D-proline reductase (dithiol) explained
| D-proline reductase (dithiol) |
| Ec Number: | 1.21.4.1 |
| Cas Number: | 37255-43-9 |
| Go Code: | 0050002 |
In enzymology, a D-proline reductase (dithiol) is an enzyme that catalyzes the chemical reaction
5-aminopentanoate + lipoate
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 . 274 - 85 . 5778643 . 10.1016/0003-9861(69)90034-4 . 1 .
- 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 . 13475375.
- 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 . 8445 - 54 . 10085076 . 10.1074/jbc.274.13.8445 . Gräntzdörffer . A . Schierhorn . A . Rücknagel . KP . Andreesen . JR . Pich . A . 13 . free .
