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

Hiroshi Kanzaki, Toru Nagasawa, Hideaki Yamada

Research output: Contribution to journalArticle

4 Citations (Scopus)

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 γ-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 animo 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.

Original languageEnglish
Pages (from-to)45-50
Number of pages6
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume913
Issue number1
DOIs
Publication statusPublished - May 27 1987
Externally publishedYes

Keywords

  • (S. phaeochromogenes)
  • Cystathionine γ-lyase
  • Elimination reaction
  • Pyridoxal phosphate enzyme
  • Replacement reaction
  • Substrate specificity

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

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