| PHD | pathological habit disorder; personal health data; post-heparin plasma diamine oxidase; potentially ... |
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| p-HPPO | p-hydroxyphenyl pyruvate oxidase |
| UOX | urate oxidase |
| XO | presence of only one sex chromosome; xanthine oxidase |
| 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) |
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| 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) |
| oxidase reaction | The formation of indol blue when a blood smear containing myeloid leukocytes is treated with a mixture of alpha-naphthol and p-dimethylaniline sulfate; the myeloid leukocytes contain an oxidase that catalyses this reaction, the lymphoid leukocytes do not, in bacteriology, a reaction that depends on the presence of certain oxidases in some bacteria that catalyze the transport of electrons between electron donors in the bacteria and an oxidation reduction dye, such as tetramethyl-p-phenylenediamine; the dye is reduced to a blue or black colour. (05 Mar 2000) |