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 |
|---|---|
| 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
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Cite this
Kanzaki, H., Nagasawa, T., & Yamada, H. (1987). Insight into the active site of Streptomyces cystathionine γ-lyase based on the results of studies on its substrate specificity. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 913(1), 45-50. https://doi.org/10.1016/0167-4838(87)90230-5