Using Difference Infrared Spectroscopy to Investigate the Effects of pH on PGK-Substrate Complexes

Autor:	Gina MacDonald, Adam E. Colbert
Rok vydání:	2009
Předmět:	chemistry.chemical_classification Phosphoglycerate kinase Chemistry Biophysics Infrared spectroscopy Substrate (chemistry) Phosphate musculoskeletal system Yeast Catalysis chemistry.chemical_compound Crystallography Enzyme Ternary operation tissues
Zdroj:	Biophysical Journal. 96(3)
ISSN:	0006-3495
DOI:	10.1016/j.bpj.2008.12.1560
Popis:	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.
Databáze:	OpenAIRE
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