Abstract
Yeast phosphoglycerate kinase catalyzes the reversible phosphate transfer in the reaction: ADP +1,3-bis-phosphoglycerate ↔ ATP + 3-phosphoglycerate. Prior research indicates a hinge-bending mechanism occurs during catalysis to bring the substrates into closer proximity. Domain closure is only initiated in ternary complexes, in which both substrates are simultaneously bound to the enzyme. The activity and conformation of PGK is directly influenced by substrate and salt concentrations as well as pH.
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