The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
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
AKIRA KATOMASAJI OGURAMASAMI SUDA
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1966 Volume 59 Issue 1 Pages 40-48

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Abstract
1. Serine dehydratase [EC 4. 2. 1. 13] was purified 250 fold from livers of rats fed on a high protein diet.
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.
3. Homoserine dehydratase and cysta-thionase were competitively inhibited by L-cysteine and L-cystine.
4. Regulatory mechanisms in the rat liver enzyme system converting L-methionine to L-cystine are discussed.
The authors gratefully acknowledge the excellent technical assistance given by Miss Toyoko Kawai.
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© The Japanese Biochemical Society
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