Diversity, properties and functions of bacterial arginases

The metalloenzyme arginase hydrolyzes l-arginine to produce l-ornithine and urea. In bacteria, arginase has important functions in basic nitrogen metabolism and redistribution, production of the key metabolic precursor l-ornithine, stress resistance and pathogenesis. We describe the regulation and specific functions of the arginase pathway as well as summarize key characteristics of related arginine catabolic pathways. The use of arginase-derived ornithine as a precursor molecule is reviewed. We discuss the biochemical and transcriptional regulation of arginine metabolism, including arginase, with the latter topic focusing on the RocR and AhrC transcriptional regulators in the model organism Bacillus subtilis. Finally, we consider similarities and contrasts in the structure and catalytic mechanism of the arginases from Bacillus caldovelox and Helicobacter pylori. The overall aim of this review is to provide a panorama of the diversity of physiological functions, regulation and biochemical features of arginases in a variety of bacterial species.

Automated summary

Arginase in bacteria plays crucial roles in nitrogen metabolism, stress resistance, and pathogenesis by hydrolyzing l-arginine to produce l-ornithine and urea. This review explores the regulation and functions of the arginase pathway, along with characteristics of related arginine catabolic pathways, emphasizing on the diverse physiological functions and biochemical features of arginases in different bacterial species.