D-proline reductase (dithiol)

In enzymology, a D-proline reductase (dithiol) (EC 1.21.4.1) is an enzyme that catalyzes the chemical reaction

5-aminopentanoate + lipoate ${\displaystyle \rightleftharpoons }$ D-proline + dihydrolipoate

Thus, the two substrates of this enzyme are 5-aminopentanoate and lipoate, whereas its two products are D-proline and dihydrolipoate.

This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with a disulfide as acceptor. The systematic name of this enzyme class is 5-aminopentanoate:lipoate oxidoreductase (cyclizing). This enzyme participates in arginine and proline metabolism. It employs one cofactor, pyruvate.

References

• Hodgins DS, Abeles RH (1969). "Studies of the mechanism of action of D-proline reductase: the presence on covalently bound pyruvate and its role in the catalytic process". Arch. Biochem. Biophys. 130 (1): 274–85. doi:10.1016/0003-9861(69)90034-4. PMID 5778643.
• Stadtman TC, Elliott P (1957). "Studies on the enzymic reduction of amino acids. II. Purification and properties of a D-proline reductase and a proline racemase from Clostridium sticklandii". J. Biol. Chem. 228: 983–997. PMID 13475375.
• JR, Pich A; Gräntzdörffer, A; Schierhorn, A; Rücknagel, KP; Andreesen, JR; Pich, A (1999). "Identification of D-proline reductase from Clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein". J. Biol. Chem. 274 (13): 8445–54. doi:10.1074/jbc.274.13.8445. PMID 10085076.

This page was last edited on 26 August 2023, at 13:43