Photoinduced Covalent Irreversible Inactivation of Proline Dehydrogenase by S-Heterocycles

2021 ◽  
Author(s):  
Ashley C. Campbell ◽  
Austin R. Prater ◽  
Alexandra N. Bogner ◽  
Thomas P. Quinn ◽  
Kent S. Gates ◽  
...  
Keyword(s):  
Proline Dehydrogenase

scholarly journals Collagen metabolism as a regulator of proline dehydrogenase/proline oxidase-dependent apoptosis/autophagy

Amino Acids ◽  
2021 ◽  
Author(s):  
Jerzy Palka ◽  
Ilona Oscilowska ◽  
Lukasz Szoka
Keyword(s):  
Cell Metabolism ◽  
Underlying Mechanism ◽  
Collagen Biosynthesis ◽  
Proline Metabolism ◽  
Proline Dehydrogenase ◽  
Histone Demethylases ◽  
Proline Oxidase ◽  
Prolyl Hydroxylases ◽  
Transport Chain ◽  
And Control

AbstractRecent studies on the regulatory role of amino acids in cell metabolism have focused on the functional significance of proline degradation. The process is catalysed by proline dehydrogenase/proline oxidase (PRODH/POX), a mitochondrial flavin-dependent enzyme converting proline into ∆1-pyrroline-5-carboxylate (P5C). During this process, electrons are transferred to electron transport chain producing ATP for survival or they directly reduce oxygen, producing reactive oxygen species (ROS) inducing apoptosis/autophagy. However, the mechanism for switching survival/apoptosis mode is unknown. Although PRODH/POX activity and energetic metabolism were suggested as an underlying mechanism for the survival/apoptosis switch, proline availability for this enzyme is also important. Proline availability is regulated by prolidase (proline supporting enzyme), collagen biosynthesis (proline utilizing process) and proline synthesis from glutamine, glutamate, α-ketoglutarate (α-KG) and ornithine. Proline availability is dependent on the rate of glycolysis, TCA and urea cycles, proline metabolism, collagen biosynthesis and its degradation. It is well established that proline synthesis enzymes, P5C synthetase and P5C reductase as well as collagen prolyl hydroxylases are up-regulated in most of cancer types and control rates of collagen biosynthesis. Up-regulation of collagen prolyl hydroxylase and its exhaustion of ascorbate and α-KG may compete with DNA and histone demethylases (that require the same cofactors) to influence metabolic epigenetics. This knowledge led us to hypothesize that up-regulation of prolidase and PRODH/POX with inhibition of collagen biosynthesis may represent potential pharmacotherapeutic approach to induce apoptosis or autophagic death in cancer cells. These aspects of proline metabolism are discussed in the review as an approach to understand complex regulatory mechanisms driving PRODH/POX-dependent apoptosis/survival.

No evidence for an association between variants at the proline dehydrogenase locus and schizophrenia or bipolar affective disorder

2005 ◽  
Vol 15 (3) ◽  
pp. 195-198 ◽  
Author(s):  
Rami Abou Jamra ◽  
Johannes Schumacher ◽  
Tim Becker ◽  
Faten Dahdouh ◽  
Stephanie Ohlraun ◽  
...  
Keyword(s):  
Affective Disorder ◽  
Bipolar Affective Disorder ◽  
Proline Dehydrogenase

scholarly journals Dye-linked d-Proline Dehydrogenase from Hyperthermophilic ArchaeonPyrobaculum islandicumIs a Novel FAD-dependent Amino Acid Dehydrogenase

2002 ◽  
Vol 277 (15) ◽  
pp. 12861-12867 ◽  
Author(s):  
Takenori Satomura ◽  
Ryushi Kawakami ◽  
Haruhiko Sakuraba ◽  
Toshihisa Ohshima
Keyword(s):  
Amino Acid ◽  
Proline Dehydrogenase ◽  
Acid Dehydrogenase ◽  
Amino Acid Dehydrogenase

scholarly journals A Conserved Active Site Tyrosine Residue of Proline Dehydrogenase Helps Enforce the Preference for Proline over Hydroxyproline as the Substrate†‡

Biochemistry ◽  
2009 ◽  
Vol 48 (5) ◽  
pp. 951-959 ◽  
Author(s):  
Elizabeth L. Ostrander ◽  
John D. Larson ◽  
Jonathan P. Schuermann ◽  
John J. Tanner
Keyword(s):  
Active Site ◽  
Tyrosine Residue ◽  
Proline Dehydrogenase ◽  
Active Site Tyrosine
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