METABOLISM OF L-LYSINE BY BACTERIAL ENZYMES:IV. δ-AMINOVALERIC ACID-GLUTAMIC ACID TRANSAMINASE

  • ICHIHARA AKIRA
    Department of Physiological Chemistry, Medical School, Institute for Protein Research, Osaka University
  • ICHIHARA ELIZABETH A.
    Department of Physiological Chemistry, Medical School, Institute for Protein Research, Osaka University
  • SUDA MASAMI
    Department of Physiological Chemistry, Medical School, Institute for Protein Research, Osaka University

この論文をさがす

説明

1. δ-Aminovaleric acid-glutamic acid transaminase was isolated from Pseudomonas and purified.<br> 2. This enzyme catalyzes the following reaction:<br> δ-aminovaleric acid+α-ketoglutaric acid_??_glutaric semialdehyde+L-glutamic acid<br> Substrate specificity was restricted to α-aminovaleric acid and α-ketoglutaric acid. None of the several amino acids nor pyruvic acid tested were inactive. Glutaric semialdehyde was identified as the product of the forward reaction and δ-aminovaleric acid as that of the reverse reaction.<br> The authors wish to thank Drs. S. Akabori and T. Okuda of this Institute for generous supply of glutaric semialdehyde ethylester.

収録刊行物

詳細情報 詳細情報について

問題の指摘

ページトップへ