PRODH2:FAD dimer dehydrogenates HPRO to 1-pyrroline-3-hydroxy-5-carboxylate

Stable Identifier
Reaction [transition]
Homo sapiens
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PRODH2 dimer dehydrogenates hydroxyproline (HPRO) to form 1-pyrroline-3-hydroxy-5-carboxylate (Adams & Goldstone 1960). The enzyme is associated with FAD and ubiquinone (not annotated here) is the likely electron acceptor (Summitt et al. 2015). The mitochondrial localization of the reaction is inferred from studies of HPRO catabolism in rat and bovine systems (Adams & Frank 1980), and the localization of PRODH2 to the inner mitochondrial membrane is inferred from that of the homologous mouse protein (Da Cruz et al. 2003).

Literature References
PubMed ID Title Journal Year
13681368 Hydroxyproline metabolism. II. Enzymatic preparation and properties of Delta 1-pyrroline-3-hydroxy-5-carboxylic acid

Adams, E, Goldstone, A

J. Biol. Chem. 1960
12865426 Proteomic analysis of the mouse liver mitochondrial inner membrane

Da Cruz, S, Xenarios, I, Langridge, J, Vilbois, F, Parone, PA, Martinou, JC

J. Biol. Chem. 2003
6250440 Metabolism of proline and the hydroxyprolines

Adams, E, Frank, L

Annu Rev Biochem 1980
25697095 Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria

Summitt, CB, Johnson, LC, J├Ânsson, TJ, Parsonage, D, Holmes, RP, Lowther, WT

Biochem. J. 2015
Participant Of
Event Information
Catalyst Activity
Catalyst Activity
proline dehydrogenase activity of PRODH2 dimer [mitochondrial inner membrane]
Physical Entity
Orthologous Events
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