D-proline reductase (dithiol)

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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.

[edit] References

IUBMB entry for 1.21.4.1
BRENDA references for 1.21.4.1 (Recommended.)
PubMed references for 1.21.4.1
PubMed Central references for 1.21.4.1
Google Scholar references for 1.21.4.1
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. 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 (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. doi:10.1074/jbc.274.13.8445. PMID 10085076.