Muscle and liver pyruvate kinases are closely related: amino acid sequence comparisons.
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.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002415:Cats; D003461:Crystallography; D007527:Isoenzymes / Q000032:analysis*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D009132:Muscles / Q000201:enzymology*; D011770:Pyruvate Kinase / Q000032:analysis*; D051381:Rats
D000596:Amino Acids; D007527:Isoenzymes; D046911:Macromolecular Substances; D011770:Pyruvate Kinase