| Comments |
A pyruvoyl- and L-selenocysteine-containing enzyme found in a number of Clostridial species. The pyruvoyl group, located on the PrdA subunit, binds the substrate, while the selenocysteine residue, located on the PrdB subunit, attacks the ¦Á-C-atom of D-proline, leading to a reductive cleavage of the C-N-bond of the pyrrolidine ring and formation of a selenoether. The selenoether is cleaved by a cysteine residue of PrdB, resulting in a mixed selenide-sulfide bridge, which is restored to its reduced state by another selenocysteine protein, PrdC. 5-aminopentanoate is released from PrdA by hydrolysis, regenerating the pyruvoyl moiety. The resulting mixed selenide-sulfide bridge in PrdC is reduced by NADH. Formerly EC 1.4.1.6 and EC 1.4.4.1. |
