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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...

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PMID: 16430212
DOI: 10.1021/bi051591e

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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