Muscle and liver pyruvate kinases are closely related: amino acid sequence comparisons

FEBS Letters

Fothergill, Linda A.¹  Schmitt, Wilfried³  Byford, Michael F.²  Hoar, Colin G.¹  Schiltz, Emile³  Dunbar, Bryan¹  Nicoll, Gordon W.¹  Bloxham, David P.² 

[1] Department of Biochemistry, University of Aberdeen, Marishal College, Aberdeen AB9 1AS, Scotland;Department of Biochemistry, University of Southampton, Southampton SO9 3TU, England;Institut für Organische Chemie und Biochemie, Albert-Ludwigs Universität, 7800 Freiburg, FRG

关键词: Pyruvate kinase;    M1isozyme;    L isozyme;    Phosphorylation;    Amino acid sequence;   

DOI  :  10.1016/0014-5793(84)80507-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Previous evidence has shown that the M₁ and L pyruvate kinase isozymes differ markedly in kinetic and immunological properties, amino acid compositions and peptide maps. However, the amino acid sequence results we present here for the N-terminal region and for a region of the C domain show that the M₁ and L isozymes are very similar. The variable length of the N-terminal sequences also explains the difference in regulation by phosphorylation between the M₁ and L isozymes. The M₁ isozyme lacks the serine residue that has been shown to be phosphorylated in the L isozyme.

【 授权许可】

Unknown