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EC 1.2.3.1 Details

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EC number

1.2.3.1

Accepted name

aldehyde oxidase

Reaction

an aldehyde + H₂O + O₂ = a carboxylate + H₂O₂

Other name(s)

quinoline oxidase, retinal oxidase

Systematic name

aldehyde:oxygen oxidoreductase

CAS registry number

9029-07-6

Comment

Contains molybdenum, [2Fe-2S] centres and FAD. The enzyme from liver exhibits a broad substrate specificity, and is involved in the metabolism of xenobiotics, including the oxidation of N-heterocycles and aldehydes and the reduction of N-oxides, nitrosamines, hydroxamic acids, azo dyes, nitropolycyclic aromatic hydrocarbons, and sulfoxides [4,6]. The enzyme is also responsible for the oxidation of retinal, an activity that was initially attributed to a distinct enzyme (EC 1.2.3.11, retinal oxidase) [5,7].

History

created 1961, modified 2002, modified 2004, modified 2012

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

1.2.1 With NAD⁺ or NADP⁺ as acceptor

1.2.2 With a cytochrome as acceptor

1.2.3 With oxygen as acceptor

1.2.3.1 aldehyde oxidase

1.2.3.2 created 1961, deleted 1984

1.2.3.3 pyruvate oxidase

1.2.3.4 oxalate oxidase

1.2.3.5 glyoxylate oxidase

1.2.3.6 pyruvate oxidase (CoA-acetylating)

1.2.3.7 indole-3-acetaldehyde oxidase

1.2.3.8 pyridoxal oxidase

1.2.3.9 aryl-aldehyde oxidase

1.2.3.10 created 1990, deleted 2003

1.2.3.11 retinal oxidase

1.2.3.12 created 2000, deleted 2003

1.2.3.13 4-hydroxyphenylpyruvate oxidase

1.2.3.14 abscisic-aldehyde oxidase

1.2.3.15 (methyl)glyoxal oxidase

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

1.2.99.1 created 1961, deleted 1984

1.2.99.2 carbon-monoxide dehydrogenase (acceptor)

1.2.99.3 aldehyde dehydrogenase (pyrroloquinoline-quinone)

1.2.99.4 formaldehyde dismutase

1.2.99.5 formylmethanofuran dehydrogenase

1.2.99.6 carboxylate reductase

1.2.99.7 aldehyde dehydrogenase (FAD-independent)

1.2.99.8 glyceraldehyde dehydrogenase (FAD-containing)

1.2.99.9 formate dehydrogenase (coenzyme F₄₂₀)

1.2.99.10 4,4′-diapolycopenoate synthase

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

1.11 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)

1.98.1. undefined

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

7 Translocases