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EC 1.8.1.21 Details

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EC number

1.8.1.21

Accepted name

dissimilatory dimethyldisulfide reductase

Reaction

2 methanethiol + NAD⁺ = dimethyl disulfide + NADH + H⁺

Systematic name

methanethiol:NAD⁺ oxidoreductase (dimethyl disulfide-forming)

Comment

The enzyme’s activity has been demonstrated in the bacterium Thiobacillus thioparus E6. The methanethiol formed is eventually oxidized to sulfate and carbon dioxide, and the latter assimilated for autotrophic growth.

History

created 2019

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

1.1.9.1 alcohol dehydrogenase (azurin)

1.1.98 With other, known, physiological acceptors

1.1.98.1 alcohol dehydrogenase (azurin)

1.1.98.2 glucose-6-phosphate dehydrogenase (coenzyme-F₄₂₀)

1.1.98.3 decaprenylphospho-β-D-ribofuranose 2-dehydrogenase

1.1.98.4 F₄₂₀H₂:quinone oxidoreductase

1.1.98.5 secondary-alcohol dehydrogenase (coenzyme-F₄₂₀)

1.1.98.6 ribonucleoside-triphosphate reductase (formate)

1.1.98.7 serine-type anaerobic sulfatase-maturating enzyme

1.1.99 With unknown physiological acceptors

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

1.8.1 With NAD⁺ or NADP⁺ as acceptor

1.8.1.1 created 1961, deleted 1972

1.8.1.2 assimilatory sulfite reductase (NADPH)

1.8.1.3 hypotaurine dehydrogenase

1.8.1.4 dihydrolipoyl dehydrogenase

1.8.1.5 2-oxopropyl-CoM reductase (carboxylating)

1.8.1.6 cystine reductase

1.8.1.7 glutathione-disulfide reductase

1.8.1.8 protein-disulfide reductase

1.8.1.9 thioredoxin-disulfide reductase

1.8.1.10 CoA-glutathione reductase

1.8.1.11 asparagusate reductase

1.8.1.12 trypanothione-disulfide reductase

1.8.1.13 bis-γ-glutamylcystine reductase

1.8.1.14 CoA-disulfide reductase

1.8.1.15 mycothione reductase

1.8.1.16 glutathione amide reductase

1.8.1.17 dimethylsulfone reductase

1.8.1.18 NAD(P)H sulfur oxidoreductase (CoA-dependent)

1.8.1.19 sulfide dehydrogenase

1.8.1.20 4,4′-dithiodibutanoate disulfide reductase

1.8.1.21 dissimilatory dimethyldisulfide reductase

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

1.8.7.1 assimilatory sulfite reductase (ferredoxin)

1.8.7.2 ferredoxin:thioredoxin reductase

1.8.7.3 ferredoxin:CoB-CoM heterodisulfide reductase

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

1.18 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

1.21.98 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)