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B6db references: 87214223

type Journal Article
authors Kanzaki, H.; Nagasawa, T.; Yamada, H.
title Insight into the active site of Streptomyces cystathionine gamma-lyase based on the results of studies on its substrate specificity
journal Biochim Biophys Acta
ui 87214223
year (1987)
volume 913
number 1
pages 45-50.
keywords Allosteric Site
abstract The results of studies on the substrate specificities of elimination and replacement reactions allowed insight into the active and regulatory sites of Streptomyces phaeochromogenes cystathionine gamma- lyase (L-cystathionine cysteine-lyase (deaminating), EC The enzyme has an active site and a regulatory site. The active site consists of two subsites; one recognizes the L-forms of amino acids (L- homoserine and L-moieties of cystathionine isomers) and the other shows affinity for thiol compounds with a carboxyl group. The regulatory site is specific for L-cysteine and has no affinity for ordinary thiol compounds, such as 3-mercaptopropionate and thioglycolate.
last changed 2008/04/02 19:23

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