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EC 1.5.3.22 Details

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EC number

1.5.3.22

Accepted name

coenzyme F₄₂₀H₂ oxidase

Reaction

2 reduced coenzyme F₄₂₀ + O₂ = 2 oxidized coenzyme F₄₂₀ + 2 H₂O

Other name(s)

FprA

Systematic name

reduced coenzyme F₄₂₀:oxygen oxidoreductase

Comment

The enzyme contains FMN and a binuclear iron center. The enzyme from the archaeon Methanothermobacter marburgensis is Si-face specific with respect to C-5 of coenzyme F₄₂₀ [2].

History

created 2013

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

1.5.1 With NAD⁺ or NADP⁺ as acceptor

1.5.3 With oxygen as acceptor

1.5.3.1 sarcosine oxidase (formaldehyde-forming)

1.5.3.2 N-methyl-L-amino-acid oxidase

1.5.3.3 created 1961, deleted 1972

1.5.3.4 N⁶-methyl-lysine oxidase

1.5.3.5 (S)-6-hydroxynicotine oxidase

1.5.3.6 (R)-6-hydroxynicotine oxidase

1.5.3.7 L-pipecolate oxidase

1.5.3.8 created 1989, deleted 1992

1.5.3.9 created 1989, modified 1999, deleted 2002

1.5.3.10 dimethylglycine oxidase

1.5.3.11 polyamine oxidase

1.5.3.12 dihydrobenzophenanthridine oxidase

1.5.3.13 N¹-acetylpolyamine oxidase

1.5.3.14 polyamine oxidase (propane-1,3-diamine-forming)

1.5.3.15 N⁸-acetylspermidine oxidase (propane-1,3-diamine-forming)

1.5.3.16 spermine oxidase

1.5.3.17 non-specific polyamine oxidase

1.5.3.18 L-saccharopine oxidase

1.5.3.19 4-methylaminobutanoate oxidase (formaldehyde-forming)

1.5.3.20 N-alkylglycine oxidase

1.5.3.21 4-methylaminobutanoate oxidase (methylamine-forming)

1.5.3.22 coenzyme F₄₂₀H₂ oxidase

1.5.3.23 glyphosate oxidoreductase

1.5.3.24 sarcosine oxidase (5,10-methylenetetrahydrofolate-forming)

1.5.3.25 fructosyl amine oxidase (glucosone-forming)

1.5.3.26 fructosyl amine oxidase (fructosamine-forming)

1.5.4 With a disulfide as acceptor

1.5.5 With a quinone or similar compound as acceptor

1.5.7 With an iron-sulfur protein as acceptor

1.5.8 With a flavin or flavoprotein as acceptor

1.5.98 With other, known, physiological acceptors

1.5.99 With unknown physiological acceptors

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

1.13 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

1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses

1.97.1.1 chlorate reductase

1.97.1.2 pyrogallol hydroxytransferase

1.97.1.3 sulfur reductase

1.97.1.4 [formate-C-acetyltransferase]-activating enzyme

1.97.1.5 created 2000 deleted 2001

1.97.1.6 created 2000 deleted 2001

1.97.1.7 created 2000, deleted 2001

1.97.1.8 tetrachloroethene reductive dehalogenase

1.97.1.9 selenate reductase

1.97.1.10 thyroxine 5′-deiodinase

1.97.1.11 thyroxine 5-deiodinase

1.97.1.12 photosystem I

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)