| dicarboxylic acid-CoA oxidase | <enzyme> Oxidises dicarboxylic acid CoA esters using molecular oxygen and producing hydrogen peroxide, ultimately producing a dicarboxylic acid with 2 fewer carbon atoms Registry number: EC 1.3.3.- Synonym: dicarboxylyl-CoA oxidase, dicarboxylic acid-coenzyme a oxidase (26 Jun 1999) |
|---|---|
| dihdroxyindole-carboxylic acid oxidase | <enzyme> Converts 5,6-dihydroxyindole-2-carboxylic acid to melanochrome in premelanosomes; no further information on mechanism 6/95 Registry number: EC 1.- Synonym: dhica oxidase, dhi2c oxidase (26 Jun 1999) |
| dihydrobenzophenanthridine oxidase | <enzyme> Copper-containing oxidase from sanguinaria canadensis; converts dihydrophenanthridines to the corresponding alkaloids, sanguinarine or chelerythrine; requires oxygen, does not contain flavins or pyridine nucleotides; inhibited by thiols Registry number: EC 1.3.3.- Synonym: dihydrosanguinarine oxidase, dihydronorsanguinarine oxidase, dihydrochelerythrine oxidase (26 Jun 1999) |
| dihydrogeodin oxidase | <enzyme> Copper-containing enzyme which converts dihydrogeodin to (+)-geodin by an intramolecular phenol oxidative coupling reaction; isolated from aspergillus terreus Registry number: EC 1.10.3.- (26 Jun 1999) |
| dihydroorotate oxidase | <enzyme> An enzyme that in the course of pyrimidine biosynthesis, catalyses the oxidation of dihydro-orotic acid to orotic acid utilizing oxygen as the electron acceptor. This enzyme is a flavoprotein which contains both fad and fmn as well as iron-sulfur centres. Chemical name: (S)-Dihydroorotate:oxygen oxidoreductase Registry number: EC 1.3.3.1 (12 Dec 1998) |
| dihydropterin oxidase | <enzyme> From drosophila melanogaster; uses a variety of 2-amino-4-oxo-7,8-dihydropteridine cpds as substrates; during reaction 1 mole of molecular o2 is consumed/mole substrate oxidised producing h2o2 Registry number: EC 1.5.3.- (26 Jun 1999) |
| dihydrouracil oxidase | <enzyme> Oxygen dependent; no cofactor required, forms uracil irreversibly; enzyme from rhodosporidium toruloides Registry number: EC 1.3.3.- (26 Jun 1999) |
| diphenol oxidase | <enzyme> An enzyme of the oxidoreductase class that catalyses the reaction between catechol and oxygen to yield benzoquinone and water. It is a complex of copper-containing proteins that acts also on a variety of substituted catechols. Chemical name: 1,2-Benzenediol:oxygen oxidoreductase Registry number: EC 1.10.3.1 (12 Dec 1998) |
| dopa oxidase | Provisional name given the enzyme(s) catalyzing the formation of melanins from dopa; it now appears that the copper-containing monophenol monooxygenases and/or catechol oxidases are responsible for the oxidation of l-tyrosine to dopa and dopa quinone. (05 Mar 2000) |
| duroquinol oxidase | <enzyme> Consists of fixn, fixo, and fixp proteins in bradyrhizobium, in which fixo and fixp are c-type cytochromes; does not contain cytochromes, probably a flavoprotein; a proto-haem containing oxidase expressed by the cyoabc locus in paracoccus denitrificans Registry number: EC 1.- Synonym: aroid alternative oxidase, quinol oxidase, trypanosoma alternative oxidase, cyanide-resistant alternative oxidase, cytochrome bb3, cytochrome bb(3) (26 Jun 1999) |
| indole-3-ethanol oxidase | <enzyme> Involved in conversion of indole-3-ethanol to indole-3-acetic acid; isolated from seeds of the bean phaseolus vulgaris; not stimulated by nadp or fad; do not confuse with nad- or nadp-dependent indole-3-ethanol oxidases Registry number: EC 1.1.- Synonym: tryptophol oxidase (26 Jun 1999) |
| indoleacetic acid oxidase | <enzyme> Found in tomatoes Registry number: EC 1.11.- Synonym: iaa oxidase (26 Jun 1999) |
| indophenol oxidase | <enzyme> Also oxidises tetrazolium salts in the presence of phenazine methosulfate; this is not EC 1.9.3.1 Registry number: EC 1.- (26 Jun 1999) |
| octopine oxidase | <enzyme> Catalyses oxidative cleavage of octopine into l-arginine and pyruvate; no required cofactors; activity requires ooxa and ooxb gene products; isolated from agrobacterium tumefaciens Registry number: EC 1.5.99.- (26 Jun 1999) |
| oxidase | Classically, one of a group of enzymes, now termed oxidoreductases (EC class 1), that bring about oxidation by the addition of oxygen to a metabolite or by the removal of hydrogen or of one or more electrons. Oxidase is now used for those cases in which O2 acts as an acceptor (of H or of electrons); those removing hydrogen are now termed dehydrogenases. For individual oxidases, see the specific names. Direct oxidase, originally, an oxidase catalyzing the transfer of O2 directly to other bodies; now termed oxygenase. Indirect oxidase, originally, an oxidase that acts by reducing a peroxide; now termed peroxidase. Terminal oxidase, the last protein in the electron transport, respiratory chain. In mammals this is cytochrome c oxidase. (05 Mar 2000) |