Programa de Genómica Funcional de Procariotes, Centro de Ciencias Genómicas-Universidad Nacional Autónoma de México (CCG-UNAM), Cuernavaca, Morelos, C.P. 62210, Mexico.
FEMS Microbiol Rev. 2021 Nov 23;45(6). doi: 10.1093/femsre/fuab034.
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.
金属酶精氨酸酶将 l-精氨酸水解为 l-鸟氨酸和尿素。在细菌中,精氨酸酶在基础氮代谢和重新分配、关键代谢前体 l-鸟氨酸的产生、应激抗性和发病机制方面具有重要功能。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。还回顾了精氨酸酶衍生的鸟氨酸作为前体分子的用途。我们讨论了包括精氨酸酶在内的精氨酸代谢的生化和转录调节,后者的主题侧重于模式生物枯草芽孢杆菌中的 RocR 和 AhrC 转录调节剂。最后,我们考虑了巴氏芽孢杆菌和幽门螺杆菌精氨酸酶的结构和催化机制的相似性和对比。本综述的总体目标是提供各种细菌中精氨酸酶的生理功能、调节和生化特征的多样性全景。