D-proline reductase (dithiol)

D-proline reductase (dithiol)
D-proline reductase (dithiol)
Identifiers
EC number 1.21.4.1
CAS number 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 / EGO

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

5-aminopentanoate + lipoate \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 and 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. 
  • 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. 
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