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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 1.21.4.1

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]
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
PRIAM enzyme-specific profiles1.21.4.1
KEGG Ligand Database for Enzyme Nomenclature1.21.4.1
IUBMB Enzyme Nomenclature1.21.4.1
IntEnz1.21.4.1
MEDLINEFind literature relating to 1.21.4.1
MetaCyc1.21.4.1
UniProtKB/Swiss-Prot
Q9Z4P6, PRDA_ACESD;  Q9Z4Q7, PRDB_ACESD;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.21.4.-
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