The reaction is observed only in the direction of D-proline reduction. Other dithiols can function as reducing agents; the enzyme contains a pyruvoyl group and a selenocysteine residue, both essential for activity.
Hodgins, D.S. and Abeles, R.H. 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 (1969) 274–285. [PMID: 5778643]
Stadtman, T.C. and Elliott, P. 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 (1957) 983–997. [PMID: 13475375]
Kabisch, U.C., Gräntzdörffer, A., Schierhorn, A., Rücknagel, K.P, Andreesen, J.R. and Pich, A. 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 (1999) 8445–8454. [PMID: 10085076]
[EC 188.8.131.52 created 1972 as EC 184.108.40.206, modified 1982 (EC 220.127.116.11 created 1961, incorporated 1982), transferred 2003 to EC 18.104.22.168]