D-proline reductase (dithiol)
| D-proline reductase (dithiol) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.21.4.1 | ||||||||
| CAS no. | 37255-43-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a D-proline reductase (dithiol) (EC 1.21.4.1) 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 (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.
