Control Mechanism in the Rat Liver Enzyme System Converting L-Methionine to L-Cystine:III. Noncompetitive Inhibition of Cystathionine Synthetase-Serine Dehydratase by Elemental Sulfur and Competitive Inhibition of Cystathionase-Homoserine Dehydratase by L-Cysteine and L-Cystine

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  • KATO AKIRA
    Department of Physiological Chemsity and Nutrition Osaka University Medical School
  • OGURA MASAJI
    Department of Physiological Chemsity and Nutrition Osaka University Medical School
  • SUDA MASAMI
    Department of Physiological Chemsity and Nutrition Osaka University Medical School

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Description

1. Serine dehydratase [EC 4. 2. 1. 13] was purified 250 fold from livers of rats fed on a high protein diet.<br> 2. Serine dehydratase activity was strongly and noncompetitively inhibited by elemental sulfur, one of the end products of the decom-position of L-cystine by cystine desulfurase.<br> 3. Homoserine dehydratase and cysta-thionase were competitively inhibited by L-cysteine and L-cystine.<br> 4. Regulatory mechanisms in the rat liver enzyme system converting L-methionine to L-cystine are discussed.<br> The authors gratefully acknowledge the excellent technical assistance given by Miss Toyoko Kawai.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 59 (1), 40-48, 1966

    The Japanese Biochemical Society

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