ENZYME entry: EC 220.127.116.11
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|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
- 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
- Formerly EC 18.104.22.168 and EC 22.214.171.124.
|PRIAM enzyme-specific profiles||126.96.36.199|
|KEGG Ligand Database for Enzyme Nomenclature||188.8.131.52|
|IUBMB Enzyme Nomenclature||184.108.40.206|
|MEDLINE||Find literature relating to 220.127.116.11|
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.-.-.-