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Inactivation of microbial arginine deiminases by L-canavanine

Authors :
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.
Liwen Zhang
Source :
Journal of the American Chemical Society. Feb 13, 2008, Vol. 130 Issue 6, 1918-1931
Publication Year :
2008

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.

Details

Language :
English
ISSN :
00027863
Volume :
130
Issue :
6
Database :
Gale General OneFile
Journal :
Journal of the American Chemical Society
Publication Type :
Academic Journal
Accession number :
edsgcl.176005202