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EC 1.21.4.1 Details

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EC number

1.21.4.1

Accepted name

D-proline reductase

Reaction

5-aminopentanoate + a [PrdC protein with a selenide-sulfide bridge] = D-proline + a [PrdC protein with thiol/selenol residues]

Other name(s)

prdAB (gene names), D-proline reductase (dithiol)

Systematic name

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

CAS registry number

37255-43-9

Comment

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 α-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.

History

created 1972 as EC 1.4.4.1, modified 1982 (EC 1.4.1.6 created 1961, incorporated 1982), transferred 2003 to EC 1.21.4.1, modified 2018

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.12.1 With NAD⁺ or NADP⁺ as acceptor

1.12.2 With a cytochrome as acceptor

1.12.5 With a quinone or similar compound as acceptor

1.12.7 With an iron-sulfur protein as acceptor

1.12.98 With other, known, physiological acceptors

1.12.99 With unknown physiological acceptors

1.12.99.1 created 1989, deleted 2002

1.12.99.2 created 1992, deleted 2002

1.12.99.3 created 1999, deleted 2002

1.12.99.4 created 1999, deleted 2002

1.12.99.5 created 1999, deleted 2001

1.12.99.6 hydrogenase (acceptor)

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.13.1. undefined

1.13.11 With incorporation of two atoms of oxygen

1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)

1.13.99 Miscellaneous

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

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

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.4.1 D-proline reductase

1.21.4.2 glycine reductase

1.21.4.3 sarcosine reductase

1.21.4.4 betaine reductase

1.21.4.5 tetrachlorohydroquinone reductive dehalogenase

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

2 Transferases

2.1 Transferring one-carbon groups

2.2 Transferring aldehyde or ketonic groups

2.3 Acyltransferases

2.4 Glycosyltransferases

2.5 Transferring alkyl or aryl groups, other than methyl groups

2.6 Transferring nitrogenous groups

2.7 Transferring phosphorus-containing groups

2.8 Transferring sulfur-containing groups

2.9 Transferring selenium-containing groups

2.10 Transferring molybdenum- or tungsten-containing groups