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

Urness, James M; Clapp, Kelly M; Timmons, J Cody; Bai, Xinyan; Chandrasoma, Nalin; Buszek, Keith R; Fenton, Aron W

Urness, James M; Clapp, Kelly M; Timmons, J Cody; Bai, Xinyan; Chandrasoma, Nalin; Buszek, Keith R; Fenton, Aron W.

Affiliation

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

Biochemistry ; 52(1): 1-3, 2013 Jan 08.

Article in En | MEDLINE | ID: mdl-23256782

Subject(s)

Muscles/enzymology; Phenylalanine/metabolism; Phosphoenolpyruvate/chemistry; Phosphoenolpyruvate/metabolism; Pyruvate Kinase/metabolism; Allosteric Regulation; Allosteric Site; Animals; Muscles/chemistry; Phosphoenolpyruvate/analogs & derivatives; Protein Binding; Pyruvate Kinase/chemistry; Rabbits; Substrate Specificity

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Full text: 1 Database: MEDLINE Main subject: Phosphoenolpyruvate / Phenylalanine / Pyruvate Kinase / Muscles Limits: Animals Language: En Year: 2013 Type: Article

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Full text: 1 Database: MEDLINE Main subject: Phosphoenolpyruvate / Phenylalanine / Pyruvate Kinase / Muscles Limits: Animals Language: En Year: 2013 Type: Article