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Metabolic regulation of glycolysis in sea bass (Dicentrarchus labrax L.) muscle. I. Kinetic study and characteristic modulators of pyruvate kinase.

作者信息

Fideu M D, Maroto M L, Serradilla M C, Pérez M L, Herranz M J, Ruiz-Amil M

机构信息

Departamento de Bioquímica, Facultad de Veterinaria, Universidad Complutense, Madrid.

出版信息

Rev Esp Fisiol. 1988 Dec;44(4):381-6.

PMID:3244885
Abstract

White muscle pyruvate kinase from sea bass presents positive cooperativity with respect to PEP substrate. The enzyme is regulated by F-1.6-P2 and L-Phenylalanine. The activator effect of F-1.6-P2 in experiments carried out for the substrate PEP with crude extract seems to indicate that the enzyme is activated in vivo by this compound. The enzyme was not inhibited by either alanine or ATP but was inhibited by L-phenylalanine. Therefore this enzyme presents kinetic and regulatory properties similar to those of the mammalian isozyme M2.

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