Proline dehydrogenase

In enzymology, a proline dehydrogenase (, formerly ) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are L-proline and ubiquinone, whereas its two products are (S)-1-pyrroline-5-carboxylate and ubiquinol.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with a quinone or similar compounds as acceptors. The systematic name of this enzyme class is L-proline:quinone oxidoreductase. Other names in common use include L-proline dehydrogenase, and L-proline:(acceptor) oxidoreductase. This enzyme participates in arginine and proline metabolism. It employs one cofactor, FAD.
Structural studies.
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , and .