Proline_dehydrogenase
In enzymology, proline dehydrogenase (PRODH) (EC 1.5.5.2, formerly EC 1.5.99.8) is an enzyme of the oxidoreductase family, active in the oxidation of L-proline to (S)-1-pyrroline-5-carboxylate during proline catabolism. The end product of this reaction is then further oxidized in a (S)-1-pyrroline-5-carboxylate dehydrogenase (P5CDH)-dependent reaction of the proline metabolism, or spent to produce ornithine, a crucial metabolite of ornithine and arginine metabolism. The systematic name of this enzyme class is L-proline:quinone oxidoreductase. Other names in common use include L-proline dehydrogenase, L-proline oxidase,and L-proline:(acceptor) oxidoreductase. It employs one cofactor, FAD, which requires riboflavin (vitamin B2).
Proline dehydrogenase is in humans encoded by PRODH[1] and PRODH2[2] genes, located on the chromosomes 22 and 19, respectively. Their mutations lead to hyperprolinemia, manifested by increased proline levels in blood and urine. The deficiency of PRODH has also been linked to the susceptibility to schizophrenia-4.[citation needed]