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ENZYME

ENZYME entry: EC 1.21.4.1

PURL: https://purl.expasy.org/enzyme/EC/1.21.4.1
Accepted Name
D-proline reductase
Reaction catalysed
[PrdC protein]-Se-L-selenocysteinyl-S-L-cysteine + 5-aminopentanoate = [PrdC protein]-L-selenocysteine/L-cysteine + D-proline
Comment(s)
  • 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 1.4.1.6 and EC 1.4.4.1.
Cross-references
BRENDA1.21.4.1
EC2PDB1.21.4.1
ExplorEnz1.21.4.1
KEGG Ligand Database for Enzyme Nomenclature1.21.4.1
IUBMB Enzyme Nomenclature1.21.4.1
MEDLINEFind literature relating to 1.21.4.1
MetaCyc1.21.4.1
Rhea expert-curated reactions1.21.4.1
UniProtKB/Swiss-Prot
Q9Z4P6, PRDA_ACESDQ9Z4Q7, PRDB_ACESD

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