51. Inactivation of microbial arginine deiminases by L-canavanine
- Author
-
Ling Li, Zhimin Li, Danqi Chen, Xuefeng Lu, Xiaohua Feng, Wright, Elizabeth C., Solberg, Nathan O., Dunaway-Mariano, Debra, Mariano, Patrick S., Galkin, Andrey, Kulakova, Liudmila, Herzberg, Osnat, Green-Church, Kari B., and Liwen Zhang
- Subjects
Arginine -- Chemical properties ,Catalysis -- Research ,Hydrolysis -- Research ,Pseudomonas aeruginosa -- Physiological aspects ,Chemistry - Abstract
The isolation, structure and chemical mechanism for catalysis of the Pseudomonas aeruginosa, arginine deiminase (ADI) (L-arginine) which involves initial formation and subsequent hydrolysis of a Cys-alkylthiouronium ion intermediate is described. The findings from the studies would help to design the arginine analogs such as L-canavanine that migaht react with the ADIs to form inactive covalent adduct during catalytic turnover.
- Published
- 2008