Distinguishing the chemical moiety of phosphoenolpyruvate that contributes to allostery in muscle pyruvate kinase.
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ABSTRACT:
SUBMITTER: Urness JM
PROVIDER: S-EPMC3548419 | biostudies-literature | 2013 Jan
REPOSITORIES: biostudies-literature
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Distinguishing the chemical moiety of phosphoenolpyruvate that contributes to allostery in muscle pyruvate kinase.
Urness James M JM Clapp Kelly M KM Timmons J Cody JC Bai Xinyan X Chandrasoma Nalin N Buszek Keith R KR Fenton Aron W AW
Biochemistry 20121224 1
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 bind ...[more]
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