Change in kinetic property of M1-type pyruvate kinase from hyperbolic type to sigmoidal type by limited proteolysis with an acid fraction from rabbit liver.
An acid extract of rabbit liver contained M1-type pyruvate kinase inactivating activity, and was separated to three fractions. The optimal inactivation of the enzyme with Fraction II (Mr 42,000) was observed at pH 5.5, and this inactivation was completely prevented by leupeptin and antipain, but not by pepstatin. With Fraction III (Mr 22,000), on the other hand, optimal inactivation of the enzyme was observed at pH 8-9, and was not prevented by these inhibitors. The kinetic properties, with phosphoenolpyruvate, of the enzyme were changed from hyperbolic type to sigmoidal type by the limited proteolysis with Fractions II and III. The subunit molecular weight of the enzyme (57,300) was decreased to 55,800 via 56,400 in the former case and to 56,400 in the latter case.
D000818:Animals; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D011770:Pyruvate Kinase / Q000378:metabolism*; D011817:Rabbits
D007527:Isoenzymes; D010446:Peptide Fragments; D011480:Protease Inhibitors; D011770:Pyruvate Kinase; D010447:Peptide Hydrolases