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3-phosphoglycerate 1-phosphotransferase
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3-phosphoglycerate kinase
3-phosphoglycerate phosphokinase
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3-phosphoglyceric acid kinase
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3-phosphoglyceric acid phosphokinase
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3-phosphoglyceric kinase
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ATP-3-phospho-D-glycerate-1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
ATP:D-3-phosphoglycerate 1-phosphotransferase
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glycerate 3-phosphate kinase
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glycerophosphate kinase
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human 3-phosphoglycerate kinase
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kinase (phosphorylating), phosphoglycerate
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phosphoglycerate kinase 1
phosphoglycerate kinase 2
phosphoglycerate kinase B
phosphoglycerate kinase-1
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phosphoglyceric acid kinase
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phosphoglyceric kinase
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phosphoglycerokinase
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testis-specific phosphoglycerate kinase 2
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X chromosome-linked phosphoglycerate kinase-1
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
Pyrococcus woesei Vul 4 / DSM 3773
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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3-phosphoglycerate kinase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
Spirulina geitleri
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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ATP:3-phospho-D-glycerate 1-phosphotransferase
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hPGK
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Mfer_0156
ordered locus name
Mfer_0156
ordered locus name
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PAS-PGK
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PGK
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PGK
Spirulina geitleri
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PGK-1
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PGK1
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PGK2
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PGKA
isoform
PGKB
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PGKC
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phosphoglycerate kinase
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phosphoglycerate kinase
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phosphoglycerate kinase
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phosphoglycerate kinase
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phosphoglycerate kinase
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phosphoglycerate kinase
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phosphoglycerate kinase
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phosphoglycerate kinase 1
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phosphoglycerate kinase 1
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phosphoglycerate kinase 1
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phosphoglycerate kinase 1
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phosphoglycerate kinase 1
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phosphoglycerate kinase 1
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phosphoglycerate kinase 2
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phosphoglycerate kinase 2
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phosphoglycerate kinase 2
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phosphoglycerate kinase 2
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phosphoglycerate kinase B
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phosphoglycerate kinase B
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SSO0527
locus name
TRSC58_02767
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
mechanism
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
mechanism
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
mechanism
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
mechanism
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
mechanism
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
mechanism
Frog
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
mechanism
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
mechanism
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
mechanism
Esox sp.
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
mechanism
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
mechanism
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
sequential mechanism
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
random sequential mechanism
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
rapid equilibrium random mechanism
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
mechanism, substrate-induced effects combine synergistically to induce major conformational changes of the active site to catalytic status
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
C-terminal part is important for full activity
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
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
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
substrate binding conformations of the 2 enzyme domains
ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
Pro204 is important for stability and catalytic mechanism of the enzyme
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
substrate binding
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
substrate binding
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
active site structure containing 2 tryptophan residues, substrate binding
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
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
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
catalytic mechanism and cycle, conformational changes for substrate binding and positioning, overview
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
an ordered mechanism is assumed where 3-phospho-D-glycerate and 3-phospho-D-glyceroyl phosphate bind before ADP and ATP, respectively
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
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 / DSM 3773
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
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
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ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate
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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
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?
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
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?
2'-dATP + 3-phospho-D-glycerate
2'-dADP + 3-phospho-D-glyceroyl phosphate
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?
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
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?
2'-dTTP + 3-phospho-D-glycerate
2'-dTDP + 3-phospho-D-glyceroyl phosphate
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?
3'-deoxy-3'-azidothymidine triphosphate + 3-phospho-D-glycerate
3'-deoxy-3'-azidothymidine diphosphate + 3-phospho-D-glyceroyl phosphate
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?
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
acyclovir triphosphate + 3-phospho-D-glycerate
acyclovir diphosphate + 3-phospho-D-glyceroyl phosphate
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?
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
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r
ATP + Beclin1
ADP + Ser30-phosphorylated Beclin1
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?
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
?
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?
D-ATP + 1,3-bisphospho-D-glycerate
?
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?
D-ATP + 3-phospho-D-glycerate
D-ADP + 3-phospho-D-glyceroyl phosphate
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?
D-CDP + 1,3-bisphospho-D-glycerate
?
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?
D-CTP + 3-phospho-D-glycerate
D-CDP + 3-phospho-D-glyceroyl phosphate
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?
D-GTP + 3-phospho-D-glycerate
D-GDP + 3-phospho-D-glyceroyl phosphate
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?
dATP + 3-phospho-D-glycerate
dADP + 1,3-diphosphoglycerate
dATP + 3-phospho-D-glycerate
dADP + 3-phospho-D-glyceroyl phosphate
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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
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?
L-2'-dCTP + 3-phospho-D-glycerate
L-2'-dCDP + 3-phospho-D-glyceroyl phosphate
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r
L-2'-dGTP + 3-phospho-D-glycerate
L-2'-dGDP + 3-phospho-D-glyceroyl phosphate
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?
L-2'-dTTP + 3-phospho-D-glycerate
L-2'-dTDP + 3-phospho-D-glyceroyl phosphate
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?
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
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?
L-ADP + 3-phospho-D-glyceroyl phosphate
ATP + 3-phospho-D-glycerate
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L-MgADP is almost as a good substrate for hPGK as the natural D-MgADP
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?
L-ATP + 1,3-bisphospho-D-glycerate
?
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?
L-ATP + 3-phospho-D-glycerate
L-ADP + 3-phospho-D-glyceroyl phosphate
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?
L-CDP + 1,3-bisphospho-D-glycerate
?
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?
L-CTP + 3-phospho-D-glycerate
L-CDP + 3-phospho-D-glyceroyl phosphate
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?
L-GTP + 3-phospho-D-glycerate
L-GDP + 3-phospho-D-glyceroyl phosphate
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?
L-UTP + 3-phospho-D-glycerate
L-UDP + 3-phospho-D-glyceroyl phosphate
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-
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?
UTP + 3-phospho-D-glycerate
UDP + 1,3-diphosphoglycerate
UTP + 3-phospho-D-glycerate
UDP + 3-phospho-D-glyceroyl phosphate
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?
additional information
?
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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
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isozyme PGK1
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?
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
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3.6fold higher activity compared to 2'-deoxycytidine
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?
2'-deoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2'-deoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
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?
2'-deoxycytidine 5'-triphosphate + 3-phospho-D-glycerate
2'-deoxycytidine 5'-diphosphate + 1,3-diphosphoglycerate
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isozyme PGK1
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?
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
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r
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
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?
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
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r
3-phospho-D-glycerate
ADP + 3-phospho-D-glyceroyl 1-phosphate
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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
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?
ADP + 1,3-bisphosphoglycerate
ATP + 3-phosphoglycerate
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r
ADP + 1,3-bisphosphoglycerate
ATP + 3-phosphoglycerate
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r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
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r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
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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
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?
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
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r
ADP + 3-phospho-D-glyceroyl 1-phosphate
ATP + 3-phospho-D-glycerate
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2.7.2.3 phosphoglycerate kinase
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