Article
Kinetic analysis of Pseudomonas aeruginosa arginine deiminase mutants and alternate substrates provides insight into structural determinants of function.
Biochemistry - 31 Jan 2006
Lu Xuefeng, Li Ling, Wu Rui, Feng Xiaohua, Li Zhimin, Yang Heyi, Wang Canhui, Guo Hua, Galkin Andrey, Herzberg Osnat, Mariano Patrick S, Martin Brian M, Dunaway-Mariano Debra
Abstract excerpt
L-Arginine deiminase from Pseudomonas aeruginosa (PaADI) catalyzes the hydrolysis of arginine to citrulline and ammonia. PaADI belongs to the guanidino group-modifying enzyme superfamily (GMSF), which conserves backbone fold and a Cys-, His-, and Asp-based catalytic core. In this paper the contributions made by the PaADI core residues Cys406, His278, and Asp166 and the contribution from the neighboring Asp280...
Topics
- Binding Sites
- Catalysis
- Crystallography, X-Ray
- Evolution, Molecular
- Guanidines
- Hydrogen-Ion Concentration
- Hydrolases
- Kinetics
- Models, Molecular
- Molecular Sequence Data