Abstract

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.

中文翻译：

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细菌精氨酸酶的多样性、性质和功能

摘要

金属酶精氨酸酶水解 L-精氨酸以产生 L-鸟氨酸和尿素。在细菌中，精氨酸酶在基本的氮代谢和再分配、关键代谢前体 L-鸟氨酸的产生、抗逆性和发病机制中具有重要作用。我们描述了精氨酸酶途径的调节和特定功能，并总结了相关精氨酸分解代谢途径的关键特征。回顾了使用精氨酸酶衍生的鸟氨酸作为前体分子。我们讨论精氨酸代谢的生化和转录调控，包括精氨酸酶，后者的主题集中在模式生物枯草芽孢杆菌中的 RocR 和 AhrC 转录调控因子. 最后，我们考虑了来自Bacillus caldovelox和Helicobacter pylori的精氨酸酶的结构和催化机制的相似性和对比。本综述的总体目的是提供各种细菌物种中精氨酸酶的生理功能、调节和生化特征多样性的全景图。