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2',3'-didehydro-2',3'-dideoxythymidine triphosphate + 3-phospho-D-glycerate
2',3'-didehydro-2',3'-dideoxythymidine diphosphate + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
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
2',3'-dideoxy-GTP + 3-phospho-D-glycerate
2',3'-dideoxy-GDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
2'-dATP + 3-phospho-D-glycerate
2'-dADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
2'-deoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2'-deoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
2'-dGTP + 3-phospho-D-glycerate
2'-dGDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
2'-dTTP + 3-phospho-D-glycerate
2'-dTDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
3'-deoxy-3'-azidothymidine triphosphate + 3-phospho-D-glycerate
3'-deoxy-3'-azidothymidine diphosphate + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
acyclovir triphosphate + 3-phospho-D-glycerate
acyclovir diphosphate + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ADP + 1,3-bisphosphoglycerate
ATP + 3-phosphoglycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate.
ATP + 3-phosphoglycerate
ADP + 1,3-bisphosphoglycerate
-
-
-
-
r
ATP + Beclin1
ADP + Ser30-phosphorylated Beclin1
-
-
-
?
beta-L(-)-dioxolanecytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L(-)-dioxolanecytidine 5'-diphosphate + 1,3-diphosphoglycerate
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
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
D-ADP + 1,3-bisphosphoglycerate
?
-
-
-
?
D-ATP + 1,3-bisphospho-D-glycerate
?
-
-
-
-
?
D-ATP + 3-phospho-D-glycerate
D-ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
D-CDP + 1,3-bisphospho-D-glycerate
?
-
-
-
-
?
D-CTP + 3-phospho-D-glycerate
D-CDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
D-GTP + 3-phospho-D-glycerate
D-GDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
dATP + 3-phospho-D-glycerate
dADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
dITP + 3-phospho-D-glycerate
dIDP + 1,3-diphosphoglycerate
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
L-2'-dATP + 3-phospho-D-glycerate
L-2'-dADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
L-2'-dCTP + 3-phospho-D-glycerate
L-2'-dCDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
L-2'-dGTP + 3-phospho-D-glycerate
L-2'-dGDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
L-2'-dTTP + 3-phospho-D-glycerate
L-2'-dTDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
L-ADP + 1,3-bisphosphoglycerate
?
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
-
L-MgADP is almost as a good substrate for hPGK as the natural D-MgADP
-
-
?
L-ATP + 1,3-bisphospho-D-glycerate
?
-
-
-
-
?
L-ATP + 3-phospho-D-glycerate
L-ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
L-CDP + 1,3-bisphospho-D-glycerate
?
-
-
-
-
?
L-CTP + 3-phospho-D-glycerate
L-CDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
L-GTP + 3-phospho-D-glycerate
L-GDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
L-UTP + 3-phospho-D-glycerate
L-UDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
UTP + 3-phospho-D-glycerate
UDP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
additional information
?
-
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
-
isozyme PGK1
-
-
?
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
-
3.6fold higher activity compared to 2'-deoxycytidine
-
-
?
2'-deoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2'-deoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
-
-
-
?
2'-deoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2'-deoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
isozyme PGK1
-
-
?
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
-
-
-
-
r
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
-
-
-
-
?
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
-
-
-
-
r
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
-
-
-
-
r
ADP + 1,3-bisphosphoglycerate
ATP + 3-phosphoglycerate
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 + 1,3-bisphosphoglycerate
ATP + 3-phosphoglycerate
-
-
-
-
r
ADP + 1,3-bisphosphoglycerate
ATP + 3-phosphoglycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
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
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
-
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
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Esox sp.
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Frog
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
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
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
the enzyme favors the forward reaction
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
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
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
key enzyme of anaerobic glycolysis in Plasmodium falciparum
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Pyrococcus woesei Vul 4 / DSM 3773
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
the reaction occurs at 70°C
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
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
-
the enzyme favors the forward reaction
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Spirulina geitleri
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
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
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
?
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
key enzyme in glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Bufo vulgaris
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Chrysophrys guttulatus
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Esox sp.
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Frog
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
absolute specificity for 3-phospho-D-glycerate
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
absolute specificity for 3-phospho-D-glycerate
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
absolute specificity for 3-phospho-D-glycerate
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
absolute specificity for 3-phospho-D-glycerate
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
simultaneous binding of both substrates is essential for domain closure
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
specific for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
specific for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Pyrococcus woesei Vul 4 / DSM 3773
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
high specificity for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
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
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
high specificity for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Spirulina geitleri
-
high specificity for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
reaction equilibrium favors ATP production
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
high specificity for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
high specificity for ATP
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
trout
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
Vombatus sp.
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 1,3-diphosphoglycerate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
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
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
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
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
Pyrococcus woesei Vul 4 / DSM 3773
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
the reaction occurs at 30°C
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
Spirulina geitleri
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate.
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate.
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate.
Pyrococcus woesei Vul 4 / DSM 3773
-
-
-
?
beta-L(-)-dioxolanecytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L(-)-dioxolanecytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
isozyme PGK1
-
-
?
beta-L(-)-dioxolanecytidine 5'-triphosphate + 3-phospho-D-glycerate
beta-L(-)-dioxolanecytidine 5'-diphosphate + 1,3-diphosphoglycerate
-
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
-
isozyme PGK1
-
-
?
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
-
4fold higher activity compared to 2'-deoxycytidine
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
low activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
1% of the activity with ATP
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
1% of the activity with ATP
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
Spirulina geitleri
-
no activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
low activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
-
low activity
-
-
?
CTP + 3-phospho-D-glycerate
CDP + 1,3-diphosphoglycerate
trout
-
no activity
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
Esox sp.
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
Frog
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
-
27% of the activity with ATP
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
-
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
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
Spirulina geitleri
-
low activity
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
-
-
-
-
?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
Esox sp.
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
Frog
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
-
isozyme PGK2C with lower activity, all other isozymes show slightly lower activity compared to ATP
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
Spirulina geitleri
-
no activity
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
-
-
-
-
?
dGTP + 3-phospho-D-glycerate
dGDP + 1,3-diphosphoglycerate
-
-
-
-
?
dITP + 3-phospho-D-glycerate
dIDP + 1,3-diphosphoglycerate
-
-
-
-
?
dITP + 3-phospho-D-glycerate
dIDP + 1,3-diphosphoglycerate
Spirulina geitleri
-
no activity
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
Esox sp.
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
Frog
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
27% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
27% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
36% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
60% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
60% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
60% of the activity with ATP
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
low activity
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
Spirulina geitleri
-
very low activity
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
low activity
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
low activity
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
trout
-
-
-
-
?
GTP + 3-phospho-D-glycerate
GDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
Esox sp.
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
Frog
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
42% of the activity with ATP
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
42% of the activity with ATP
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
45% of the activity with ATP
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
64% of the activity with ATP
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
low activity
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
Spirulina geitleri
-
very low activity
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
trout
-
-
-
-
?
ITP + 3-phospho-D-glycerate
IDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
-
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
Esox sp.
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
Frog
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
-
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
-
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
1% of the activity with ATP
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
1% of the activity with ATP
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
-
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
low activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
only traces of activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
-
no activity
-
-
?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
trout
-
-
-
-
?
additional information
?
-
enzymes is confirmed by total proteome analysis of glycerol-grown cells
-
-
?
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
?
-
3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation
-
-
?
additional information
?
-
-
3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation
-
-
?
additional information
?
-
3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation
-
-
?
additional information
?
-
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
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
?
-
Esox sp.
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
Frog
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
-
single-nucleotide polymorphisms is an adaptation to the external anoxic environment
-
-
?
additional information
?
-
-
no activity with pyrimidine nucleotides
-
-
?
additional information
?
-
-
no activity with pyrimidine nucleotides
-
-
?
additional information
?
-
-
-
-
-
?
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
?
-
-
also catalyzes ADP-ATP exchange reaction
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
phylogenetic tree
-
-
?
additional information
?
-
-
phylogenetic tree
-
-
?
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
?
-
-
nucleotide substrate specificity
-
-
?
additional information
?
-
-
no activity with dTTP
-
-
?
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
?
-
-
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 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
?
-
-
no activity with dCTP, dUTP, dTTP
-
-
?
additional information
?
-
-
2',3'-dideoxycytidine is a very poor substrate
-
-
?
additional information
?
-
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
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
?
-
-
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
?
-
-
no activity with dCTP, dUTP, dTTP
-
-
?
additional information
?
-
Spirulina geitleri
-
no activity with dCTP, dUTP, dTTP
-
-
?
additional information
?
-
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
-
enzyme is regulated by multivalent anions
-
-
?
additional information
?
-
-
2-domain hinge-binding enzyme
-
-
?
additional information
?
-
-
the oxidized PGK contains chloroplast-type thioredoxin (Trx)-accessible disulfide bond
-
-
?
additional information
?
-
-
reactivity in descending order: ATP, ITP, GTP, dGTP, dATP
-
-
?
additional information
?
-
trout
-
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
?
-
trout
-
nucleotide substrate specificity
-
-
?
additional information
?
-
trout
-
no activity with dTTP
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + 1,3-bisphosphoglycerate
ATP + 3-phosphoglycerate
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phosphoglycerate
ADP + 1,3-bisphosphoglycerate
-
-
-
-
r
ATP + Beclin1
ADP + Ser30-phosphorylated Beclin1
-
-
-
?
additional information
?
-
ADP + 1,3-bisphosphoglycerate
ATP + 3-phosphoglycerate
-
-
-
-
r
ADP + 1,3-bisphosphoglycerate
ATP + 3-phosphoglycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Esox sp.
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Frog
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
the enzyme favors the forward reaction
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
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
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
key enzyme of anaerobic glycolysis in Plasmodium falciparum
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Pyrococcus woesei Vul 4 / DSM 3773
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
the reaction occurs at 70°C
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
the enzyme favors the forward reaction
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
Spirulina geitleri
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
responsible for production of ATP during glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
key enzyme in glycolysis
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
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
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
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
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
Pyrococcus woesei Vul 4 / DSM 3773
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
the reaction occurs at 30°C
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
Spirulina geitleri
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
?
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
ATP + 3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl phosphate
-
-
-
-
r
additional information
?
-
-
enzyme is identical with the socalled host factor, which activates RNA transcription in Sendai virus, when bound in a complex with host tubulin and a complementary factor
-
-
?
additional information
?
-
3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation
-
-
?
additional information
?
-
-
3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation
-
-
?
additional information
?
-
3-phosphoglycerate kinase catalyzes phosphoryl transfer from 1,3-biphosphoglycerate to ADP to yield 3-phosphoglycerate and ATP in substrate chain phosphorylation
-
-
?
additional information
?
-
-
single-nucleotide polymorphisms is an adaptation to the external anoxic environment
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
phylogenetic tree
-
-
?
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
?
-
-
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
?
-
-
the oxidized PGK contains chloroplast-type thioredoxin (Trx)-accessible disulfide bond
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0022 - 11.9
3-phospho-D-glycerate
0.0005 - 5.6
3-phospho-D-glyceroyl phosphate
0.48 - 0.68
3-phosphoglycerate
0.077
D-ADP
pH 7.5, temperature not specified in the publication
0.348
GTP
-
recombinant purified mutant Y239F/E309M, at 37°C, pH 7.0
1.1
Mg2+
native and recombinant enzyme, 70°C
additional information
additional information
-
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
0.146
3-phospho-D-glycerate
-
at pH 7.4, temperature not specified in the publication
0.15
3-phospho-D-glycerate
-
isozyme PGK2B, ADP, isoenzyme PGK2A
0.16
3-phospho-D-glycerate
isoform PGK-2, pH and temperature not specified in the publication
0.174
3-phospho-D-glycerate
native isozyme PGKA, pH 7.5, 22°C
0.174
3-phospho-D-glycerate
wild type enzyme, isoform PGKA, pH and temperature not specified in the publication
0.18
3-phospho-D-glycerate
-
pH and temperature not specified in the publication
0.18
3-phospho-D-glycerate
-
wild-type, 30°C, pH not specified in the publication
0.186
3-phospho-D-glycerate
at pH 7.4, temperature not specified in the publication
0.192
3-phospho-D-glycerate
isozyme PGKC, pH 7.5, 22°C
0.192
3-phospho-D-glycerate
wild type enzyme, isoform PGKC, pH and temperature not specified in the publication
0.2
3-phospho-D-glycerate
-
pH 6.9, 25°C
0.2
3-phospho-D-glycerate
-
isoenzyme PGK2A
0.22
3-phospho-D-glycerate
isoform PGK-1, pH and temperature not specified in the publication
0.24
3-phospho-D-glycerate
-
mutant D218A/D374A, pH and temperature not specified in the publication
0.26
3-phospho-D-glycerate
pH 7.4, 30°C, recombinant enzyme
0.26
3-phospho-D-glycerate
-
pH and temperature not specified in the publication
0.27
3-phospho-D-glycerate
-
mutant D218A, pH and temperature not specified in the publication
0.28
3-phospho-D-glycerate
wild type enzyme, pH and temperature not specified in the publication
0.28
3-phospho-D-glycerate
natural enzyme, at pH 7.6 and 25°C
0.31
3-phospho-D-glycerate
mutant enzyme E343A
0.32
3-phospho-D-glycerate
-
mutant enzyme S392A
0.35
3-phospho-D-glycerate
pH 7.9, 25°C, recombinant oxidized wild-type enzyme
0.37
3-phospho-D-glycerate
pH 7.9, 25°C, recombinant reduced wild-type enzyme
0.4
3-phospho-D-glycerate
wild type enzyme, at pH 8.0 and 37°C
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, 25°C
0.48
3-phospho-D-glycerate
native enzyme, pH and temperature not specified in the publication
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, 25°C
0.53
3-phospho-D-glycerate
-
mutant enzyme E192A
0.53
3-phospho-D-glycerate
wild type enzyme, pH and temperature not specified in the publication
0.54
3-phospho-D-glycerate
70°C, pH 6.5
0.54
3-phospho-D-glycerate
mutant enzyme N336A
0.547
3-phospho-D-glycerate
recombinant enzyme, pH and temperature not specified in the publication
0.57
3-phospho-D-glycerate
-
-
0.57
3-phospho-D-glycerate
-
at pH 7.0 and 30°C
0.58
3-phospho-D-glycerate
mutant enzyme M189I, at pH 8.0 and 37°C
0.589
3-phospho-D-glycerate
-
pH 8.2, 25°C
0.59
3-phospho-D-glycerate
-
pH 7.5, 25°C
0.59
3-phospho-D-glycerate
-
isozyme PGK1, pH 7.3
0.6 - 0.7
3-phospho-D-glycerate
-
pH 7.5, 30°C
0.601
3-phospho-D-glycerate
-
pH 7, 25°C
0.62
3-phospho-D-glycerate
wild type enzyme, isoform PGKB, pH and temperature not specified in the publication
0.63
3-phospho-D-glycerate
mutant enzyme T375A
0.63
3-phospho-D-glycerate
recombinant truncated isozyme PGKA mutant, pH 7.5, 22°C
0.661
3-phospho-D-glycerate
pH and temperature not specified in the publication
0.683
3-phospho-D-glycerate
-
pH 8.2, 25°C
0.69
3-phospho-D-glycerate
-
mutant enzyme F196A
0.707
3-phospho-D-glycerate
-
pH 7, 25°C
0.71
3-phospho-D-glycerate
recombinant enzyme, pH and temperature not specified in the publication
0.71
3-phospho-D-glycerate
recombinant enzyme, at pH 7.6 and 25°C
0.711
3-phospho-D-glycerate
-
pH 7.6, 25°C
0.719
3-phospho-D-glycerate
-
pH 7.6, 25°C
0.72
3-phospho-D-glycerate
-
-
0.75
3-phospho-D-glycerate
native enzyme, 70°C
0.75
3-phospho-D-glycerate
pH 7.5, 70°C, recombinant enzyme
0.75
3-phospho-D-glycerate
pH 7.5, 70°C, native enzyme
0.77
3-phospho-D-glycerate
-
wild-type enzyme, pH 7.5, 25°C
0.77
3-phospho-D-glycerate
recombinant enzyme, 70°C
0.77
3-phospho-D-glycerate
pH 7.5, 70°C, recombinant enzyme
0.77
3-phospho-D-glycerate
pH 7.5, 70°C, enzyme expressed in Escherichia coli
0.78
3-phospho-D-glycerate
mutant enzyme V216F, at pH 8.0 and 37°C
0.8
3-phospho-D-glycerate
-
-
0.81
3-phospho-D-glycerate
-
-
0.85
3-phospho-D-glycerate
recombinant wild-type isozyme PGKA, pH 7.5, 22°C
0.85
3-phospho-D-glycerate
recombinant enzyme, isoform PGKA, pH and temperature not specified in the publication
0.89
3-phospho-D-glycerate
recombinant His-tagged enzyme, pH 7.5, 25°C
0.89
3-phospho-D-glycerate
His-tagged recombinant enzyme, pH and temperature not specified in the publication
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
native enzyme, 70°C
1.1
3-phospho-D-glycerate
-
at 0.1 M
1.1
3-phospho-D-glycerate
-
at 1.5-13 mM 3-phospho-D-glycerate concentration
1.1
3-phospho-D-glycerate
-
pH and temperature not specified in the publication
1.11
3-phospho-D-glycerate
pH 7.5, 70°C, recombinant enzyme
1.25
3-phospho-D-glycerate
-
native cytosolic isozyme, pH 7.6, 25°C
1.26
3-phospho-D-glycerate
-
-
1.28
3-phospho-D-glycerate
-
at 1.5-13 mM 3-phospho-D-glycerate concentration
1.28
3-phospho-D-glycerate
pH and temperature not specified in the publication
1.37
3-phospho-D-glycerate
-
pH and temperature not specified in the publication
1.39
3-phospho-D-glycerate
-
-
1.4
3-phospho-D-glycerate
-
-
1.4
3-phospho-D-glycerate
recombinant enzyme, 70°C
1.4
3-phospho-D-glycerate
-
heart enzyme, pH 7.4, 25°C
1.4
3-phospho-D-glycerate
pH 7.5, 70°C, recombinant enzyme
1.4
3-phospho-D-glycerate
pH 7.5, 70°C, enzyme expressed in Escherichia coli
1.41
3-phospho-D-glycerate
-
-
1.45
3-phospho-D-glycerate
-
isoform PGKB, pH and temperature not specified in the publication
1.5
3-phospho-D-glycerate
-
pH 6.5, 25°C
1.5
3-phospho-D-glycerate
Spirulina geitleri
-
at 1.5-13 mM 3-phospho-D-glycerate concentration
1.5
3-phospho-D-glycerate
-
pH and temperature not specified in the publication
1.5
3-phospho-D-glycerate
Spirulina geitleri
-
pH and temperature not specified in the publication
1.54
3-phospho-D-glycerate
mutant enzyme G166D, at pH 8.0 and 37°C
1.55
3-phospho-D-glycerate
-
native glycosomal isozyme, pH 7.6, 25°C
1.55
3-phospho-D-glycerate
-
pH and temperature not specified in the publication
1.55
3-phospho-D-glycerate
wild type enzyme, isoform PGKC, pH and temperature not specified in the publication
1.61
3-phospho-D-glycerate
mutant enzyme R65W, at pH 8.0 and 37°C
1.635
3-phospho-D-glycerate
-
pH 8.2, 25°C
1.65
3-phospho-D-glycerate
-
liver enzyme, pH 7.4, 25°C
1.66
3-phospho-D-glycerate
-
skeletal muscle enzyme, pH 7.4, 25°C
1.66
3-phospho-D-glycerate
-
mutant enzyme S392A/T393A
1.72
3-phospho-D-glycerate
mutant enzyme k219A
1.77
3-phospho-D-glycerate
at pH 8.5 and 25°C
1.787
3-phospho-D-glycerate
-
pH 7.6, 25°C
1.79
3-phospho-D-glycerate
-
pH 7.5, 22°C
1.79
3-phospho-D-glycerate
pH and temperature not specified in the publication
1.948
3-phospho-D-glycerate
-
pH 7, 25°C
1.95
3-phospho-D-glycerate
mutant enzyme A199V, at pH 8.0 and 37°C
2
3-phospho-D-glycerate
-
recombinant glycosomal isozyme and native cytosoli isozyme, pH 7.6, 25°C
2
3-phospho-D-glycerate
50°C, pH not specified in the publication
2.02
3-phospho-D-glycerate
recombinant enzyme, isoform PGKC, pH and temperature not specified in the publication
2.04
3-phospho-D-glycerate
wild type enzyme, isoform PGKB, pH and temperature not specified in the publication
2.2
3-phospho-D-glycerate
-
pH 7.6, 25°C
2.2
3-phospho-D-glycerate
-
pH and temperature not specified in the publication
2.4
3-phospho-D-glycerate
-
recombinant isozyme 56PGK
2.5
3-phospho-D-glycerate
-
mutant P204H, pH 7.5, 25°C
2.6
3-phospho-D-glycerate
-
pH 6.8, 45°C
2.75
3-phospho-D-glycerate
-
isoform PGKB, pH and temperature not specified in the publication
3.15
3-phospho-D-glycerate
mutant enzyme R38M, at pH 8.0 and 37°C
4.5
3-phospho-D-glycerate
mutant enzyme R38A
4.8
3-phospho-D-glycerate
pH 7.5, 70°C, native enzyme
5.87
3-phospho-D-glycerate
mutant enzyme F241S, at pH 8.0 and 37°C
7.6
3-phospho-D-glycerate
-
pH 7.3
11.9
3-phospho-D-glycerate
-
recombinant truncated glycosomal isozyme, pH 7.6, 25°C
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
0.00438
3-phospho-D-glyceroyl phosphate
-
at pH 7.4, temperature not specified in the publication
0.005
3-phospho-D-glyceroyl phosphate
wild-type enzyme
0.00686
3-phospho-D-glyceroyl phosphate
at pH 7.4, temperature not specified in the publication
0.0077
3-phospho-D-glyceroyl phosphate
mutant enzyme k219A
0.008
3-phospho-D-glyceroyl phosphate
-
at pH 7.0 and 70°C
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
70°C, pH 6.5
0.48
3-phosphoglycerate
-
mutant enzyme H111A, at pH 7.5 and 25°C
0.49
3-phosphoglycerate
-
mutant enzyme H71A, at pH 7.5 and 25°C
0.511
3-phosphoglycerate
-
mutant enzyme H57A, at pH 7.5 and 25°C
0.517
3-phosphoglycerate
-
mutant enzyme H89A, at pH 7.5 and 25°C
0.53
3-phosphoglycerate
-
wild type enzyme, at pH 7.5 and 25°C
0.61
3-phosphoglycerate
-
mutant enzyme H57A, at pH 5.5 and 25°C
0.63
3-phosphoglycerate
-
mutant enzyme H89A, at pH 5.5 and 25°C
0.638
3-phosphoglycerate
-
mutant enzyme H111A, at pH 5.5 and 25°C
0.661
3-phosphoglycerate
-
wild type enzyme, at pH 5.5 and 25°C
0.68
3-phosphoglycerate
-
mutant enzyme H71A, at pH 5.5 and 25°C
0.039
ADP
-
isozyme PGK2C
0.077
ADP
-
wild-type, at 4°C, in 30% methanol, 20 mM triethanolamine, pH 7.5, 0.1 M potassium acetate, and 1 mM free Mg2+
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
wild-type enzyme
0.12
ADP
-
mutant enzyme F165A
0.126
ADP
-
mutant K215A, at 4°C, 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
0.2
ADP
-
ADP in form of MgADP-
0.221
ADP
at pH 7.4, temperature not specified in the publication
0.27
ADP
-
at pH 7.4, temperature not specified in the publication
0.27
ADP
-
ADP in form of MgADP-
0.28
ADP
-
recombinant purified mutant Y239F/E309M, at 37°C, pH 7.0
0.37
ADP
-
at pH 7.0 and 70°C
0.42
ADP
mutant enzyme N336A
0.5
ADP
-
wild-type, in cytosolic-enriched cellular extracts, at 37°C, 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 37°C, pH 7.0
1.696
ADP
-
recombinant purified mutant V311L, at 37°C, pH 7.0
1.723
ADP
-
recombinant purified mutant E309Q, at 37°C, pH 7.0
2.016
ADP
-
recombinant purified wild-type, at 37°C, pH 7.0
2.693
ADP
-
recombinant purified mutant Y239F, at 37°C, pH 7.0
7.4
ADP
-
wild-type, in cytosolic-enriched cellular extracts, at 37°C, pH 7.0
0.01
ATP
isozyme PGKC, pH 7.5, 22°C
0.017
ATP
-
wild-type, at 4°C, 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
0.04
ATP
-
ATP in form of MgATP2-
0.078
ATP
-
mutant enzyme S392A
0.09
ATP
-
pH 7.5, isozyme PGKA, in presence of 0.05 mM 1,3-bisphosphoglycerate
0.09
ATP
-
ATP in form of MgATP2-
0.09
ATP
wild type enzyme, isoform PGKB, pH and temperature not specified in the publication
0.095
ATP
-
pH 7.5, isozyme PGKB, in presence of 0.05 mM 1,3-bisphosphoglycerate
0.095
ATP
-
ATP in form of MgATP2-
0.1
ATP
wild type enzyme, isoform PGKC, pH and temperature not specified in the publication
0.102
ATP
-
mutant enzyme H71A, at pH 5.5 and 25°C
0.11
ATP
-
wild-type enzyme
0.11
ATP
wild-type enzyme
0.11
ATP
pH 7.4, 30°C, recombinant enzyme
0.11
ATP
-
pH and temperature not specified in the publication
0.11
ATP
-
wild-type, pH and temperature not specified in the publication
0.11
ATP
-
mutant D218A, pH and temperature not specified in the publication
0.118
ATP
pH and temperature not specified in the publication
0.118
ATP
-
wild type enzyme, at pH 5.5 and 25°C
0.12
ATP
-
recombinant isozyme 56PGK
0.12
ATP
-
ATP in form of MgATP2-
0.12
ATP
isoform PGK-1, pH and temperature not specified in the publication
0.122
ATP
-
mutant enzyme H71A, at pH 7.5 and 25°C
0.125
ATP
-
mutant enzyme H89A, at pH 5.5 and 25°C
0.128
ATP
-
mutant enzyme H111A, at pH 5.5 and 25°C
0.13
ATP
-
mutant enzyme T393del
0.13
ATP
wild type enzyme, pH and temperature not specified in the publication
0.13
ATP
-
isoform PGKB, pH and temperature not specified in the publication
0.13
ATP
natural enzyme, at pH 7.6 and 25°C
0.134
ATP
-
mutant enzyme H57A, at pH 5.5 and 25°C
0.139
ATP
-
mutant enzyme H89A, at pH 7.5 and 25°C
0.15 - 0.2
ATP
-
pH 7.5, 30°C
0.15 - 0.2
ATP
-
heart and skeletal muscle enzymes, pH 7.4, 25°C
0.15 - 0.2
ATP
-
ATP in form of MgATP2-
0.15 - 0.2
ATP
-
ATP in form of MgATP2-
0.152
ATP
-
wild type enzyme, at pH 7.5 and 25°C
0.156
ATP
-
mutant enzyme H57A, at pH 7.5 and 25°C
0.163
ATP
-
mutant enzyme H111A, at pH 7.5 and 25°C
0.18
ATP
-
mutant D374A, pH and temperature not specified in the publication
0.19
ATP
-
pH and temperature not specified in the publication
0.19
ATP
-
wild-type, 30°C, pH not specified in the publication
0.2
ATP
-
mutant D218A/D374A, pH and temperature not specified in the publication
0.21
ATP
recombinant wild-type enzyme, pH 7.5, 25°C
0.21
ATP
-
recombinant cytosolic isozyme, pH 7.6, 25°C
0.21
ATP
wild type enzyme, pH and temperature not specified in the publication
0.217
ATP
native isozyme PGKA, pH 7.5, 22°C
0.217
ATP
wild type enzyme, isoform PGKA, pH and temperature not specified in the publication
0.22
ATP
-
isoenzyme PGK1
0.236
ATP
recombinant wild-type isozyme PGKA, pH 7.5, 22°C
0.236
ATP
recombinant enzyme, isoform PGKA, pH and temperature not specified in the publication
0.24
ATP
native wild-type enzyme, pH 7.5, 25°C
0.24
ATP
-
mutant enzyme E192A
0.24
ATP
native enzyme, pH and temperature not specified in the publication
0.24
ATP
-
isoform PGKB, pH and temperature not specified in the publication
0.28
ATP
-
native glycosomal isozyme, pH 7.6, 25°C
0.28
ATP
pH and temperature not specified in the publication
0.28
ATP
wild type enzyme, isoform PGKC, pH and temperature not specified in the publication
0.29
ATP
-
recombinant glycosomal isozyme, pH 7.6, 25°C
0.29
ATP
recombinant enzyme, isoform PGKC, pH and temperature not specified in the publication
0.3
ATP
-
pH and temperature not specified in the publication
0.3
ATP
-
ATP in form of MgATP2-
0.31
ATP
pH 7.9, 25°C, recombinant oxidized wild-type enzyme
0.32
ATP
-
isozyme PGK2, pH 7.3-7.8
0.32
ATP
-
ATP in form of MgATP2-
0.33
ATP
-
wild-type enzyme, pH 7.5, 25°C
0.33
ATP
-
recombinant truncated glycosomal isozyme, pH 7.6, 25°C
0.33
ATP
-
mutant enzyme F196A
0.34
ATP
isoform PGK-2, pH and temperature not specified in the publication
0.35
ATP
-
ATP in form of MgATP2-
0.37
ATP
-
isozyme PGK1, pH 7.3
0.37
ATP
-
ATP in form of MgATP2-
0.37
ATP
-
ATP in form of MgATP2-
0.38
ATP
recombinant His-tagged enzyme, pH 7.5, 25°C
0.38
ATP
His-tagged recombinant enzyme, pH and temperature not specified in the publication
0.4
ATP
pH 7.9, 25°C, recombinant reduced wild-type enzyme
0.41
ATP
-
truncated enzyme, at pH 5.5 and 25°C
0.42
ATP
-
wild-type, in cytosolic-enriched cellular extracts, at 37°C, pH 7.0
0.42
ATP
-
pH and temperature not specified in the publication
0.46
ATP
-
native glycosomal isozyme, pH 7.6, 25°C
0.46
ATP
wild type enzyme, isoform PGKB, pH and temperature not specified in the publication
0.48
ATP
Spirulina geitleri
-
pH and temperature not specified in the publication
0.48
ATP
pH and temperature not specified in the publication
0.48
ATP
-
ATP in form of MgATP2-
0.48
ATP
Spirulina geitleri
-
ATP in form of MgATP2-
0.5
ATP
recombinant enzyme, pH and temperature not specified in the publication
0.5
ATP
recombinant enzyme, at pH 7.6 and 25°C
0.54
ATP
-
full-length enzyme, at pH 7.5 and 25°C
0.587
ATP
-
recombinant purified mutant Y239F/E309M, at 37°C, pH 7.0
0.637
ATP
-
recombinant purified mutant E309M, at 37°C, pH 7.0
0.64
ATP
recombinant truncated isozyme PGKA mutant, pH 7.5, 22°C
0.66
ATP
-
mutant enzyme S392A/T393A
0.73
ATP
recombinant enzyme, 70°C
0.73
ATP
pH 7.5, 70°C, enzyme expressed in Escherichia coli
0.73
ATP
pH 7.5, 70°C, native enzyme
0.83
ATP
-
mutant enzyme F165A
0.86
ATP
-
mutant enzyme T393A
0.89
ATP
-
pH and temperature not specified in the publication
0.96
ATP
mutant enzyme R38A
0.961
ATP
at pH 8.5 and 25°C
1
ATP
-
full-length enzyme, at pH 5.5 and 25°C
1.04
ATP
mutant enzyme T375A
1.1
ATP
native enzyme, 70°C
1.1
ATP
-
pH and temperature not specified in the publication
1.1
ATP
pH 7.5, 70°C, native enzyme
1.104
ATP
-
recombinant purified mutant V311L, at 37°C, pH 7.0
1.11
ATP
pH 7.5, 70°C, enzyme expressed in Escherichia coli
1.25
ATP
-
mutant P204H, pH 7.5, 25°C
1.313
ATP
-
recombinant purified mutant E309Q, at 37°C, pH 7.0
1.34
ATP
mutant enzyme N336A
1.439
ATP
-
recombinant purified wild-type, at 37°C, pH 7.0
1.439
ATP
recombinant enzyme, pH and temperature not specified in the publication
1.6
ATP
-
mutant K215A, at 4°C, 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
ATP
-
truncated enzyme, at pH 7.5 and 25°C
2.244
ATP
-
recombinant purified mutant Y239F, at 37°C, pH 7.0
2.47
ATP
mutant enzyme K125A
2.7
ATP
50°C, pH not specified in the publication
2.9
ATP
-
pH and temperature not specified in the publication
4.05
ATP
native enzyme, 70°C
4.05
ATP
pH 7.5, 70°C, native enzyme
4.1
ATP
-
ATP in form of MgATP2-
4.43
ATP
mutant enzyme k219A
4.8
ATP
recombinant enzyme, 70°C
4.8
ATP
pH 7.5, 70°C, native enzyme
5
ATP
-
wild-type, in cytosolic-enriched cellular extracts, at 37°C, pH 7.0
5
ATP
wild type enzyme, pH and temperature not specified in the publication
9.31
ATP
-
at pH 7.0 and 30°C
3.45
dATP
-
pH 7.8, 25°C
3.45
dATP
-
ATP in form of MgdATP2-
0.1
L-ADP
pH 7.5, temperature not specified in the publication
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
trout
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
biphasic kinetics
-
additional information
additional information
-
Km values at different pH-values
-
additional information
additional information
-
temperature-dependence of the kinetics
-
additional information
additional information
-
temperature-dependence of the kinetics
-
additional information
additional information
-
Km for ATP at different concentrations
-
additional information
additional information
-
kinetics for 3-phospho-D-glycerate are biphasic
-
additional information
additional information
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pH-dependence of Km values for the substrates in forward and reverse reaction
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additional information
additional information
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pH-dependence of Km values for the substrates in forward and reverse reaction
-
additional information
additional information
-
pH-dependence of Km values for the substrates in forward and reverse reaction
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
Bufo vulgaris
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
Km-value for MgATP, activation energy
-
additional information
additional information
Chrysophrys guttulatus
-
Km-value for MgATP, activation energy
-
additional information
additional information
-
pH-dependence of Km values for the substrates in forward and reverse reaction, 2 isozymes
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additional information
additional information
-
Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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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
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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
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additional information
additional information
Michaelis-Menten kinetics, kinetic analysis or CrPGK1, overview
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additional information
additional information
-
Michaelis-Menten kinetics, kinetic analysis or CrPGK1, overview
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