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 language | English |
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Pages (from-to) | 45-50 |
Number of pages | 6 |
Journal | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular |
Volume | 913 |
Issue number | 1 |
DOIs | |
Publication status | Published - May 27 1987 |
Externally published | Yes |
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