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1.1.3.13: alcohol oxidase

This is an abbreviated version!
For detailed information about alcohol oxidase, go to the full flat file.

Word Map on EC 1.1.3.13

Reaction

a primary alcohol
+
O2
=
an aldehyde
+
H2O2

Synonyms

alcohol oxidase 1, alcohol oxidase 2, alcohol oxidase A, alcohol oxidase B, alcohol oxidase I, alcohol: O2 oxidoreductase, alcohol:dioxygen-oxidoreductase, alcohol:O2 oxidoreductase, AlcOx, AOd, AOD1, AOext, AOint, AOX, AOX1, AOX2, AOXI, broad substrate specific alcohol oxidase, EC 1.1.3.31, ethanol oxidase, extracellular alcohol oxidase, FAD-dependent alcohol oxidase, FAO1, GLRG_05590, intracellular alcohol oxidase, long chain fatty alcohol oxidase, methanol oxidase, Mod1p, Mod2p, oxidase, alcohol, P-AOD, peroxisomal alcohol oxidase, primary alcohol oxidase, SCAO, short chain alcohol oxidase, short-chain alcohol oxidase, VAO, veratryl alcohol oxidase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.13 alcohol oxidase

Renatured

Renatured on EC 1.1.3.13 - alcohol oxidase

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
enzyme dissociation by 2 M KBr in 0.25 M potassium phosphate, pH 7.5, 0.3 mM EDTA, 5 mM 2-mercaptoethanol and 20% glycerol, for 4 days at 4°C. The inactive dissociated enzyme protein is renaturated, but still catalytically inactive, by assembly after removal of 2-mercaptoethanol and incubation with cofactor FAD. The enzyme activity is regained by incubation with the substrate. The dissociation process traverses through two FAD-associated intermediate proteins, one of whhich shows the enzyme activity. The catalytic reactivation is a slow process. Dynamic light scattering analysis, overview. DMSO and ethylene glycol are ineffective in dissociating this alcohol oxidase
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