliphatic bisphosphonates
-
additional information
-
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
-
additional information
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
-
inhibition at high concentration, acceleration of activity at low concentrations
1,3-diphosphoglycerate
-
substrate activation
acetate
-
as Na or K salt continues to activate at concentrations above 200 mM
ATP4-
-
binds to the free enzyme as an inhibitor, when binding to the enzyme-MgATP2-(3-phospho-D-glycerate)complex, ATP4- acts as an activator; inhibition at high concentration, acceleration of activity at low concentrations
SO42-
-
activation with yeast PGK, inhibition with Trypanosomal PGK
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
ATP4-
-
inhibition at high concentration, acceleration of activity at low concentrations
additional information
-
enzyme is regulated by multivalent anions, overview
-
additional information
-
no effect by glucose 6-phosphate, fructose 6-phosphate, fructose 1,6-phosphate, pyruvate, phosphoenolpyruvate and lactate
-
additional information
-
in bloodstream forms, after XRNA depletion, abundance of PGKB mRNA increases to about one-third of the PGKC mRNA abundance, with a corresponding decrease in the apparent degradation rate. The degradation of PGKC mRNA is not affected. In procyclic forms, PGKB mRNA is unaffected by XRNA depletion, PGKC mRNA is undetectable, but after XRNA depletion, PGKC mRNA is detectable
-
additional information
-
hypoxic treatment induces the protein expression of PGK 3fold, induction of HIF-1alpha by addition of 0.5 mM dimethyloxallyl glycine increases PGK expression under normoxic conditions
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0022
-
3-phospho-D-glycerate
-
pH 7.0
0.028
-
3-phospho-D-glycerate
-
isozyme PGK2C
0.05
-
3-phospho-D-glycerate
-
wild-type enzyme
0.062
-
3-phospho-D-glycerate
-
mutant enzyme S398A
0.1
-
3-phospho-D-glycerate
-
wild-type enzyme
0.1
-
3-phospho-D-glycerate
-
wild-type, pH and temperature not specified in the publication
0.11
-
3-phospho-D-glycerate
-
mutant enzyme T393del
0.12
-
3-phospho-D-glycerate
-
mutant D374A, pH and temperature not specified in the publication
0.15
-
3-phospho-D-glycerate
-
isozyme PGK2B, ADP, isoenzyme PGK2A
0.18
-
3-phospho-D-glycerate
-
wild-type, 30C, pH not specified in the publication
0.2
-
3-phospho-D-glycerate
-
isoenzyme PGK2A
0.2
-
3-phospho-D-glycerate
-
pH 6.9, 25C
0.24
-
3-phospho-D-glycerate
-
mutant D218A/D374A, pH and temperature not specified in the publication
0.27
-
3-phospho-D-glycerate
-
mutant D218A, pH and temperature not specified in the publication
0.31
-
3-phospho-D-glycerate
-
mutant enzyme E343A
0.32
-
3-phospho-D-glycerate
-
mutant enzyme S392A
0.41
-
3-phospho-D-glycerate
-
mutant enzyme K125A
0.46
-
3-phospho-D-glycerate
-
isozyme PGK2, pH 7.3-7.8
0.48
-
3-phospho-D-glycerate
-
native wild-type enzyme, pH 7.5, 25C
0.5
-
3-phospho-D-glycerate
-
-
0.52
-
3-phospho-D-glycerate
-
-
0.52
-
3-phospho-D-glycerate
-
-
0.53
-
3-phospho-D-glycerate
-
recombinant wild-type enzyme, pH 7.5, 25C
0.53
-
3-phospho-D-glycerate
-
mutant enzyme E192A
0.54
-
3-phospho-D-glycerate
-
mutant enzyme N336A
0.54
-
3-phospho-D-glycerate
-
70C, pH 6.5
0.57
-
3-phospho-D-glycerate
-
-
0.589
-
3-phospho-D-glycerate
-
pH 8.2, 25C
0.59
-
3-phospho-D-glycerate
-
isozyme PGK1, pH 7.3
0.59
-
3-phospho-D-glycerate
-
pH 7.5, 25C
0.6
0.7
3-phospho-D-glycerate
-
pH 7.5, 30C
0.601
-
3-phospho-D-glycerate
-
pH 7, 25C
0.63
-
3-phospho-D-glycerate
-
mutant enzyme T375A
0.683
-
3-phospho-D-glycerate
-
pH 8.2, 25C
0.69
-
3-phospho-D-glycerate
-
mutant enzyme F196A
0.707
-
3-phospho-D-glycerate
-
pH 7, 25C
0.711
-
3-phospho-D-glycerate
-
pH 7.6, 25C
0.719
-
3-phospho-D-glycerate
-
pH 7.6, 25C
0.72
-
3-phospho-D-glycerate
-
-
0.75
-
3-phospho-D-glycerate
-, P20971
native enzyme, 70C; pH 7.5, 70C, native enzyme; pH 7.5, 70C, recombinant enzyme
0.77
-
3-phospho-D-glycerate
-, P20971
pH 7.5, 70C, enzyme expressed in Escherichia coli; pH 7.5, 70C, recombinant enzyme; recombinant enzyme, 70C
0.77
-
3-phospho-D-glycerate
-
wild-type enzyme, pH 7.5, 25C
0.8
-
3-phospho-D-glycerate
-
-
0.81
-
3-phospho-D-glycerate
-
-
0.89
-
3-phospho-D-glycerate
-
recombinant His-tagged enzyme, pH 7.5, 25C
0.9
-
3-phospho-D-glycerate
-
-
0.95
-
3-phospho-D-glycerate
-
mutant enzyme F165A
0.99
-
3-phospho-D-glycerate
-
mutant enzyme T393A
1.02
-
3-phospho-D-glycerate
-
-
1.1
-
3-phospho-D-glycerate
-
at 1.5-13 mM 3-phospho-D-glycerate concentration
1.1
-
3-phospho-D-glycerate
-
at 0.1 M
1.1
-
3-phospho-D-glycerate
P61884
native enzyme, 70C
1.11
-
3-phospho-D-glycerate
P61884
pH 7.5, 70C, recombinant enzyme
1.25
-
3-phospho-D-glycerate
-
native cytosolic isozyme, pH 7.6, 25C
1.26
-
3-phospho-D-glycerate
-
-
1.28
-
3-phospho-D-glycerate
-
at 1.5-13 mM 3-phospho-D-glycerate concentration
1.39
-
3-phospho-D-glycerate
-
-
1.4
-
3-phospho-D-glycerate
-
heart enzyme, pH 7.4, 25C
1.4
-
3-phospho-D-glycerate
P61884
pH 7.5, 70C, enzyme expressed in Escherichia coli; pH 7.5, 70C, recombinant enzyme; recombinant enzyme, 70C
1.4
-
3-phospho-D-glycerate
-
-
1.41
-
3-phospho-D-glycerate
-
-
1.5
-
3-phospho-D-glycerate
-
pH 6.5, 25C
1.5
-
3-phospho-D-glycerate
Spirulina geitleri
-
at 1.5-13 mM 3-phospho-D-glycerate concentration
1.55
-
3-phospho-D-glycerate
-
native glycosomal isozyme, pH 7.6, 25C
1.635
-
3-phospho-D-glycerate
-
pH 8.2, 25C
1.65
-
3-phospho-D-glycerate
-
liver enzyme, pH 7.4, 25C
1.66
-
3-phospho-D-glycerate
-
skeletal muscle enzyme, pH 7.4, 25C
1.66
-
3-phospho-D-glycerate
-
mutant enzyme S392A/T393A
1.72
-
3-phospho-D-glycerate
-
mutant enzyme k219A
1.787
-
3-phospho-D-glycerate
-
pH 7.6, 25C
1.79
-
3-phospho-D-glycerate
-
pH 7.5, 22C
1.948
-
3-phospho-D-glycerate
-
pH 7, 25C
2
-
3-phospho-D-glycerate
-
recombinant glycosomal isozyme and native cytosoli isozyme, pH 7.6, 25C
2.2
-
3-phospho-D-glycerate
-
pH 7.6, 25C
2.4
-
3-phospho-D-glycerate
-
recombinant isozyme 56PGK
2.5
-
3-phospho-D-glycerate
-
mutant P204H, pH 7.5, 25C
2.6
-
3-phospho-D-glycerate
-
pH 6.8, 45C
4.5
-
3-phospho-D-glycerate
-
mutant enzyme R38A
4.8
-
3-phospho-D-glycerate
P61884
pH 7.5, 70C, native enzyme
7.6
-
3-phospho-D-glycerate
-
pH 7.3
11.9
-
3-phospho-D-glycerate
-
recombinant truncated glycosomal isozyme, pH 7.6, 25C
0.0005
-
3-phospho-D-glyceroyl phosphate
-
wild-type enzyme
0.0013
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme E343A
0.0022
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme N336A
0.003
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme T375A
0.0038
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme K125A
0.005
-
3-phospho-D-glyceroyl phosphate
-
wild-type enzyme
0.0077
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme k219A
0.0091
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme E192A
0.01
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme T393A
0.017
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme F165A
0.29
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme R38A
5.6
-
3-phospho-D-glyceroyl phosphate
-
70C, pH 6.5
0.039
-
ADP
-
isozyme PGK2C
0.077
-
ADP
-
wild-type, at 4C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
0.085
-
ADP
-
70C, pH 6.5
0.09
-
ADP
-
mutant enzyme E192A
0.1
-
ADP
-
enzymatic activity of immobilized PGK on glass
0.1
-
ADP
-
mutant enzyme R38A
0.1
-
ADP
-
mutant enzyme T393A
0.12
-
ADP
-
wild-type enzyme
0.12
-
ADP
-
mutant enzyme F165A; wild-type enzyme
0.126
-
ADP
-
mutant K215A, at 4C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
0.15
-
ADP
-
mutant enzyme K125A
0.18
-
ADP
-
enzymatic activity in bulk condition
0.19
-
ADP
-
isozyme PGK2B
0.23
-
ADP
-
isozyme PGK1
0.28
-
ADP
-
recombinant purified mutant Y239F/E309M, at 37C, pH 7.0
0.42
-
ADP
-
mutant enzyme N336A
0.5
-
ADP
-
wild-type, in cytosolic-enriched cellular extracts, at 37C, pH 7.0
0.91
-
ADP
-
mutant enzyme E343A
1.12
-
ADP
-
mutant enzyme T375A
1.42
-
ADP
-
mutant enzyme k219A
1.606
-
ADP
-
recombinant purified mutant E309M, at 37C, pH 7.0
1.696
-
ADP
-
recombinant purified mutant V311L, at 37C, pH 7.0
1.723
-
ADP
-
recombinant purified mutant E309Q, at 37C, pH 7.0
2.016
-
ADP
-
recombinant purified wild-type, at 37C, pH 7.0
2.693
-
ADP
-
recombinant purified mutant Y239F, at 37C, pH 7.0
7.4
-
ADP
-
wild-type, in cytosolic-enriched cellular extracts, at 37C, pH 7.0
0.017
-
ATP
-
wild-type, at 4C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
0.03
-
ATP
-
mutant enzyme S398A
0.038
-
ATP
-
isoenzyme PGK2C
0.078
-
ATP
-
mutant enzyme S392A
0.11
-
ATP
-
pH 6.9, 25C
0.11
-
ATP
-
wild-type enzyme
0.11
-
ATP
-
mutant D218A, pH and temperature not specified in the publication; wild-type, pH and temperature not specified in the publication
0.13
-
ATP
-
mutant enzyme T393del
0.18
-
ATP
-
mutant D374A, pH and temperature not specified in the publication
0.19
-
ATP
-
wild-type, 30C, pH not specified in the publication
0.2
-
ATP
-
mutant D218A/D374A, pH and temperature not specified in the publication
0.21
-
ATP
-
recombinant cytosolic isozyme, pH 7.6, 25C
0.21
-
ATP
-
recombinant wild-type enzyme, pH 7.5, 25C
0.215
-
ATP
-
pH 8.2, 25C
0.22
-
ATP
-
isoenzyme PGK1
0.227
-
ATP
-
pH 7.6, 25C
0.24
-
ATP
-
liver enzyme
0.24
-
ATP
-
native wild-type enzyme, pH 7.5, 25C
0.24
-
ATP
-
mutant enzyme E192A
0.243
-
ATP
-
pH 7, 25C
0.28
-
ATP
-
pH 7.5, 22C
0.28
-
ATP
-
native glycosomal isozyme, pH 7.6, 25C
0.29
-
ATP
-
recombinant glycosomal isozyme, pH 7.6, 25C
0.3
-
ATP
-
pH 7, 25C
0.33
-
ATP
-
recombinant truncated glycosomal isozyme, pH 7.6, 25C
0.33
-
ATP
-
wild-type enzyme, pH 7.5, 25C
0.33
-
ATP
-
mutant enzyme F196A
0.356
-
ATP
-
pH 8.2, 25C
0.357
-
ATP
-
pH 7, 25C
0.367
-
ATP
-
pH 7.6, 25C
0.38
-
ATP
-
recombinant His-tagged enzyme, pH 7.5, 25C
0.404
-
ATP
-
pH 8.2, 25C
0.406
-
ATP
-
pH 7.6, 25C
0.42
-
ATP
-
isozyme PGK2A
0.42
-
ATP
-
wild-type, in cytosolic-enriched cellular extracts, at 37C, pH 7.0
0.46
-
ATP
-
native glycosomal isozyme, pH 7.6, 25C
0.587
-
ATP
-
recombinant purified mutant Y239F/E309M, at 37C, pH 7.0
0.637
-
ATP
-
recombinant purified mutant E309M, at 37C, pH 7.0
0.66
-
ATP
-
mutant enzyme S392A/T393A
0.73
-
ATP
-, P20971
pH 7.5, 70C, enzyme expressed in Escherichia coli; pH 7.5, 70C, native enzyme; recombinant enzyme, 70C
0.83
-
ATP
-
mutant enzyme F165A
0.86
-
ATP
-
mutant enzyme T393A
0.96
-
ATP
-
mutant enzyme R38A
1.04
-
ATP
-
mutant enzyme T375A
1.1
-
ATP
-
pH 6.5, 25C
1.1
-
ATP
-, P20971
native enzyme, 70C; pH 7.5, 70C, native enzyme
1.104
-
ATP
-
recombinant purified mutant V311L, at 37C, pH 7.0
1.11
-
ATP
P61884
pH 7.5, 70C, enzyme expressed in Escherichia coli
1.25
-
ATP
-
mutant P204H, pH 7.5, 25C
1.313
-
ATP
-
recombinant purified mutant E309Q, at 37C, pH 7.0
1.34
-
ATP
-
mutant enzyme N336A
1.439
-
ATP
-
recombinant purified wild-type, at 37C, pH 7.0
1.6
-
ATP
-
mutant K215A, at 4C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
1.69
-
ATP
-
mutant enzyme E343A
2.244
-
ATP
-
recombinant purified mutant Y239F, at 37C, pH 7.0
2.47
-
ATP
-
mutant enzyme K125A
4.05
-
ATP
P61884
native enzyme, 70C; pH 7.5, 70C, native enzyme
4.43
-
ATP
-
mutant enzyme k219A
4.8
-
ATP
P61884
pH 7.5, 70C, native enzyme; recombinant enzyme, 70C
5
-
ATP
-
wild-type, in cytosolic-enriched cellular extracts, at 37C, pH 7.0
9.7
-
ATP
-
70C, pH 6.5
0.077
-
D-ADP
-
pH 7.5, temperature not specified in the publication
0.5
-
D-ATP
-
-
0.5
-
D-GTP
-
-
0.348
-
GTP
-
recombinant purified mutant Y239F/E309M, at 37C, pH 7.0
2.5
-
L-2'-dCTP
-
-
1
-
L-2'-dGTP
-
-
0.1
-
L-ADP
-
pH 7.5, temperature not specified in the publication
0.27
-
L-ADP
-
L-MgADP-
0.3
-
L-ATP
-
-
1.5
-
L-CTP
-
-
0.15
-
L-GTP
-
-
1.1
-
Mg2+
-, P20971
native and recombinant enzyme, 70C
0.27
-
MgADP-
-
-
0.04
-
MgATP2-
-
pH 7.8, 25C
0.09
-
MgATP2-
-
pH 7.5, isozyme PGKA, in presence of 0.05 mM 1,3-bisphosphoglycerate
0.095
-
MgATP2-
-
pH 7.5, isozyme PGKB, in presence of 0.05 mM 1,3-bisphosphoglycerate
0.12
-
MgATP2-
-
recombinant isozyme 56PGK
0.15
0.2
MgATP2-
-
pH 7.5, 30C
0.15
0.2
MgATP2-
-
heart and skeletal muscle enzymes, pH 7.4, 25C
0.3
-
MgATP2-
-
-
0.32
-
MgATP2-
-
isozyme PGK2, pH 7.3-7.8
0.35
-
MgATP2-
-
pH 7.0
0.37
-
MgATP2-
-
isozyme PGK1, pH 7.3
0.37
-
MgATP2-
-
isozyme PGK2B
0.48
-
MgATP2-
Saccharomyces cerevisiae, Spirulina geitleri
-
-
4.1
-
MgATP2-
-
pH 7.3
3.45
-
MgdATP2-
-
pH 7.8, 25C
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
pH-dependence of Km values for the substrates in forward and reverse reaction
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics for 3-phospho-D-glycerate are biphasic
-
additional information
-
additional information
-
Km for ATP at different concentrations
-
additional information
-
additional information
-
biphasic kinetics
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
Km-value for MgATP, activation energy
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
pH-dependence of Km values for the substrates in forward and reverse reaction, 2 isozymes
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
temperature-dependence of the kinetics
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
Km values at different pH-values
-
additional information
-
additional information
-
the enzyme shows hyperbolic saturation kinetics for 3-phospho-D-glycerate, ATP and 3-phospho-D-glyceroyl phosphate. For ADP it shows a high affinity binding for the reaction in the reverse direction and a low affinity inhibitory effect for the forward as well as the reverse reaction
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4
-
2'-dCTP
-
-
110
-
2'-dGTP
-
-
0.067
-
3-phospho-D-glycerate
-
mutant enzyme T393del
0.45
-
3-phospho-D-glycerate
-
mutant enzyme R38A
0.48
-
3-phospho-D-glycerate
-
mutant enzyme K125A
0.9
-
3-phospho-D-glycerate
-
mutant enzyme k219A
3.4
-
3-phospho-D-glycerate
-
mutant P204H, pH 7.5, 25C
6
-
3-phospho-D-glycerate
-
mutant enzyme N336A
13.5
-
3-phospho-D-glycerate
-
co-substrate: ATP, mutant D218A/D374A, pH and temperature not specified in the publication
14.3
-
3-phospho-D-glycerate
-
mutant enzyme E343A
16.4
-
3-phospho-D-glycerate
-
mutant enzyme S392A/T393A
58
-
3-phospho-D-glycerate
-
mutant enzyme T393A
100
-
3-phospho-D-glycerate
-
co-substrate: ATP, mutant D218A, pH and temperature not specified in the publication
113
-
3-phospho-D-glycerate
P61884
recombinant enzyme, 70C
113.4
-
3-phospho-D-glycerate
P61884
pH 7.5, 70C; pH 7.5, 70C, recombinant enzyme
125
-
3-phospho-D-glycerate
-
mutant enzyme T375A
149.8
-
3-phospho-D-glycerate
-, P20971
pH 7.5, 60C, recombinant enzyme; pH 7.5, 70C
150
-
3-phospho-D-glycerate
-, P20971
recombinant enzyme, 70C
155
-
3-phospho-D-glycerate
-
mutant enzyme E192A
200
-
3-phospho-D-glycerate
-
mutant enzyme S398A
208
-
3-phospho-D-glycerate
-
co-substrate: ATP, mutant D374A, pH and temperature not specified in the publication
220
-
3-phospho-D-glycerate
-
co-substrate: ATP, wild-type, pH and temperature not specified in the publication
225.2
-
3-phospho-D-glycerate
-, P20971
pH 7.5, 70C, recombinant enzyme; pH 7.5, 80C
238.5
-
3-phospho-D-glycerate
P61884
pH 7.5, 80C; pH 7.5, 80C, recombinant enzyme
254.5
-
3-phospho-D-glycerate
-, P20971
pH 7.5, 73C, recombinant enzyme; pH 7.5, 90C
270
-
3-phospho-D-glycerate
-
mutant enzyme F165A
338.9
-
3-phospho-D-glycerate
-, P20971
pH 7.5, 80C, recombinant enzyme; pH 7.5, 98C
339
-
3-phospho-D-glycerate
-, P20971
recombinant enzyme, 98C
354
-
3-phospho-D-glycerate
-
wild-type enzyme, pH 7.5, 25C
362
-
3-phospho-D-glycerate
-
recombinant His-tagged enzyme
505.8
-
3-phospho-D-glycerate
P61884
pH 7.5, 90C; pH 7.5, 90C, recombinant enzyme
537
-
3-phospho-D-glycerate
-
recombinant wild-type enzyme
540
-
3-phospho-D-glycerate
-
native wild-type enzyme
570
-
3-phospho-D-glycerate
-
-
575
-
3-phospho-D-glycerate
-
mutant enzyme S392A
610
-
3-phospho-D-glycerate
-
mutant enzyme F196A
833
-
3-phospho-D-glycerate
-
wild-type enzyme
916
-
3-phospho-D-glycerate
P61884
pH 7.5, 98C; pH 7.5, 98C, recombinant enzyme; recombinant enzyme, 98C
0.78
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme K125A
5.25
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme k219A
6
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme R38A
23.2
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme N336A
84
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme E343A
250
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme T393A
675
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme T375A
1130
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme E192A
1170
-
3-phospho-D-glyceroyl phosphate
-
mutant enzyme F165A
2630
-
3-phospho-D-glyceroyl phosphate
-
wild-type enzyme
2633
-
3-phospho-D-glyceroyl phosphate
-
wild-type enzyme
0.06
-
ADP
-
mutant K215A, at 4C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
0.78
-
ADP
-
mutant enzyme K125A
0.78
-
ADP
-
mutant K215A, at 20C, in methanol-free buffer, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
5.25
-
ADP
-
mutant enzyme k219A
6
-
ADP
-
mutant enzyme R38A
23.3
-
ADP
-
mutant enzyme N336A
84
-
ADP
-
mutant enzyme E343A
200
-
ADP
-
wild-type, at 4C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
250
-
ADP
-
mutant enzyme T393A
675
-
ADP
-
mutant enzyme T375A
963.1
-
ADP
-
enzymatic activity in bulk condition
1130
-
ADP
-
mutant enzyme E192A
1170
-
ADP
-
mutant enzyme F165A
2630
-
ADP
-
wild-type enzyme
2633
-
ADP
-
wild-type enzyme
2633
-
ADP
-
wild-type, at 20C, in methanol-free buffer, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
0.05
-
ATP
-
mutant K215A, at 4C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
0.067
-
ATP
-
mutant enzyme T393del
0.45
-
ATP
-
mutant enzyme R38A
0.48
-
ATP
-
mutant enzyme K125A
0.48
-
ATP
-
mutant K215A, at 20C, in methanol-free buffer, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
0.9
-
ATP
-
mutant enzyme k219A
2.48
-
ATP
-
wild-type, at 4C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
3.4
-
ATP
-
mutant P204H, pH 7.5, 25C
6
-
ATP
-
mutant enzyme N336A
14.3
-
ATP
-
mutant enzyme E343A
16.4
-
ATP
-
mutant enzyme S392A/T393A
58
-
ATP
-
mutant enzyme T393A
113.4
-
ATP
P61884
pH 7.5, 70C; pH 7.5, 70C, native enzyme
125
-
ATP
-
mutant enzyme T375A
149.8
-
ATP
-, P20971
pH 7.5, 60C, native enzyme; pH 7.5, 70C
155
-
ATP
-
mutant enzyme E192A
200
-
ATP
-
mutant enzyme S398A
225.2
-
ATP
-, P20971
pH 7.5, 70C, native enzyme; pH 7.5, 80C
238.5
-
ATP
P61884
pH 7.5, 80C; pH 7.5, 80C, native enzyme
254.5
-
ATP
-, P20971
pH 7.5, 73C, native enzyme; pH 7.5, 90C
270
-
ATP
-
mutant enzyme F165A
338.9
-
ATP
-, P20971
pH 7.5, 98C; pH 7.5, 98C, native enzyme
354
-
ATP
-
wild-type enzyme, pH 7.5, 25C
411
-
ATP
-
recombinant His-tagged enzyme
500
-
ATP
-
recombinant wild-type enzyme
505.8
-
ATP
P61884
pH 7.5, 90C; pH 7.5, 90C, native enzyme
519
-
ATP
-
native wild-type enzyme
575
-
ATP
-
mutant enzyme S392A
610
-
ATP
-
mutant enzyme F196A
833
-
ATP
-
wild-type enzyme
833
-
ATP
-
wild-type, at 20C, in methanol-free buffer, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
916
-
ATP
P61884
pH 7.5, 98C; pH 7.5, 98C, native enzyme
200
-
D-ADP
-
pH 7.5, temperature not specified in the publication
500
-
D-ATP
-
-
420
-
D-GTP
-
-
86
-
L-ADP
-
pH 7.5, temperature not specified in the publication
685
-
L-ADP
-
L-MgADP-
100
-
L-ATP
-
-
120
-
L-GTP
-
-
additional information
-
additional information
-
temperature-dependence of kinetic
-
additional information
-
additional information
-
temperature-dependence of kinetic
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.48
-
ADP
-
mutant K215A, at 4C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
13
2600
-
ADP
-
wild-type, at 4C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
13
0.03
-
ATP
-
mutant K215A, at 4C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
4
90
-
ATP
P61884
pH 7.5, 93C
4
100
-
ATP
-, P20971
pH 7.5, 73C
4
150
-
ATP
-
wild-type, at 4C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
4
2600
-
D-ADP
-
pH 7.5, temperature not specified in the publication
23600
900
-
L-ADP
-
pH 7.5, temperature not specified in the publication
8594
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.44
1.5
1,3-bis(difluoro)-1,3-diphospho-2-dihydroxypropane
-
pH 7.5, 25C
-
3.25
3.3
1,4-bis(difluoro)-1,4-diphospho-diethylether
-
pH 7.5, 25C
0.56
-
1,4-Bisphosphonobutane
-
pH 8.5, 27C
1.19
-
1,5-Bisphosphonopentane
-
pH 8.5, 27C
26
-
1,5-Bisphosphonopentane
-
pH 7.5, 20C, versus 3-phospho-D-glycerate
0.109
-
1-beta-D-arabinofuranosylcytosine
-
pH 7.5
0.087
-
2',2'-difluorodeoxycytidine
-
pH 7.5
0.12
-
2',3'-dideoxy-2',3'-didehydro-beta-L(-)-5-fluorodeoxycytidine
-
pH 7.5
0.065
-
2'-fluoro-5-methyl-beta-L-arabinofuranosyluracil
-
pH 7.5
0.35
-
2,3-diphosphoglycerate
-
pH 7.5, 20C, versus 3-phospho-D-glycerate
2.3
-
2,3-diphosphoglycerate
-
versus MgATP2-
3.8
-
2,3-diphosphoglycerate
-
versus 3-phospho-D-glycerate
0.1
-
2-(p-Sulfophenylazo)-1,8-dihydroxy-3,6-naphthalene disulfonic acid
-
pH 7.5, versus 3-phospho-D-glycerate
0.15
-
2-(p-Sulfophenylazo)-1,8-dihydroxy-3,6-naphthalene disulfonic acid
-
pH 7.5, versus MgATP2-
0.065
-
2-Hydroxy-3,5-diiodobenzoate
-
versus 3-phospho-D-glycerate, pH 7.8, 25C
0.075
-
2-Hydroxy-3,5-diiodobenzoate
-
versus MgATP2-, pH 7.8, 25C
0.06
-
2-Hydroxy-5-iodobenzoate
-
versus 3-phospho-D-glycerate, pH 7.8, 25C
0.084
-
2-Oxo-1,4-bisphosphonobutane
-
pH 8.5, 27C
0.2
-
2-Oxo-1,5-bisphosphonopentane
-
pH 8.5, 27C
4
-
2-Phosphoglycolate
-
pH 7.5, 20C, versus 3-phospho-D-glycerate
3.5
-
4-Phosphonobutyronitrile
-
pH 8.5, 27C
0.08
-
ADP
-
pH 6.5, 25C, versus ATP
0.175
-
ADP
-
pH 6.5, 25C, versus 3-phospho-D-glycerate
1.14
-
ADP
-
70C, pH 6.5
0.17
-
ADP3-
-
pH7.8, 25C, versus MgATP2-, dependent on concentration of MgATP2-
0.22
-
ADP3-
-
pH7.8, 25C, versus MgATP2-, dependent on concentration of MgATP2-
1.5
-
AMP
-
pH 7.8, 25C, versus 3-phospho-D-glycerate
2
-
AMP
-
pH 7.8, 25C, versus MgATP2-
1.5
-
AMP2-
-
pH 7.8, 25C
0.25
-
beta-L-2',3'-dideoxy-3'-thiacytidine
-
pH 7.5
0.045
-
D-2',3'-dideoxycytidine
-
pH 7.5
0.035
-
D-MgADP-
-
-
0.09
-
diphosphate
-
mutant enzyme N336A
0.13
-
diphosphate
-
mutant enzyme R38A
0.14
-
diphosphate
-
mutant enzyme E343A
0.22
-
diphosphate
-
wild-type enzyme
0.51
-
diphosphate
-
mutant enzyme K125A
0.52
-
diphosphate
-
mutant enzyme k219A
1.9
-
diphosphate
-
mutant enzyme T375A
9.6
-
Glycerol 2-phosphate
-
pH 7.5, 20C, versus 3-phospho-D-glycerate
0.7
-
glycerol 3-phosphate
-
pH 7.5, 20C, versus 3-phospho-D-glycerate
1.28
-
Hexametaphosphate
-
pH 7.5, versus 3-phospho-D-glycerate
23
-
hydroxyethylidene bisphosphonic acid
-
pH 7.5, versus MgATP2-
25
-
hydroxyethylidene bisphosphonic acid
-
pH 7.5, versus 3-phospho-D-glycerate
0.125
-
L-2',3'-dideoxycytidine
-
pH 7.5
-
0.063
-
L-MgADP-
-
-
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
5.5
-
Naphthalene-1,3,6-trisulfonic acid
-
pH 7.5, versus 3-phospho-D-glycerate
8.3
-
phosphate
-
pH 7.5, 20C, versus 3-phospho-D-glycerate
0.009
-
salicylate
-
versus 3-phospho-D-glycerate, pH 7.8, 25C
0.011
-
salicylate
-
versus MgATP2-, plote: slope, pH 7.8, 25C
14
-
sulfate
-
pH 7.5, 20C, versus 3-phospho-D-glycerate
0.13
-
suramin
-
pH 7.5, versus MgATP2-
0.16
-
suramin
-
pH 7.5, versus 3-phospho-D-glycerate
0.039
-
MgADP-
-
pH 7.5, 20C
additional information
-
additional information
-
inhibition kinetics
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
Ki-values for phosphonate analogues of 1,3-diphosphoglycerate
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.007
-
suramin
-
IC50: 0.007 mM
additional information
-
additional information
-
the IC50 values are predicted within a factor of 2 over the 240x experimental range in activity
-
additional information
-
additional information
-
IC50 values are predicted within a factor of ca. 4 over a 2500x range in activity
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.02
-
-
pH 8.1, 37C, activity in undialyzed cell extracts
1.4
-
-
purified mutant P204F
4.5
-
-
purified mutant P204H
8.5
-
-
purified isozyme PGK2C
8.69
-
-
pH 7.5, 50C
47.5
-
-
pH 8, 30C, purified enzyme
65
-
-
mutant T378P, pH 7.4, 25C
69
-
-
purified cytosolic isozyme
75
-
-, P20971
purified recombinant enzyme
75
-
P61884
pH 7.5, 70C
90
-
-
mutant I47N, pH 7.4, 25C
98
-
-
purified enzyme
143
-
-
purified enzyme
150
-
-, P20971
pH 7.5, 70C; purified recombinant enzyme
159
-
-
purified recombinant cytosolic isozyme; purified recombinant truncated glycosomal isozyme
169
-
-
purified enzyme
184
-
-
purified enzyme
220
-
-
mutant E252A, pH 7.4, 25C
259
-
-
purified enzyme
260
450
-
purified isozyme PGKB
260
-
-
mutant L89P, pH 7.4, 25C
300
-
-
purified liver enzyme
420
-
-
wild-type, pH 7.4, 25C
430
-
-
purified isozyme PGK2B
450
-
-
purified isozyme PGK2A
460
-
-
purified muscle enzyme
468
-
-
purified wild-type enzyme
470
-
Bufo vulgaris
-
purified enzyme
480
-
-
purified enzyme
481
-
-
purified enzyme
500
-
-
purified isozyme PGK1
500
-
-
purified isozyme PGKA
504
-
-
purified enzyme
530
-
P50311
purified, detagged recombinant enzyme
540
-
-
purified liver enzyme
550
-
-
purified recombinant His-tagged enzyme
557
-
-
purified enzyme
560
-
-
purified enzyme
580
-
-
purified crystalline enzyme
600
700
-
purified enzyme
600
-
-
purified testis enzyme
600
-
-
purified enzyme
620
-
-
purified enzyme
644
-
-
purified chloroplastic isozyme
650
700
-
purified enzyme, at 25C
650
-
-
purified liver enzyme
650
-
-
purified enzyme
680
-
-
purified erythrocyte enzyme
680
-
-
purified enzyme
690
-
Chrysophrys guttulatus, Pseudocheirus peregrinus, Salmo trutta
-
purified enzyme
695
-
-
purified enzyme
700
-
trout
-
purified enzyme
700
-
-
purified muscle enzyme
700
-
-
-
700
-
-
purified muscle enzyme
700
-
-
purified enzyme
700
-
-
purified muscle enzyme
700
-
-
purified isozyme PGKA
700
-
-
purified New Guinea variant
702
-
-
purified enzyme
710
-
-
purified muscle enzyme
710
-
-
purified enzyme
710
-
-
purified muscle enzyme
720
-
Spirulina geitleri
-
purified enzyme
720
-
-
-
720
-
-
purified isozyme PGKB
750
-
-
purified recombinant wild-type and native wild-type enzyme
760
-
-
purified enzyme
780
-
-
purified enzyme
785
-
-
purified enzyme
798
-
-
purified cytosolic isozyme
800
-
-
purified enzyme
800
-
-
purified chloroplastic isozyme
810
-
-
purified enzyme
850
-
-
purified enzyme
900
980
-
purified enzyme, depending on purification method
914
-
-
purified isozymes
945
-
-
purified eenzyme
1000
-
Equus caballus, Sus scrofa, Vombatus sp.
-
about, purified enzyme
1000
-
-
purified enzyme, at 35C
1311
-
-
purified recombinant glycosomal isozyme
2260
-
-
purified, crystalline enzyme
additional information
-
-
-
additional information
-
-
-
additional information
-
-
high specific activity at low temperature, cold-adapted organism
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7.5
-
-
6
8.5
-
-
6
9
trout
-
-
6
-
-
assay at
6.5
8.5
-
-
6.5
-
-
assay at
6.5
-
-
-
6.5
-
-
assay at
7.3
7.8
-
PGK2
7.3
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
both isozymes
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-, P20971
assay at
7.5
-
P61884
assay at
7.5
-
P46273
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.6
-
-
assay at
7.6
-
P50311
assay at
7.8
-
-
assay at
7.9
-
-
assay at
7.9
-
P00558
assay at
8
-
-
assay at
8
-
-
recombinant wild-type
8.3
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.8
10
-
pH 4.8: about 45% of activity maximum, pH 10.0: about 90% of activity maximum
5.4
8
-
30% activity at pH 5.4, 60% activity at pH 8.0
5.5
7.6
-
90% activity at pH 6.0 and pH 7.4, 70% activity at pH 5.5, about 35% activity at pH 7.6
7.5
8.75
-
optimal pH range
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
assay at
22
-
-
assay at
22
-
-
assay at
22
-
-
assay at
23
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
P46273
assay at
25
-
-
assay at
25
-
P00558
assay at
25
-
-
assay at
25
-
P50311
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
35
-
-
-
37
-
-
assay at
40
-
-
-
55
60
-
physiological temperature
70
-
-, P20971
assay at
70
-
P61884
assay at
100
-
P61884
optimum beyond 100C; temperature optimum beyond 100C, where activity can not be assayed under the experimental conditions
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
40
-
activity of both isozymes in either reaction direction increases steadily with increasing temperature within this range
40
90
-, P20971
the enzyme shows considerable activity at 40C, 90C: optimum
40
-
P61884
only active above 40C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.8
-
-
3 peaks of purified enzyme at pH 3.8, pH 5.75, and pH 7.45, isoelectric focusing using an analytical column with carrier ampholytes
4.3
4.4
-
thin-layer isoelectric focusing
4.7
4.8
-
New Guinea population variant, isoelectric focusing
4.8
-
-
thin-layer isoelectric focusing
4.8
-
Spirulina geitleri
-
-
4.9
-
-
recombinant wild-type
5
-
-
analytical electric focusing
5.2
-
-
chloroplastic isozyme, isoelectric focusing
5.3
-
-
thin-layer isoelectric focusing
5.4
-
-
cytsolic isozyme, isoelectric focusing
5.75
-
-
3 peaks of purified enzyme at pH 3.8, pH 5.75, and pH 7.45, isoelectric focusing using an analytical column with carrier ampholytes
6.3
6.8
-
native cytosolic isozyme, isoelectric focusing
6.5
-
-
recombinant cytosolic isozyme, isoelectric focussing
7.45
-
-
3 peaks of purified enzyme at pH 3.8, pH 5.75, and pH 7.45, isoelectric focusing using an analytical column with carrier ampholytes
7.9
-
-
isoelectric focusing
8.75
-
-
isoelectric focusing
9.2
-
-
truncated glycosomal isozyme, isoelectric focusing
9.3
-
-
glycosomal isozyme, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
hypoxic treatment induces the protein expression of PGK
Manually annotated by BRENDA team
-
pancreatic carcinoma cell line, low amount of enzyme compared to HT-1080 cells
Manually annotated by BRENDA team
-
of 10 cancer patients whose serum is tested, 3 of 4 with pancreatic cancer have 65-900% higher levels of PGK1 than that found in normal serum
Manually annotated by BRENDA team
-
PGKB and PGKC genes-encoding phosphoglycerate kinase are co-transcribed as part of a polycistronic RNA. PGKC mRNA and glycosomal PGKC protein are specific to bloodstream forms
Manually annotated by BRENDA team
-
quantitative analysis of the expression of phosphoglycerate kinase in bloodstream form
Manually annotated by BRENDA team
Q9DG72, -
approximately 2fold increase in pgk1 transcripts in brain of frozen frogs. PGK1 protein levels rise by 3- to 5fold within 4-8 hr of freezing
Manually annotated by BRENDA team
-
moderate PGK1 expression
Manually annotated by BRENDA team
-
breast carcinoma cell line, reduced amount of enzyme compared to HT-1080 cells
Manually annotated by BRENDA team
-
pancreatic carcinoma cell line, low amount of enzyme compared to HT-1080 cells
Manually annotated by BRENDA team
-
moderate PGK1 expression
Manually annotated by BRENDA team
-
-, high expression
Manually annotated by BRENDA team
-
intrauterine, high concentration. Probably the miracidia in the eggs may accumulate the enzyme to produce the energy required for swimming after hatching
Manually annotated by BRENDA team
-
from intraperitoneal cavity
Manually annotated by BRENDA team
-
single-nucleotide polymorphisms is an adaptation to the external anoxic environment
Manually annotated by BRENDA team
-
remarkably low (less than 5% of normal) PGK enzyme activity level in patients with PGK deficiency
Manually annotated by BRENDA team
-
18-year-old man with muscle cramps and recurrent exertional myoglobinuria, without hemolytic anemia or brain dysfunction. PGK deficiency of the patient's erythrocytes, markedly decreased PGK activity
Manually annotated by BRENDA team
-
primary gastric carcinoma, overexpression of PGK1 and its signalling targets may be a expression-pathway in diffuse primary gastric carcinomas promoting peritoneal dissemination and may function as prognostic markers and/or be potential therapeutic targets to prevent the migration of gastric carcinoma cells into the peritoneum
Manually annotated by BRENDA team
-
of testis, PTBP2 is a trans-acting factor that helps to stabilize Pgk2 mRNA in male mouse germ cells
Manually annotated by BRENDA team
-
Pgk2 mRNA accumulates in postmeiotic germ cells
Manually annotated by BRENDA team
-
of adult and newborn rats
Manually annotated by BRENDA team
-
of adult and newborn rats
Manually annotated by BRENDA team
-
-, hypoxic treatment induces the protein expression of PGK
Manually annotated by BRENDA team
-
hypoxic treatment induces the protein expression of PGK
Manually annotated by BRENDA team
-
pancreatic carcinoma cell line, the same amount of enzyme compared to HT-1080 cells, pancreatic carcinoma cell line, reduced amount of enzyme compared to HT-1080 cells
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
-
colon carcinoma cell line, nearly the same amount of enzyme compared to HT-1080 cells
Manually annotated by BRENDA team
-
colon carcinoma cell line, increased amount of enzyme compared to HT-1080 cells
Manually annotated by BRENDA team
-
colon carcinoma cell line, increased amount of enzyme compared to HT-1080 cells
Manually annotated by BRENDA team
-
of adult and newborn rats
Manually annotated by BRENDA team
Q9DG72, -
freezing elevates pgk1 transcripts in liver
Manually annotated by BRENDA team
-
there is no significant difference in cell proliferation between parental Lewis lung carcinoma (LLC-1) and LLC-1 transduced with PGK-1. Overexpression of PGK-1 in LLC-1 reduces the COX-2 expression, and, in turn, affects prostaglandin E2, cell invasion, angiogenesis, and the immune functions, and finally inhibit the tumor progression
Manually annotated by BRENDA team
-
breast carcinoma cell line, the same amount of enzyme compared to HT-1080 cells
Manually annotated by BRENDA team
-
breast carcinoma cell line, low amount of enzyme compared to HT-1080 cells
Manually annotated by BRENDA team
Frog
-
-
Manually annotated by BRENDA team
trout
-
-
Manually annotated by BRENDA team
Esox sp., Testudinidae
-
-
Manually annotated by BRENDA team
-
isozyme PGKA
Manually annotated by BRENDA team
-
isozyme PGKA
Manually annotated by BRENDA team
-
18-year-old man with muscle cramps and recurrent exertional myoglobinuria, without hemolytic anemia or brain dysfunction. PGK deficiency of the patient's muscle, PGK activity in muscle extracts in patients is less than 10% of normal
Manually annotated by BRENDA team
Mus musculus DBA/2J
-
isozyme PGKA
-
Manually annotated by BRENDA team
-
surrounding the intestine and sperm ducts of adults
Manually annotated by BRENDA team
-
2fold higher level than in testis
Manually annotated by BRENDA team
-
-, hypoxic treatment induces the protein expression of PGK
Manually annotated by BRENDA team
-
strong expression of PGK1 in more than 70% of the tumors, 7.7- to 11.7fold higher expression in the tumor tissues versus the adjacent nontumor samples
Manually annotated by BRENDA team
-
normal or cancer-associated fibroblasts
Manually annotated by BRENDA team
-
clonality analysis of pulmonary sclerosis hemangioma samples with androgen receptor and phosphoglycerate kinase gene polymorphisms and an analysis of gene expression demonstrate that polygonal and surface cuboidal cells in pulmonary sclerosing hemangioma likely arise from a common progenitor
Manually annotated by BRENDA team
-
-, hypoxic treatment induces the protein expression of PGK
Manually annotated by BRENDA team
-
levels of PGK1 are significantly higher in pancreatic ductal adenocarcinoma patients than in the control group, patients with gastric cancer have significantly elevated serum levels of PGK1 comparable to those observed in pancreatic ductal adenocarcinoma patients. In breast cancer patients levels of PGK1 are increased only slightly, and show no significant difference in colorectal cancer patients
Manually annotated by BRENDA team
-
of adult and newborn rats
Manually annotated by BRENDA team
Q9DG72, -
freezing does not elevate pgk1 transcripts in skin
Manually annotated by BRENDA team
P09041
phosphoglycerate kinase 2 is a sperm-specific isoform
Manually annotated by BRENDA team
-
in early meiosis
Manually annotated by BRENDA team
-
pancreatic carcinoma cell line, very high amount of enzyme compared to HT-1080 cells
Manually annotated by BRENDA team
-
ovarian cancer cell line
Manually annotated by BRENDA team
-
mature, isozyme PGK2
Manually annotated by BRENDA team
-
isozyme PGKB
Manually annotated by BRENDA team
-
testis-specific isozyme PGKB, isozyme PGKA
Manually annotated by BRENDA team
-
polypyrimidine tract binding protein 2 binds to PGK2 mRNA in the testis, PTBP2 is a trans-acting factor that helps to stabilize Pgk2 mRNA in male mouse germ cells
Manually annotated by BRENDA team
-
similar levels of Pgk2 mRNA transcription in nuclei isolated from the testes of prepuberal (17 day old) and adult mice
Manually annotated by BRENDA team
Mus musculus DBA/2J
-
isozyme PGKB
-
Manually annotated by BRENDA team
-
of the mouse lower first molar. Strong expression of Pgk1 mRNA in the odontogenic epithelial cells and surrounding mesenchymal cells of the tooth germ from embryonic day 10.5 to embryonic day 18.0
Manually annotated by BRENDA team
-
distinct expression of PGK1
Manually annotated by BRENDA team
additional information
-
commercial product
Manually annotated by BRENDA team
additional information
-
isozyme PGK1 is found in all somatic tissues
Manually annotated by BRENDA team
additional information
-
A-673 cell
Manually annotated by BRENDA team
additional information
-
H460 cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
90% of total enzyme activity
Manually annotated by BRENDA team
-
hypoxia has no effect on the subcellular distribution of the PGK protein
Manually annotated by BRENDA team
trout
-
-
Manually annotated by BRENDA team
-
in parasites grown in the gut of tsetse fly
Manually annotated by BRENDA team
-
cytosolic isozyme
Manually annotated by BRENDA team
-
10% of total enzyme activity
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
isozyme 56PGK, glycosomal microbody
Manually annotated by BRENDA team
-
in parasites grown in mammalian bloodstream
Manually annotated by BRENDA team
-
both chloroplastic and cytosolic phosphoglycerate kinase isozymes are present in the pea leaf nucleus
Manually annotated by BRENDA team
-
patients with peritoneal carcinomatosis show a medium to strong nuclear staining for PGK1
Manually annotated by BRENDA team
additional information
-
the catalytically active cytosolic isozyme is toxic and lethal for bloodstream parasites
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Escherichia coli (strain K12)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Staphylococcus aureus (strain MRSA252)
Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
34000
47000
-
gel filtration, ultracentrifugation, amino acid analysis, tryptophan content
38000
48000
-
gel filtration, ultracentrifugation, amino acid analysis, tryptophan content
38000
-
-
cytoplasmic and chloroplastic isoenzyme, gel filtration
39000
-
-
gel filtration, cytosolic and chloroplastic isoenzyme
39000
-
-
gel filtration, in presence of 0.37 M KCl
42000
-
-
gel filtration
42000
-
-
gel filtration
42300
-
-
calculated from cDNA
42400
-
-
calculated from cDNA
43000
49500
-
gel filtration, sedimentation equilibrium studies, equilibrium diffusion ultracentrifugation
43000
-
-
UV cross-linking experiments
43700
-
-
high speed sedimentation equilibrium method
44000
-
-
gel filtration
44000
-
-
isoenzyme PGK1 and PGK2, gel filtration
44000
-
-
gel filtration
44500
-
-
gel filtration
44520
-
-
amino acid sequence
44600
-
-
sedimentation equilibrium studies
44660
-
-
erythrocytes, amino acid sequence
45000
-
-
gel filtration; isozymes PGKA and PGKB
45000
-
-
SDS-PAGE, recombinant protein
45000
-
-
gel filtration
45100
-
-
2-DE and MALDI-TOF MS
47000
-
-
gel filtration; isoenzymes PGK1, PGK2A, PGK2B, PGK2C
47000
-
-
isozyme PGKA and PGKB, tryptophan content
47000
-
-
gel filtration
47000
-
-
gel filtration
47900
-
-
sedimentation equilibrium method
48000
-
-
analytical ultracentrifugation
49000
50000
-
gel filtration, ultracentrifugation, tryptophan content
49600
-
-
sedimentation equilibrium method
50000
-
-
gel filtration, ultracentrifugation, amino acid analysis, tryptophan content
50000
-
-
sedimentation equilibrium method
87000
-
P61884
gel filtration, at 600 mM K+, recombinant enzyme
87100
90000
P61884
recombinant enzyme, gel filtration in presence of 0.6 M KCl, and analytical ultracentrifugation
90000
-
P61884
ultracentrifugation, recombinant enzyme
94700
-
-, P20971
gel filtration, at 600 mM K+, recombinant enzyme; recombinant enzyme, gel filtration in presence of 0.6 M KCl
97000
-
-, P20971
gel filtration, at 600 mM K+, native enzyme
97100
-
-, P20971
gel filtration at 600 mM K+; native enzyme, gel filtration in presence of 0.6 M KCl
102700
-
P61884
gel filtration at 600 mM K+; gel filtration, at 600 mM K+, native enzyme; native enzyme, gel filtration in presence of 0.6 M KCl
180000
-
-
ternary complex of 2 dimers build of 4 enzyme molecules, crystal structure determination
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 47000, SDS-PAGE
?
-
x * 48000, SDS-PAGE
?
-
x * 45000, SDS-PAGE
?
P50311
x * 45000, SDS-PAGE
?
-
x * 46000, SDS-PAGE
?
-
x * 46000, SDS-PAGE
?
-
x * 46000, SDS-PAGE
?
-
x * 46000, SDS-PAGE
?
Spirulina geitleri
-
x * 46000, SDS-PAGE
?
-
x * 41000, SDS-PAGE
?
-
x * 40000, recombinant wild-type, SDS-PAGE
?
-
x * 47000, glycosomal isozyme, SDS-PAGE
?
-
x * 44395, calculated from sequence
dimer
-, P20971
2 * 45000, SDS-PAGE
dimer
P61884
2 * 45000, SDS-PAGE
dimer
-, P20971
2 * 45870, DNA and amino acid sequence determination
dimer
-
x * 45000, cytosolic and truncated glycosomal isozymes, SDS-PAGE
dimer
P61884
2 * 46161, DNA and amino acid sequence determination
dimer
Pyrococcus woesei Vul 4
-
2 * 45000, SDS-PAGE, 2 * 46161, DNA and amino acid sequence determination
-
dimer
Pyrococcus woesei DSM 3773
-
2 * 45000, SDS-PAGE, 2 * 46161, DNA and amino acid sequence determination
-
homodimer
P61884
2 * 45000, SDS-PAGE
homodimer
-, P20971
2 * 45000, SDS-PAGE
homodimer
-, P20971
2 * 45871, calculated from sequence
homodimer
P61884
2 * 46195, calculated from sequence, 2 * 46224, calculated from sequence
homodimer
-
2 * 45000, SDS-PAGE, 2 * 45871, calculated from sequence
-
homodimer
Pyrococcus woesei Vul 4
-
2 * 45000, SDS-PAGE, 2 * 46195, calculated from sequence, 2 * 46224, calculated from sequence
-
homodimer
Pyrococcus woesei DSM 3773
-
2 * 45000, SDS-PAGE, 2 * 46195, calculated from sequence, 2 * 46224, calculated from sequence
-
monomer
-
-
monomer
-
-
monomer
-
-
monomer
trout
-
-
monomer
Esox sp., Testudinidae
-
-
monomer
-
1 * 47000, SDS-PAGE
monomer
-
1 * 47000, SDS-PAGE
monomer
-
1 * 46000, SDS-PAGE
monomer
-
1 * 46000, SDS-PAGE
monomer
-
1 * 48000, SDS-PAGE
monomer
-
1 * 48000, SDS-PAGE
monomer
-
1 * 42000, SDS-PAGE
monomer
-
1 * 50000, SDS-PAGE
monomer
-
1 * 44000, SDS-PAGE
monomer
-
1 * 44600
monomer
-
1 * 44800, SDS-PAGE
monomer
-
1 * 44300
monomer
-
1 * 45600, SDS-PAGE
monomer
-
1 * 46100
monomer
-
1 * 44000, isoenzymes PGK1 and PGK2, SDS-PAGE
monomer
-
1 * 47000-47500, isozymes PGKA and PGKB, SDS-PAGE
monomer
-
1 * 47000, isozymes PGKA and PGKB, SDS-PAGE
monomer
-
1 * 47900, SDS-PAGE
monomer
-
1 * 38000, chloroplastic and cytoplasmic enzyme
monomer
-
1 * 43000
monomer
-
1 * 43700
monomer
-
1 * 40700, cytosolic isozyme, SDS-PAGE
monomer
-
1 * 43400
monomer
-
1 * 41000, chloroplastic isozyme, SDS-PAGE
monomer
-
1 * 43900
monomer
-
1 * 44200
monomer
-
1 * 44400
monomer
-
1 * 45200
monomer
-
1 * 45700
monomer
-
gel filtration, 1 * 45000
monomer
Mus musculus DBA/2J
-
1 * 47000, isozymes PGKA and PGKB, SDS-PAGE
-
monomer
Rhodopseudomonas palustris JCM2524
-
1 * 43400
-
monomer
Geobacillus stearothermophilus NCA 1503
-
1 * 42000, SDS-PAGE
-
monomer
Lactobacillus delbrueckii subsp. lactis NCC88
-
1 * 46000, SDS-PAGE
-
monomer
Entamoeba histolytica HM1:IMSS
-
-
-
additional information
-
-
additional information
P50311
secondary structure
additional information
-
ternary structure
additional information
-
secondary structure: 29% alpha-helix, 11% pleated sheets
additional information
-
secondary and tertiary structure
additional information
-
overview: structure functioin relationship
additional information
-
structure model
additional information
-
secondary structure: 20% alpha-helix, 45% beta-structure
additional information
Geobacillus stearothermophilus NCA 1503
-
secondary structure: 20% alpha-helix, 45% beta-structure
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystallized using lithium sulfate as the precipitant to a resolution of 2.5 A. The AbPGK crystals belong to space group P2221
-
crystallization from ammonium sulfate precipitation
-
in the presence of 1 mM AMP-PNP and 1 mM MgCl2, by the vapor diffusion method, solved by molecular replacement to 2.4 A resolution; vapor diffusion method
-, P0A799
hanging drop vapour phase diffusion method, 18C, protein solution: 15 mg/ml, Tris-HCl, pH 7.0, 1 mM MgATP2-, 0.1 mM NaN3, 10% w/v polyethylene glycol 600, precipitant is 40% w/v polyethylene glycol 600, X-ray diffraction structure determination and analysis
-
crystallization from ammonium sulfate precipitate within 10 min, recrystallization
-
crystallization via precipitation with ammonium sulfate stepwise from 30-35% to 65% w/v within 24 h
-
crystallization via precipitation with ammonium sulfate stepwise from 60% to 75% w/v at room temperature for 2 h, then 4C, several days
-
crystals of the 3PG-HsPGK binary complex in an open conformation (HsPGK-3PG-open) are grown, and ADP and the nonhydrolyzable ATP analogue, AMP-PCP, are introduced, by soaking, to investigate the effect of their binding on the open conformation
-
hPGK crystals are obtained at 20 C by the sitting drop method. A crystal structure of hPGK in a fully closed conformation in complex with L-ADP, 3-phosphoglycerate, and the transition-state analogue AlF4- is determined
-
vapour diffusion in hanging drop method. Crystal structures of hPGK in its free state, or bound to L-ADP, D-ADP, D-CDP or L-CDP
P00558
crystallized in three forms: as the apoenzyme, as a complex with 3-phosphoglycerate, and as a complex with 3-phosphoglycerate and ATP. The crystal structures are solved to 2.7, 2.0, and 2.7 A resolutions, respectively
P09041
crystal structures of Plasmodium falciparum phosphoglycerate kinase (PfPGK) is determined in open conformation in two different crystal forms to 2.7 A and 3 A resolution, respectively. In both structures a sulfate ion is bound in the ATP binding site and a second sulfate ion is located at the regulatory basic patch in the second crystal form
P27362
hanging-drop vapour-diffusion method, recombinant enzyme forms a hexagonal space group P6(1)22 with unit cell parameters a = b = 140.7 A, c = 263.9 A, 3.0 A resolution
-
crystallization as native enzyme within 8-12 months or in complex with 3-phosphoglycerate and ATP analogue inhibitor beta,gamma-imido-adenosine-5'-triphosphate within 2-3 days, X-ray diffraction structure determination and analysis
-
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
-
mutant 72p yPGK
-
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
-
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 15C, within about 2 weeks
-
crystal structure of unliganded PGK, solved by molecular replacement to 1.8 A resolution, crystals belong to the P212121 space group with one molecule per asymmetric unit
Q08GC7
hanging drop vapour-diffusion method, enzyme crystallizes in the P2(1)2(1)2(1) space group with one molecule in the asymmetric unit, cell dimension a = 65.1, b = 71.3, c = 80.2 A, up to 1.8 A resolution
-
crystallization from ammonium sulfate precipitation overnight with gradually raising of temperature from 4C to room temperature, in presence of ATP
-
crystallization from ammonium sulfate precipitation with 37% w/v by hanging or sitting drop vapour diffusion method, protein solution: 4 mg/ml, PIPES buffer, pH 6.8, 10 mM MgCl2, 1 mM ATP, 10% (NH4)2SO4, 22C, 7-14 days, high resolution X-ray diffraction structure determination and analysis, rotating camera system
-
purified, recombinant enzyme is crystallized as a ternary complex by vapour diffusion method, 10C, protein solution: 6 mg/ml, 10 mM 3-phospho-D-glycerate, 10 mM MgADP, 25 mM Tris, pH 7.5, 50 mM NaCl, 10 m DTT, plus equal volume of 2.5 M sodium potassium phosphate, pH 8.0; purified, recombinant enzyme is crystallized in complex with nucleotide analogue Mg-beta,gamma-imido-adenosine-5'-triphosphate by vapour diffusion method, 10C, protein solution: 6 mg/ml, 10 mM 3-phospho-D-glycerate, 10 mM MgADP-, 25 mM Tris, pH 7.5, 50 mM NaCl, 10 m DTT, plus equal volume of 2.5 M sodium potassium phosphate, pH 7.5; structure determination and analysis
-
vapour diffusion method, protein solution containing 2.5 M potassium sodium phosphate, pH 8.0, X-ray diffraction structure determination and analysis
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.7
-
-
isozyme PGKB: loss of 70% activity after 45 min, isozyme PGKA: loss of 10% activity after 45 min
5.5
-
-
inactivation below
6
-
-
unstable below
6.5
8
-
crystallized enzyme, solved at a low concentration loses 10% activity per 24 h; enzyme in crude hemolysate is stable at 4C for at least 1 week, inactive below pH 6.0
7
9.2
-
75% activity retained at pH 9.2, a sharp reduction of activity below pH 7
9.2
-
-
75% activity retained at pH 9.2
9.6
-
-
isozymes PGKA and PGKB: stable for at least 30 min
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24
-
-
two stable, folded conformers with an abrupt conformational transition occurring at 24C. 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
25
-
-
30 min, 27% loss of activity
37
-
-
30 min, nearly 80% loss of activity
47
-
-
midpoint temperature Tm, without a ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
48
-
-
midpoint temperature Tm, without a ligand, mutant enzyme W308F/W333F, value determined by differential scanning calometry
48
-
-
midpoint temperature Tm, with MgATP2- as ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
49
-
-
30 min, approximately 95% loss of activity
49
-
-
midpoint temperature Tm, with MgATP2- as ligand, mutant enzyme W308F/W333F, value determined by differential scanning calometry
49
-
-
midpoint temperature Tm, with MgADP- as ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
50
-
-
unstable above
50
-
-
pH 6.0, 10 min: 20% loss of activity, PGKA, 80% loss of activity PGKB
50
-
-
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
51
-
-
midpoint temperature Tm, with 3-phosphoglycerate as ligand, mutant enzyme W308F/W333F, value determined by differential scanning calometry
51
-
-
midpoint temperature Tm, with 3-phosphoglycerate and MgADP- as ligand, carboxamidomethylated enzyme
52
-
-
midpoint temperature Tm, with MgADP- as ligand, mutant enzyme W308F/W333F, value determined by differential scanning calometry
52
-
-
midpoint temperature Tm, with 3-phosphoglycerate as ligand, carboxamidomethylated enzyme, value determined by differential scanning calometry
52.8
-
-
Tm (wild-type): 52.8C, t1/2 (wild-type, 37C): 3 years
53
-
-
midpoint temperature Tm, without a ligand, mutant enzyme W333F, value determined by differential scanning calometry
53
-
-
midpoint temperature Tm, without a ligand, unmodified enzyme, 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
55
-
-
midpoint temperature Tm, with MgATP2- as ligand, unmodified enzyme, value determined by differential scanning calometry
56
-
-
midpoint temperature Tm, with MgATP2- as ligand, mutant enzyme W333F, value determined by differential scanning calometry; midpoint temperature Tm, without a ligand, wild-type enzyme, value determined by differential scanning calometry
57
-
-
midpoint temperature Tm, with 3-phosphoglycerate as ligand, mutant enzyme W333F, value determined by differential scanning calometry; midpoint temperature Tm, with MgADP- as ligand, mutant enzyme W333F, 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, mutant enzyme W333F, with 3-phosphoglycerate and MgADP- as ligand, 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
60
-
-
10 min, stable
60
-
-
midpoint temperature Tm, with 3-phosphoglycerate as ligand, wild-type enzyme, value determined by differential scanning calometry; midpoint temperature Tm, with MgATP2- as ligand, wild-type enzyme, value determined by differential scanning calometry
61
-
-
30 min, enzyme retains less than 4% of its activity
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
65
-
-
80% activity at 65C, then rapidly decreasing between 65-80C; enzymatic activity is completely lost at temperatures over 65C
79
-
-
20 min, no loss of activity
80
-
-
half life: 39 min
83
-
-, P20971
half-life: 44 min
85
-
P61884
the enzyme from the original organism is completely resistant to heat inactivation for 35 min. Expression in Escherichia coli at optimal growth temperatures (37C) yields a product which shows a tight association with a 28000 Da protein and exhibits low thermal stability (about 80% loss of activity after 5 min) suggesting a misfolding of the protein. As proved by N-terminal amino acid sequence analysis, the 28000 Da protein represents a 226-amino acid C-terminal fragment of the 3-phosphoglycerate kinase. Mutagenesis experiments confirm the assumption that the fragment originates by an internal translation initiation
86
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-, P20971
half-life: 44 min
89
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-, P20971
half-life: 10 min
92
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5 min, 75% loss of activity
100
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P61884
half-life: 28 min
104
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P61884
half-life: 10 min
additional information
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PGK1 is more heat-stable than PGK2
additional information
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additional information
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thermal analysis
additional information
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additional information
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thermal denaturation at pH 5.5 and pH 7.5 of the isoenzymes
additional information
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-, P20971
stabilizing effects of anions on thermal stability
additional information
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P61884
stabilizing effects of anions on thermal stability
additional information
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thermal analysis
additional information
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the recombinant His-tagged wild-type enzyme shows reduced thermostability compared to the native and recombinant wild-type without tag
additional information
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decreased thermostability, cold-adapted organism
additional information
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the psychrophilic enzyme enzyme exhibits two distinct stability domains in the free, open conformation. These stability domains do not match the structural N- and C-domains as the heat-stable domain corresponds to about 80 residues of the C-domain, including the nucleotide binding site, whereas the remaining of the protein contributes to the main heat-labile domain
additional information
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L-MgADP binds to the specific adenosine-binding site and protects the conformation of hPGK molecule against heat denaturation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
bovine serum albumin and dithioerythritol stabilize in the enzyme assay
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phosphoglycerate kinase is resistant to proteolytic cleavage. ecPGK can only be digested through its globally unfolded state, suggesting that cooperativity between the two domains results in a more rigid protein that has low susceptibility to proteolysis
-, P0A799
bovine serum albumin and dithioerythritol stabilize in the enzyme assay
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crystalline enzyme is rather unstable, dried crystals or dilute aqueous solutions lose all activity within a few weeks
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dissolved cyrstallized enzyme at low concentration is rapidly inactivated at neutral pH
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freeze-drying inactivates
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L-MgADP binds to the specific adenosine-binding site and protects the conformation of hPGK molecule against heat denaturation
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K+ stabilizes
-, P20971
stabilized by anions in decreasing order of efficiency: 2,3-bisphospho-D-glycerate, PO43-, SO42-, Cl-
-, P20971
the stabilizing effects of anions on thermal stability
-, P20971
bovine serum albumin and dithioerythritol stabilize in the enzyme assay
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optimal stabilization at 1 mM EDTA and 5 mM 2-mercaptoethanol
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bovine serum albumin and dithioerythritol stabilize in the enzyme assay
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K+ stabilizes
P61884
potassium salts of polyvalent anions stabilize the enzyme
P61884
the stabilizing effects of anions on thermal stability
P61884
enzyme shows highest thermal stability in ternary complex with 3-phosphoglycerate and MgADP-, due to domain closure
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Pro204 is important for stability and catalytic mechanism of the enzyme
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the extrapolated unfolding rate of Escherichia coli PGK is 100000 slower than that of the yeast homolog