UPMC Paris 06 University, UR5 EAC7180 CNRS, Physiologie Cellulaire et Moleculaire des Plantes, Case 156, 4 place Jussieu, F-75005, Paris.
Front Biosci (Landmark Ed). 2012 Jan 1;17(2):607-20. doi: 10.2741/3947.
Proline dehydrogenase (ProDH), also called proline oxidase (POX), is a universal enzyme in living organisms. It catalyzes the oxidation of L-proline to delta1-pyrroline-5-carboxylate leading to the release of electrons, which can be transferred to either electron transfer systems or to molecular oxygen. ProDH is not only essential for proline catabolism but also plays key roles in providing energy, shuttling redox potential between cellular compartments and reactive oxygen species production. Structural analysis of prokaryotic ProDHs already gives some insights into the biochemical activity and biological functions of this enzyme, which can be extended to eukaryotic ProDHs based on sequence similarities. Here we report the most recent investigations on the biochemical and regulation of ProDH at transcriptional, post-transcriptional and translational levels. The biological roles of ProDH in cell homeostasis and adaptation through energetic, developmental, adaptive, physiological and pathological processes in eukaryotes are presented and discussed to create a framework for future research direction.
脯氨酸脱氢酶（ProDH），也称为脯氨酸氧化酶（POX），是生物体内普遍存在的一种酶。它催化 L-脯氨酸氧化为 δ1-吡咯啉-5-羧酸，同时释放电子，这些电子可被转移到电子传递系统或分子氧中。ProDH 不仅对脯氨酸的分解代谢至关重要，而且在提供能量、在细胞区室之间穿梭氧化还原电势以及产生活性氧物种方面也起着关键作用。对原核 ProDH 的结构分析已经为该酶的生化活性和生物学功能提供了一些见解，这些见解可以基于序列相似性扩展到真核 ProDH。本文报道了在转录、转录后和翻译水平上对 ProDH 的生化和调控的最新研究。本文还介绍并讨论了 ProDH 在真核生物的细胞内稳态和适应中的生物学作用，这些作用涉及能量、发育、适应、生理和病理过程，为未来的研究方向提供了框架。
