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Insight into the active site of Streptomyces cystathionine gamma-lyase based on the results of studies on its substrate specificity.

作者信息

Kanzaki H, Nagasawa T, Yamada H

出版信息

Biochim Biophys Acta. 1987 May 27;913(1):45-50. doi: 10.1016/0167-4838(87)90230-5.

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 4.4.1.1). 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.

摘要

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