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

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  • 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

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Description

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.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 48 (3), 412-420, 1960

    The Japanese Biochemical Society

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