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Muscle and liver pyruvate kinases are closely related: amino acid sequence comparisons
Author(s) -
Hoar Colin G.,
Nicoll Gordon W.,
Schiltz Emile,
Schmitt Wilfried,
Bloxham David P.,
Byford Michael F.,
Dunbar Bryan,
Fothergill Linda A.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80507-4
Subject(s) - isozyme , pyruvate kinase , biochemistry , pkm2 , serine , amino acid , peptide sequence , phosphorylation , biology , kinase , pyruvate dehydrogenase kinase , pyruvate dehydrogenase lipoamide kinase isozyme 1 , peptide , pyruvate dehydrogenase phosphatase , amino acid residue , sequence (biology) , chemistry , enzyme , pyruvate dehydrogenase complex , gene , glycolysis
Previous evidence has shown that the M 1 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 M 1 and L isozymes are very similar. The variable length of the N‐terminal sequences also explains the difference in regulation by phosphorylation between the M 1 and L isozymes. The M 1 isozyme lacks the serine residue that has been shown to be phosphorylated in the L isozyme.