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Information on EC - D-proline reductase

for references in articles please use BRENDA:EC1.21.4.1
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IUBMB 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 alpha-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.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
a [PrdC protein with a selenide-sulfide bridge]
a [PrdC protein with thiol/selenol residues]
5-aminopentanoate:lipoate oxidoreductase (cyclizing), D-proline reductase, D-proline reductase (dithiol), EC, EC, lipoate-linked proline reductase, PrdB, more
5-aminopentanoate + a [PrdC protein with a selenide-sulfide bridge] = D-proline + a [PrdC protein with thiol/selenol residues]
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