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EC 1.10.3.17 Details

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EC number

1.10.3.17

Accepted name

superoxide oxidase

Reaction

2 O₂ + ubiquinol = 2 superoxide + ubiquinone + 2 H⁺

Other name(s)

SOO, CybB, cytochrome b₅₆₁, superoxide:ubiquinone oxidoreductase

Systematic name

ubiquinol:oxygen oxidoreductase (superoxide-forming)

Comment

This membrane-bound, di-heme containing enzyme, identified in the bacterium Escherichia coli, is responsible for the detoxification of superoxide in the periplasm. In vivo the reaction proceeds in the opposite direction of that shown and produces oxygen. Superoxide production was only observed when the enzyme was incubated in vitro with an excess of ubiquinol.

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

1.1.98 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

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.10.1 With NAD⁺ or NADP⁺ as acceptor

1.10.2 With a cytochrome as acceptor

1.10.3 With oxygen as acceptor

1.10.3.1 catechol oxidase

1.10.3.2 laccase

1.10.3.3 L-ascorbate oxidase

1.10.3.4 o-aminophenol oxidase

1.10.3.5 3-hydroxyanthranilate oxidase

1.10.3.6 rifamycin-B oxidase

1.10.3.7 created 1986, deleted 2002

1.10.3.8 created 1986, deleted 2002

1.10.3.9 photosystem II

1.10.3.10 ubiquinol oxidase (H⁺-transporting)

1.10.3.11 ubiquinol oxidase (non-electrogenic)

1.10.3.12 menaquinol oxidase (H⁺-transporting)

1.10.3.13 caldariellaquinol oxidase (H⁺-transporting)

1.10.3.14 ubiquinol oxidase (electrogenic, non H⁺-transporting)

1.10.3.15 grixazone synthase

1.10.3.16 dihydrophenazinedicarboxylate synthase

1.10.3.17 superoxide oxidase

1.10.5 With a quinone or related compound as acceptor

1.10.9 With a copper protein as acceptor

1.10.99 With unknown physiological acceptors

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)

4.1 Carbon-carbon lyases

4.2 Carbon-oxygen lyases

4.3 Carbon-nitrogen lyases

4.4 Carbon-sulfur lyases

4.5 Carbon-halide lyases

4.6 Phosphorus-oxygen lyases

4.7 carbon-phosphorus lyases

4.8 Nitrogen-oxygen lyases

4.98 ATP-independent chelatases

4.99 Other lyases

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Release 2023.1 (January 2023)