Insight into the active site of Streptomyces cystathionine gamma-lyase based on the results of studies on its substrate specificity.
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.
D000495:Allosteric Site; D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D003542:Cystathionine gamma-Lyase / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism*; D006714:Homoserine / Q000378:metabolism; D008190:Lyases / Q000378:metabolism*; D051381:Rats; D013237:Stereoisomerism; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity; D013438:Sulfhydryl Compounds / Q000378:metabolism
D000596:Amino Acids; D005656:Fungal Proteins; D013438:Sulfhydryl Compounds; D006714:Homoserine; D008190:Lyases; D003542:Cystathionine gamma-Lyase