ID   1.21.4.1
DE   D-proline reductase.
CA   5-aminopentanoate + [PrdC protein]-Se-L-selenocysteinyl-S-L-cysteine =
CA   [PrdC protein]-L-selenocysteine/L-cysteine + D-proline.
CC   -!- A pyruvoyl- and L-selenocysteine-containing enzyme found in a number
CC       of Clostridial species.
CC   -!- The pyruvoyl group, located on the PrdA subunit, binds the substrate,
CC       while the selenocysteine residue, located on the PrdB subunit,
CC       attacks the alpha-C-atom of D-proline, leading to a reductive
CC       cleavage of the C-N-bond of the pyrrolidine ring and formation of a
CC       selenoether.
CC   -!- The selenoether is cleaved by a cysteine residue of PrdB, resulting
CC       in a mixed selenide-sulfide bridge, which is restored to its reduced
CC       state by another selenocysteine protein, PrdC.
CC   -!- 5-aminopentanoate is released from PrdA by hydrolysis, regenerating
CC       the pyruvoyl moiety.
CC   -!- The resulting mixed selenide-sulfide bridge in PrdC is reduced by
CC       NADH.
CC   -!- Formerly EC 1.4.1.6 and EC 1.4.4.1.
DR   Q9Z4P6, PRDA_ACESD ;  Q9Z4Q7, PRDB_ACESD ;
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