Correlation Engine 2.0
Clear Search sequence regions


Sizes of these terms reflect their relevance to your search.

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.

Citation

James M Urness, Kelly M Clapp, J Cody Timmons, Xinyan Bai, Nalin Chandrasoma, Keith R Buszek, Aron W Fenton. Distinguishing the chemical moiety of phosphoenolpyruvate that contributes to allostery in muscle pyruvate kinase. Biochemistry. 2013 Jan 8;52(1):1-3

Expand section icon Mesh Tags

Expand section icon Substances


PMID: 23256782

View Full Text