1.21.4.1: D-proline reductase

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For detailed information about D-proline reductase, go to the full flat file.

Reaction

Synonyms

5-aminopentanoate:lipoate oxidoreductase (cyclizing), D-proline reductase, D-proline reductase (dithiol), EC 1.4.1.6, EC 1.4.4.1, lipoate-linked proline reductase, PrdB

ECTree

     1 Oxidoreductases

         1.21 Catalysing the reaction X-H + Y-H = X-Y

             1.21.4 With a disulfide as acceptor

                1.21.4.1 D-proline reductase

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5	Activating Compound
684	AA Sequence
1	CAS Registry Number
3	Cloned(Commentary)
2	Cofactor
2	Expression
3	General Information
2	General Stability
23	Inhibitors
6	Localization
12	Metals/Ions
11	Molecular Weight [Da]
6	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
16	Organism
6	Pathway
1	pH Optimum
1	pH Stability
10	Purification (Commentary)
1	Reaction
5	Reaction Type
16	Reference
6	Specific Activity [micromol/min/mg]
3	Storage Stability
28	Substrates and Products (Substrate)
8	Subunits
9	Synonyms
1	Systematic Name

Systematic Name

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Systematic Name on EC 1.21.4.1 - D-proline reductase

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SYSTEMATIC NAME

IUBMB Comments

5-aminopentanoate:[PrdC protein] oxidoreductase (cyclizing)

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.