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. 1977 Dec;358(12):1565-72.

[Modification of arginine residues in pyruvate kinase (author's transl)]

[Article in German]
  • PMID: 590939

[Modification of arginine residues in pyruvate kinase (author's transl)]

[Article in German]
J Berghäuser. Hoppe Seylers Z Physiol Chem. 1977 Dec.

Abstract

Pyruvate kinase from pig heart is inactivated by the specific arginyl reagent phenylglyoxal. The loss of activity is caused by the reaction of a single molecule of phenylglyoxal per subunit of enzyme. During inactivation 3 - 6 arginyl residues are modified dependent on the concentration of phenylglyoxal used for modification. The solubility of the protein is reduced by the modification. ATP or phosphoenolpyruvate protect against inactivation. A single arginine is less subject to chemical modification in their presence. Therefore we assume that an arginine is essential at the substrate binding site. The activating ion K does not affectinactivation, where as Mg2 diminishes inactivation. Pyruvate kinase from rabbit muscle is modified by phenylglyoxal in a similar manner.

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