Difference between revisions of "Proline dehydrogenase"
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|abbr=ProDH | |abbr=ProDH | ||
|description='''Proline dehydrogenase''' (ProDH), L-proline:quinone oxidoreductase, is located on the inner side of the [[mtIM]], oxidizing [[proline]] to delta-1-pyrroline-5-carboxylate, with reduction of FAD to FADH<sub>2</sub> and direct entry into the [[Q-junction]], exerting an additive effect of convergent pathways. ProDH is widely distributed in a variety of organisms, is a source of ROS, and may play a role in carcinogenesis. | |description='''Proline dehydrogenase''' (ProDH), L-proline:quinone oxidoreductase, is located on the inner side of the [[mtIM]], oxidizing [[proline]] to delta-1-pyrroline-5-carboxylate, with reduction of FAD to FADH<sub>2</sub> and direct entry into the [[Q-junction]], exerting an additive effect of convergent pathways. ProDH is widely distributed in a variety of organisms, is a source of ROS, and may play a role in carcinogenesis. | ||
|info=[[Teulier 2016 Proc Biol Sci]], Kononczuk et al 2015 | |info=[[Teulier 2016 Proc Biol Sci]], Kononczuk et al 2015, [[Soares 2015 PLoS One]] | ||
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|mitopedia topic=Enzyme | |mitopedia topic=Enzyme | ||
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Communicated by [[Garcia-Souza LF]] and [[Gnaiger E]] 2019-04-29 | |||
== References == | |||
:::# Kononczuk J, Czyzewska U, Moczydlowska J, Surażyński A, Palka J, Miltyk W (2015) Proline oxidase (POX) as a target for cancer therapy. Curr Drug Targets 16:1464-9. - [https://www.ncbi.nlm.nih.gov/pubmed/26553010 »PubMed 26553010«] | |||
:::# Teulier L, Weber JM, Crevier J, Darveau CA (2016) Proline as a fuel for insect flight: enhancing carbohydrate oxidation in hymenopterans. Proc Biol Sci 283: 20160333. - [[Teulier 2016 Proc Biol Sci |»Bioblast link«]] | |||
Latest revision as of 10:29, 29 April 2019
- high-resolution terminology - matching measurements at high-resolution
Proline dehydrogenase
Description
Proline dehydrogenase (ProDH), L-proline:quinone oxidoreductase, is located on the inner side of the mtIM, oxidizing proline to delta-1-pyrroline-5-carboxylate, with reduction of FAD to FADH2 and direct entry into the Q-junction, exerting an additive effect of convergent pathways. ProDH is widely distributed in a variety of organisms, is a source of ROS, and may play a role in carcinogenesis.
Abbreviation: ProDH
Reference: Teulier 2016 Proc Biol Sci, Kononczuk et al 2015, Soares 2015 PLoS One
MitoPedia topics: Enzyme
Communicated by Garcia-Souza LF and Gnaiger E 2019-04-29
References
- Kononczuk J, Czyzewska U, Moczydlowska J, Surażyński A, Palka J, Miltyk W (2015) Proline oxidase (POX) as a target for cancer therapy. Curr Drug Targets 16:1464-9. - »PubMed 26553010«
- Teulier L, Weber JM, Crevier J, Darveau CA (2016) Proline as a fuel for insect flight: enhancing carbohydrate oxidation in hymenopterans. Proc Biol Sci 283: 20160333. - »Bioblast link«
