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EC 1.1.3.45 Details

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EC number

1.1.3.45

Accepted name

aclacinomycin-N oxidase

Reaction

aclacinomycin N + O₂ = aclacinomycin A + H₂O₂

Other name(s)

AknOx (ambiguous), aclacinomycin oxidoreductase (ambiguous)

Systematic name

aclacinomycin-N:oxygen oxidoreductase

Comment

A flavoprotein (FAD). This bifunctional enzyme is a secreted flavin-dependent enzyme that is involved in the modification of the terminal sugar residues in the biosynthesis of aclacinomycins. The enzyme utilizes the same active site to catalyse the oxidation of the rhodinose moiety of aclacinomycin N to the cinerulose A moiety of aclacinomycin A and the oxidation of the latter to the L-aculose moiety of aclacinomycin Y (cf. EC 1.3.3.14, aclacinomycin A oxidase).

History

created 2013

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

1.6.1 With NAD⁺ or NADP⁺ as acceptor

1.6.2 With a heme protein as acceptor

1.6.3 With oxygen as acceptor

1.6.4 With a disulfide as acceptor (deleted sub-subclass)

1.6.5 With a quinone or similar compound as acceptor

1.6.6 With a nitrogenous group as acceptor

1.6.7 With an iron-sulfur protein as acceptor (deleted sub-subclass)

1.6.8 With a flavin as acceptor (deleted sub-subclass)

1.6.99 With unknown physiological acceptors

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

1.8.5 With a quinone or similar compound as acceptor

1.8.5.1 glutathione dehydrogenase (ascorbate)

1.8.5.2 thiosulfate dehydrogenase (quinone)

1.8.5.3 respiratory dimethylsulfoxide reductase

1.8.5.4 bacterial sulfide:quinone reductase

1.8.5.5 thiosulfate reductase (quinone)

1.8.5.6 sulfite dehydrogenase (quinone)

1.8.5.7 glutathionyl-hydroquinone reductase

1.8.5.8 eukaryotic sulfide quinone oxidoreductase

1.8.5.9 protein dithiol:quinone oxidoreductase DsbB

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

1.21.4.1 D-proline reductase

1.21.4.2 glycine reductase

1.21.4.3 sarcosine reductase

1.21.4.4 betaine reductase

1.21.4.5 tetrachlorohydroquinone reductive dehalogenase

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)