IMR Press / FBL / Volume 17 / Issue 2 / DOI: 10.2741/3947

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Proline dehydrogenase: a key enzyme in controlling cellular homeostasis
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1 UPMC Paris 06 University, UR5 EAC7180 CNRS, Physiologie Cellulaire et Moleculaire des Plantes, Case 156, 4 place Jussieu, F-75005, Paris, France
2 Department of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Academic Editor:Guoyao Wu
Front. Biosci. (Landmark Ed) 2012, 17(2), 607–620;
Published: 1 January 2012
(This article belongs to the Special Issue Amino acids in nutrition, health, and disease)

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.

Proline dehydrogenase
Proline oxidase
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