Home  |  Contact

ENZYME entry: EC

Accepted Name
D-proline reductase.
Reaction catalysed
5-aminopentanoate + a [PrdC protein with a selenide-sulfide bridge] <=> D-proline + a [PrdC protein with thiol/selenol residues]
  • 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.
  • Formerly EC and EC
PRIAM enzyme-specific profiles1.21.4.1
KEGG Ligand Database for Enzyme Nomenclature1.21.4.1
IUBMB Enzyme Nomenclature1.21.4.1
MEDLINEFind literature relating to

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.21.4.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.21.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-