|
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 |
Activity |
4.4.1.1 |
Family |
4.4.1.1 |
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 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. |
last changed |
2008/04/02 19:23 |
|