The stereochemical course of the reaction catalyzed by creatine kinase.
The Journal of biological chemistry
confidence
Key findings
Enzymatic study of creatine kinase stereochemistry; no clinical or biological endpoints reported.
View source on PubMed (PMID 7240185) ↗
- Population
- In vitro enzymatic reaction (creatine kinase)
- Blinding
- not_reported
- Controls
- none
- Drug class
- nootropic
Full abstract
Adenosine [gamma-(S)-16O, 17O, 18O]triphosphate has been used as a substrate in the reaction catalyzed by creatine kinase, and the configuration at phosphorus in the product [16O, 17O, 18O]phosphocreatine has been determined. The reaction proceeds with inversion of the configuration, consistent with the emerging pattern of behavior among the phosphokinases. This result, coupled with recently published data from NMR, ESR, and infrared studies of ternary and quaternary complexes od creatine kinase with its substrates and inhibitors, defines the enzyme-catalyzed transphosphorylation as an associative in-line transfer of the phosphoryl group between the bound substrates.