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Literature summary for 2.7.2.3 extracted from

  • Zerrad, L.; Merli, A.; Schroeder, G.F.; Varga, A.; Graczer, E.; Pernot, P.; Round, A.; Vas, M.; Bowler, M.W.
    A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinase (2011), J. Biol. Chem., 286, 14040-14048.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.2.3

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of the 3PG-HsPGK binary complex in an open conformation (HsPGK-3PG-open) are grown, and ADP and the nonhydrolyzable ATP analogue, AMP-PCP, are introduced, by soaking, to investigate the effect of their binding on the open conformation Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P00558
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-

Reaction

Reaction Comment Organism Reaction ID
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 Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + 3-phospho-D-glyceroyl phosphate
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 Homo sapiens ATP + 3-phospho-D-glycerate
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 ?

Synonyms

Synonyms Comment Organism
HsPGK
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 Homo sapiens
phosphoglycerate kinase
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 Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Homo sapiens