Substrate-assisted movement of the catalytic Lys 215 during domain closure: site-directed mutagenesis studies of human 3-phosphoglycerate kinase.
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A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinaseConformational dynamics in phosphoglycerate kinase, an open and shut case?Molecular basis for the lack of enantioselectivity of human 3-phosphoglycerate kinaseNucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analoguesAn allosteric signaling pathway of human 3-phosphoglycerate kinase from force distribution analysisTerazosin activates Pgk1 and Hsp90 to promote stress resistanceStructural and kinetic studies of induced fit in xylulose kinase from Escherichia coli.Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase.Thermodynamic analysis of substrate induced domain closure of 3-phosphoglycerate kinase.Role of side-chains in the operation of the main molecular hinge of 3-phosphoglycerate kinase.
P2860
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P2860
Substrate-assisted movement of the catalytic Lys 215 during domain closure: site-directed mutagenesis studies of human 3-phosphoglycerate kinase.
description
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name
Substrate-assisted movement of ...... man 3-phosphoglycerate kinase.
@en
Substrate-assisted movement of ...... man 3-phosphoglycerate kinase.
@nl
type
label
Substrate-assisted movement of ...... man 3-phosphoglycerate kinase.
@en
Substrate-assisted movement of ...... man 3-phosphoglycerate kinase.
@nl
prefLabel
Substrate-assisted movement of ...... man 3-phosphoglycerate kinase.
@en
Substrate-assisted movement of ...... man 3-phosphoglycerate kinase.
@nl
P2093
P356
P1433
P1476
Substrate-assisted movement of ...... uman 3-phosphoglycerate kinase
@en
P2093
Andrea Varga
Beáta Flachner
István Hajdú
Judit Szabó
László Barna
Péter Závodszky
P304
16853-16865
P356
10.1021/BI051726G
P407
P577
2005-12-01T00:00:00Z