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

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

Stable Identifier

R-HSA-6784224

Type

Reaction [transition]

Species

Homo sapiens

Compartment

mitochondrial matrix, mitochondrial inner membrane

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

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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, Jönsson, TJ, Parsonage, D, Holmes, RP, Lowther, WT	Biochem. J.	2015