Characterization and structural basis of D-cysteine desulfhydrase from Pectobacterium atrosepticum. (9th January 2023)

• Record Type: Journal Article
• Authors: Xu, Xuexia; Yang, Linsong; Zhang, Xianfang; Xing, Xiwen; Zhou, Jiahai
• Is Part Of: Tetrahedron. Volume 130(2023)
• Publication Date: 2023-01-09
• Subjects: Chemistry, Organic -- Periodicals; 547.005
• DOI: 10.1016/j.tet.2022.133174
• Languages: English
• ISSNs: 0040-4020

Abstract

Abstract: d -cysteine desulfhydrase belongs to the family of lyases and participates in cysteine metabolism. Here we report the identification and crystal structures of D-cysteine desulfhydrase from Pectobacterium atrosepticum . The pyruvate-bound complex structure reveals a geminal diamine intermediate trapped in the active site and enables us to build the enzyme-substrate interaction model by molecule docking. Site-directed mutagenesis on R221 or Y264, one of the two critical residues in substrate binding pocket, results in mutants with enhanced enzyme activity toward D-cysteine carbon-sulfur lysis.