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Oxidase Test Protocol - Library. American Society for Microbiology, ASM MicrobeLibrary, 1–5. Steel K J. 1961. The Oxidase Reaction as a Taxonomic Tool. Journal of General Microbiology. 25, 297–306. Zanderigo F et al. 2018. [11C]Harmine Binding to Brain Monoamine Oxidase A: Test-Retest Properties and Noninvasive Quantification.
In reactions involving donation of a hydrogen atom, oxygen is reduced to water (H 2 O) or hydrogen peroxide (H 2 O 2). Some oxidation reactions, such as those involving monoamine oxidase or xanthine oxidase, typically do not involve free molecular oxygen. [1] [2] The oxidases are a subclass of the oxidoreductases. The use of dioxygen is the ...
Oxygenases were discovered in 1955 simultaneously by two groups, Osamu Hayaishi from Japan [4] [5] [6] and Howard S. Mason from the US. [7] [8] Hayaishi was awarded the 1986 Wolf Prize in Medicine "for the discovery of the oxygenase enzymes and elucidation of their structure and biological importance."
In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP+ or NAD+ as cofactors.
[1] [2] These enzymes include a variety of proteins; choline dehydrogenase (CHD) EC 1.1.99.1, methanol oxidase (MOX) EC 1.1.3.13 and cellobiose dehydrogenase EC 1.1.99.18 [3] which share a number of regions of sequence similarities. They contain two conserved protein domains.
Squalene monooxygenase (also called squalene epoxidase) is a eukaryotic enzyme that uses NADPH and diatomic oxygen to oxidize squalene to 2,3-oxidosqualene (squalene epoxide). Squalene epoxidase catalyzes the first oxygenation step in sterol biosynthesis and is thought to be one of the rate-limiting enzymes in this pathway. [ 5 ]
Nitrite reductase EC 1.7.2.1, a 2-domain enzyme containing type-1 and type-2 copper centres. [ 6 ] [ 7 ] In addition to the above enzymes there are a number of other proteins that are similar to the multi-copper oxidases in terms of structure and sequence, some of which have lost the ability to bind copper.
The oxygen incorporated need not be derived from O2 with reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor. The systematic name of this enzyme class is 1-aminocyclopropane-1-carboxylate oxygenase (ethylene-forming). Other names in common use include ACC oxidase, and ethylene-forming enzyme.