Format

Send to

Choose Destination
Biochemistry. 2013 Jan 8;52(1):1-3. doi: 10.1021/bi301628k. Epub 2012 Dec 24.

Distinguishing the chemical moiety of phosphoenolpyruvate that contributes to allostery in muscle pyruvate kinase.

Author information

1
Department of Biochemistry and Molecular Biology, The University of Kansas Medical Center, Kansas City, KS 66160, USA.

Abstract

A series of substrate analogues has been used to determine which chemical moieties of the substrate phosphoenolpyruvate (PEP) contribute to the allosteric inhibition of rabbit muscle pyruvate kinase by phenylalanine. Replacing the carboxyl group of the substrate with a methyl alcohol or removing the phosphate altogether greatly reduces substrate affinity. However, removal of the carboxyl group is the only modification tested that removes the ability to allosterically reduce the level of Phe binding. From this, it can be concluded that the carboxyl group of PEP is responsible for energetic coupling with Phe binding in the allosteric sites.

PMID:
23256782
PMCID:
PMC3548419
DOI:
10.1021/bi301628k
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for American Chemical Society Icon for PubMed Central
Loading ...
Support Center