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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

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.2 With a cytochrome as acceptor

1.1.3 With oxygen as acceptor

1.1.4 With a disulfide as acceptor

1.1.5 With a quinone or similar compound as acceptor

1.1.7 With an iron-sulfur protein as acceptor

1.1.9 With a copper protein as acceptor

1.1.98 With other, known, physiological acceptors

1.1.99 With unknown physiological acceptors

1.2 Acting on the aldehyde or oxo group of donors

1.2.1 With NAD⁺ or NADP⁺ as acceptor

1.2.1.1 created 1961, modified 1982, modified 2002, deleted 2005

1.2.1.2 formate dehydrogenase

1.2.1.3 aldehyde dehydrogenase (NAD⁺)

1.2.1.4 aldehyde dehydrogenase (NADP⁺)

1.2.1.5 aldehyde dehydrogenase [NAD(P)⁺]

1.2.1.6 created 1961, deleted 1965

1.2.1.7 benzaldehyde dehydrogenase (NADP⁺)

1.2.1.8 betaine-aldehyde dehydrogenase

1.2.1.9 glyceraldehyde-3-phosphate dehydrogenase (NADP⁺)

1.2.1.10 acetaldehyde dehydrogenase (acetylating)

1.2.1.11 aspartate-semialdehyde dehydrogenase

1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)

1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP⁺) (phosphorylating)

1.2.1.14 created 1961, deleted 1984

1.2.1.15 malonate-semialdehyde dehydrogenase

1.2.1.16 succinate-semialdehyde dehydrogenase [NAD(P)⁺]

1.2.1.17 glyoxylate dehydrogenase (acylating)

1.2.1.18 malonate-semialdehyde dehydrogenase (acetylating)

1.2.1.19 aminobutyraldehyde dehydrogenase

1.2.1.20 glutarate-semialdehyde dehydrogenase

1.2.1.21 glycolaldehyde dehydrogenase

1.2.1.22 lactaldehyde dehydrogenase

1.2.1.23 2-oxoaldehyde dehydrogenase (NAD⁺)

1.2.1.24 succinate-semialdehyde dehydrogenase (NAD⁺)

1.2.1.25 branched-chain α-keto acid dehydrogenase system

1.2.1.26 2,5-dioxovalerate dehydrogenase

1.2.1.27 methylmalonate-semialdehyde dehydrogenase (CoA-acylating)

1.2.1.28 benzaldehyde dehydrogenase (NAD⁺)

1.2.1.29 aryl-aldehyde dehydrogenase

1.2.1.30 carboxylate reductase (NADP⁺)

1.2.1.31 L-aminoadipate-semialdehyde dehydrogenase

1.2.1.32 aminomuconate-semialdehyde dehydrogenase

1.2.1.33 (R)-dehydropantoate dehydrogenase

1.2.1.34 created 1972, deleted 1983 [transferred to EC 1.1.1.180, deleted 1984]

1.2.1.35 created 1972, deleted 1984

1.2.1.36 retinal dehydrogenase

1.2.1.37 created 1972, deleted 1984

1.2.1.38 N-acetyl-γ-glutamyl-phosphate reductase

1.2.1.39 phenylacetaldehyde dehydrogenase

1.2.1.40 3α,7α,12α-trihydroxycholestan-26-al 26-oxidoreductase

1.2.1.41 glutamate-5-semialdehyde dehydrogenase

1.2.1.42 hexadecanal dehydrogenase (acylating)

1.2.1.43 formate dehydrogenase (NADP⁺)

1.2.1.44 cinnamoyl-CoA reductase

1.2.1.45 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase

1.2.1.46 formaldehyde dehydrogenase

1.2.1.47 4-trimethylammoniobutyraldehyde dehydrogenase

1.2.1.48 long-chain-aldehyde dehydrogenase

1.2.1.49 2-oxoaldehyde dehydrogenase (NADP⁺)

1.2.1.50 long-chain acyl-protein thioester reductase

1.2.1.51 pyruvate dehydrogenase (NADP⁺)

1.2.1.52 oxoglutarate dehydrogenase (NADP⁺)

1.2.1.53 4-hydroxyphenylacetaldehyde dehydrogenase

1.2.1.54 γ-guanidinobutyraldehyde dehydrogenase

1.2.1.55 created 1990, deleted 2003

1.2.1.56 created 1990, deleted 2003

1.2.1.57 butanal dehydrogenase

1.2.1.58 phenylglyoxylate dehydrogenase (acylating)

1.2.1.59 glyceraldehyde-3-phosphate dehydrogenase (NAD(P)⁺) (phosphorylating)

1.2.1.60 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase

1.2.1.61 4-hydroxymuconic-semialdehyde dehydrogenase

1.2.1.62 4-formylbenzenesulfonate dehydrogenase

1.2.1.63 6-oxohexanoate dehydrogenase

1.2.1.64 4-hydroxybenzaldehyde dehydrogenase (NAD⁺)

1.2.1.65 salicylaldehyde dehydrogenase

1.2.1.66 mycothiol-dependent formaldehyde dehydrogenase

1.2.1.67 vanillin dehydrogenase

1.2.1.68 coniferyl-aldehyde dehydrogenase

1.2.1.69 fluoroacetaldehyde dehydrogenase

1.2.1.70 glutamyl-tRNA reductase

1.2.1.71 succinylglutamate-semialdehyde dehydrogenase

1.2.1.72 erythrose-4-phosphate dehydrogenase

1.2.1.73 sulfoacetaldehyde dehydrogenase

1.2.1.74 abieta-7,13-dien-18-al dehydrogenase

1.2.1.75 malonyl-CoA reductase (malonate semialdehyde-forming)

1.2.1.76 succinate-semialdehyde dehydrogenase (acylating)

1.2.1.77 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP⁺)

1.2.1.78 2-formylbenzoate dehydrogenase

1.2.1.79 succinate-semialdehyde dehydrogenase (NADP⁺)

1.2.1.80 long-chain acyl-[acyl-carrier-protein] reductase

1.2.1.81 sulfoacetaldehyde dehydrogenase (acylating)

1.2.1.82 β-apo-4′-carotenal oxygenase

1.2.1.83 3-succinoylsemialdehyde-pyridine dehydrogenase

1.2.1.84 alcohol-forming fatty acyl-CoA reductase

1.2.1.85 2-hydroxymuconate-6-semialdehyde dehydrogenase

1.2.1.86 geranial dehydrogenase

1.2.1.87 propanal dehydrogenase (CoA-propanoylating)

1.2.1.88 L-glutamate γ-semialdehyde dehydrogenase

1.2.1.89 D-glyceraldehyde dehydrogenase (NADP⁺)

1.2.1.90 glyceraldehyde-3-phosphate dehydrogenase [NAD(P)⁺]

1.2.1.91 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase

1.2.1.92 3,6-anhydro-α-L-galactose dehydrogenase

1.2.1.93 formate dehydrogenase (NAD⁺, ferredoxin)

1.2.1.94 farnesal dehydrogenase

1.2.1.95 L-2-aminoadipate reductase

1.2.1.96 4-hydroxybenzaldehyde dehydrogenase (NADP⁺)

1.2.1.97 3-sulfolactaldehyde dehydrogenase

1.2.1.98 2-hydroxy-2-methylpropanal dehydrogenase

1.2.1.99 4-(γ-glutamylamino)butanal dehydrogenase

1.2.1.100 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase

1.2.1.101 L-tyrosine reductase

1.2.1.102 isopyridoxal dehydrogenase (5-pyridoxate-forming)

1.2.1.103 [amino-group carrier protein]-6-phospho-L-2-aminoadipate reductase

1.2.1.104 pyruvate dehydrogenase system

1.2.1.105 2-oxoglutarate dehydrogenase system

1.2.1.106 [amino-group carrier protein]-5-phospho-L-glutamate reductase

1.2.1.107 glyceraldehyde-3-phosphate dehydrogenase (arsenate-transferring)

1.2.2 With a cytochrome as acceptor

1.2.3 With oxygen as acceptor

1.2.4 With a disulfide as acceptor

1.2.5 With a quinone or similar compound as acceptor

1.2.7 With an iron-sulfur protein as acceptor

1.2.98 With other, known, physiological acceptors

1.2.99 With unknown physiological acceptors

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

1.8.1 With NAD⁺ or NADP⁺ as acceptor

1.8.2 With a cytochrome as acceptor

1.8.3 With oxygen as acceptor

1.8.4 With a disulfide as acceptor

1.8.5 With a quinone or similar compound as acceptor

1.8.6 With a nitrogenous group as acceptor (deleted sub-subclass)

1.8.7 With an iron-sulfur protein as acceptor

1.8.98 With other, known, physiological acceptors

1.8.99 With unknown physiological acceptors

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

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

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

1.17.1 With NAD⁺ or NADP⁺ as acceptor

1.17.2 With a cytochrome as acceptor

1.17.3 With oxygen as acceptor

1.17.4 With a disulfide as acceptor

1.17.5 With a quinone or similar compound as acceptor

1.17.7 With an iron-sulfur protein as acceptor

1.17.8 With a flavin as acceptor

1.17.9 With a copper protein as acceptor

1.17.98 With other, known, physiological acceptors

1.17.99 With unknown physiological acceptors

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)

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Release 2023.1 (January 2023)