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EC 1.8.4.6 Details

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EC number

1.8.4.6

Accepted name

protein-methionine-S-oxide reductase

Reaction

protein L-methionine + thioredoxin disulfide = protein L-methionine S-oxide + thioredoxin

Other name(s)

methionine sulfoxide (protein) reductase, methionine sulfoxide peptide reductase, protein (methionine sulfoxide) reductase, Met(O)-peptide reductase, peptide methionine sulfoxide reductase, protein-L-methionine:oxidized-thioredoxin S-oxidoreductase

Systematic name

protein-L-methionine:thioredoxin-disulfide S-oxidoreductase

CAS registry number

78206-57-2

Comment

Dithiothreitol, but not 2-mercaptoethanol, can replace a reduced thioredoxin in the reverse reaction. Does not act on free methionine (cf. EC 1.8.4.5 methionine-S-oxide reductase)

History

created 1984, deleted 2006

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

1.1.3.1 created 1961, deleted 1984

1.1.3.2 L-lactate oxidase

1.1.3.3 malate oxidase

1.1.3.4 glucose oxidase

1.1.3.5 hexose oxidase

1.1.3.6 cholesterol oxidase

1.1.3.7 aryl-alcohol oxidase

1.1.3.8 L-gulonolactone oxidase

1.1.3.9 galactose oxidase

1.1.3.10 pyranose oxidase

1.1.3.11 L-sorbose oxidase

1.1.3.12 pyridoxine 4-oxidase

1.1.3.13 alcohol oxidase

1.1.3.14 catechol oxidase (dimerizing)

1.1.3.15 (S)-2-hydroxy-acid oxidase

1.1.3.16 ecdysone oxidase

1.1.3.17 choline oxidase

1.1.3.18 secondary-alcohol oxidase

1.1.3.19 4-hydroxymandelate oxidase (decarboxylating)

1.1.3.20 long-chain-alcohol oxidase

1.1.3.21 glycerol-3-phosphate oxidase

1.1.3.22 created 1961 as EC 1.2.3.2, transferred 1984 to EC 1.1.3.22, modified 1989, deleted 2004

1.1.3.23 thiamine oxidase

1.1.3.24 L-galactonolactone oxidase

1.1.3.25 created 1986, deleted 2005

1.1.3.26 created 1989, deleted 2002

1.1.3.27 hydroxyphytanate oxidase

1.1.3.28 nucleoside oxidase

1.1.3.29 N-acylhexosamine oxidase

1.1.3.30 polyvinyl-alcohol oxidase

1.1.3.31 created 1992, deleted 2003

1.1.3.32 created 1999, deleted 2002

1.1.3.33 created 1999, deleted 2002

1.1.3.34 created 1999, deleted 2002

1.1.3.35 created 1999, deleted 2002

1.1.3.36 created 1999, deleted 2002

1.1.3.37 D-arabinono-1,4-lactone oxidase

1.1.3.38 vanillyl-alcohol oxidase

1.1.3.39 nucleoside oxidase (H₂O₂-forming)

1.1.3.40 D-mannitol oxidase

1.1.3.41 alditol oxidase

1.1.3.42 prosolanapyrone-II oxidase

1.1.3.43 paromamine 6′-oxidase

1.1.3.44 6′′′-hydroxyneomycin C oxidase

1.1.3.45 aclacinomycin-N oxidase

1.1.3.46 4-hydroxymandelate oxidase

1.1.3.47 5-(hydroxymethyl)furfural oxidase

1.1.3.48 3-deoxy-α-D-manno-octulosonate 8-oxidase

1.1.3.49 (R)-mandelonitrile oxidase

1.1.3.50 C-glycoside oxidase

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

1.3 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

1.8.4.1 glutathione—homocystine transhydrogenase

1.8.4.2 protein-disulfide reductase (glutathione)

1.8.4.3 glutathione—CoA-glutathione transhydrogenase

1.8.4.4 glutathione—cystine transhydrogenase

1.8.4.5 methionine-S-oxide reductase

1.8.4.6 protein-methionine-S-oxide reductase

1.8.4.7 enzyme-thiol transhydrogenase (glutathione-disulfide)

1.8.4.8 phosphoadenylyl-sulfate reductase (thioredoxin)

1.8.4.9 adenylyl-sulfate reductase (glutathione)

1.8.4.10 adenylyl-sulfate reductase (thioredoxin)

1.8.4.11 peptide-methionine (S)-S-oxide reductase

1.8.4.12 peptide-methionine (R)-S-oxide reductase

1.8.4.13 L-methionine (S)-S-oxide reductase

1.8.4.14 L-methionine (R)-S-oxide reductase

1.8.4.15 protein dithiol oxidoreductase (disulfide-forming)

1.8.4.16 thioredoxin:protein disulfide reductase

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

1.18 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)

6.1 Forming carbon-oxygen bonds

6.2 Forming carbon-sulfur bonds

6.3 Forming carbon-nitrogen bonds

6.4 Forming carbon-carbon bonds

6.5 Forming phosphoric-ester bonds

6.6 Forming nitrogen—metal bonds

6.7 Forming nitrogen-nitrogen bonds

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Release 2023.1 (January 2023)