 Mixed Function Oxygenases
"Mixed Function Oxygenases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation.
| Descriptor ID |
D006899
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| MeSH Number(s) |
D08.811.682.690.708
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| Concept/Terms |
Mixed Function Oxygenases- Mixed Function Oxygenases
- Oxygenases, Mixed Function
- Monooxygenases
- Hydroxylases
- Mixed Function Oxidases
- Oxidases, Mixed Function
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Below are MeSH descriptors whose meaning is more general than "Mixed Function Oxygenases".
Below are MeSH descriptors whose meaning is more specific than "Mixed Function Oxygenases".
This graph shows the total number of publications written about "Mixed Function Oxygenases" by people in this website by year, and whether "Mixed Function Oxygenases" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2003 | 2 | 2 | 4 | | 2005 | 0 | 1 | 1 | | 2007 | 1 | 0 | 1 | | 2008 | 0 | 1 | 1 | | 2009 | 0 | 1 | 1 | | 2011 | 0 | 1 | 1 |
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Below are the most recent publications written about "Mixed Function Oxygenases" by people in Profiles.
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Do LH, Lippard SJ. Toward functional carboxylate-bridged diiron protein mimics: achieving structural stability and conformational flexibility using a macrocylic ligand framework. J Am Chem Soc. 2011 Jul 13; 133(27):10568-81.
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Jorgensen AL, Al-Zubiedi S, Zhang JE, Keniry A, Hanson A, Hughes DA, Eker Dv, Stevens L, Hawkins K, Toh CH, Kamali F, Daly AK, Fitzmaurice D, Coffey A, Williamson PR, Park BK, Deloukas P, Pirmohamed M. Genetic and environmental factors determining clinical outcomes and cost of warfarin therapy: a prospective study. Pharmacogenet Genomics. 2009 Oct; 19(10):800-12.
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Cápiro NL, Da Silva ML, Stafford BP, Rixey WG, Alvarez PJ. Microbial community response to a release of neat ethanol onto residual hydrocarbons in a pilot-scale aquifer tank. Environ Microbiol. 2008 Sep; 10(9):2236-44.
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Jawanda N, Ahmed K, Tu SC. Vibrio harveyi flavin reductase--luciferase fusion protein mimics a single-component bifunctional monooxygenase. Biochemistry. 2008 Jan 08; 47(1):368-77.
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Nyangulu JM, Galka MM, Jadhav A, Gai Y, Graham CM, Nelson KM, Cutler AJ, Taylor DC, Banowetz GM, Abrams SR. An affinity probe for isolation of abscisic acid-binding proteins. J Am Chem Soc. 2005 Feb 16; 127(6):1662-4.
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Zufall RA, Rausher MD. The genetic basis of a flower color polymorphism in the common morning glory (Ipomoea purpurea). J Hered. 2003 Nov-Dec; 94(6):442-8.
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Cirino PC, Tang Y, Takahashi K, Tirrell DA, Arnold FH. Global incorporation of norleucine in place of methionine in cytochrome P450 BM-3 heme domain increases peroxygenase activity. Biotechnol Bioeng. 2003 Sep 20; 83(6):729-34.
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Salazar O, Cirino PC, Arnold FH. Thermostabilization of a cytochrome p450 peroxygenase. Chembiochem. 2003 Sep 05; 4(9):891-3.
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Cirino PC, Georgescu R. Screening for thermostability. Methods Mol Biol. 2003; 230:117-25.
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Cardini G, Jurtshuk P. The enzymatic hydroxylation of n-octane by Corynebacterium sp. strain 7E1C. J Biol Chem. 1970 Jun 10; 245(11):2789-96.
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