 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.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1989 | 2 | 0 | 2 | | 1996 | 1 | 1 | 2 | | 1997 | 1 | 1 | 2 | | 1999 | 0 | 1 | 1 | | 2000 | 0 | 3 | 3 | | 2001 | 2 | 1 | 3 | | 2003 | 0 | 1 | 1 | | 2004 | 0 | 2 | 2 | | 2006 | 2 | 0 | 2 | | 2008 | 3 | 1 | 4 | | 2010 | 1 | 0 | 1 | | 2011 | 3 | 1 | 4 | | 2012 | 2 | 0 | 2 | | 2013 | 1 | 1 | 2 | | 2014 | 1 | 1 | 2 | | 2016 | 1 | 0 | 1 | | 2017 | 0 | 1 | 1 | | 2018 | 1 | 0 | 1 |
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Below are the most recent publications written about "Mixed Function Oxygenases" by people in Profiles.
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Sporer AJ, Beierschmitt C, Bendebury A, Zink KE, Price-Whelan A, Buzzeo MC, Sanchez LM, Dietrich LEP. Pseudomonas aeruginosa PumA acts on an endogenous phenazine to promote self-resistance. Microbiology. 2018 05; 164(5):790-800.
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Zhuang Y, Tripp EA. The draft genome of Ruellia speciosa (Beautiful Wild Petunia: Acanthaceae). DNA Res. 2017 Apr 01; 24(2):179-192.
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Sprenger KG, Choudhury A, Kaar JL, Pfaendtner J. Lytic Polysaccharide Monooxygenases ScLPMO10B and ScLPMO10C Are Stable in Ionic Liquids As Determined by Molecular Simulations. J Phys Chem B. 2016 04 28; 120(16):3863-72.
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Rudolph J, Erbse AH, Behlen LS, Copley SD. A radical intermediate in the conversion of pentachlorophenol to tetrachlorohydroquinone by Sphingobium chlorophenolicum. Biochemistry. 2014 Oct 21; 53(41):6539-49.
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Zhao X, Dai J, Ma Y, Mi Y, Cui D, Ju G, Macklin WB, Jin W. Dynamics of ten-eleven translocation hydroxylase family proteins and 5-hydroxymethylcytosine in oligodendrocyte differentiation. Glia. 2014 Jun; 62(6):914-26.
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Loutet SA, Kobylarz MJ, Chau CH, Murphy ME. IruO is a reductase for heme degradation by IsdI and IsdG proteins in Staphylococcus aureus. J Biol Chem. 2013 Sep 06; 288(36):25749-59.
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Yadid I, Rudolph J, Hlouchova K, Copley SD. Sequestration of a highly reactive intermediate in an evolving pathway for degradation of pentachlorophenol. Proc Natl Acad Sci U S A. 2013 Jun 11; 110(24):E2182-90.
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Ukpabi G, Takayama SJ, Mauk AG, Murphy ME. Inactivation of the heme degrading enzyme IsdI by an active site substitution that diminishes heme ruffling. J Biol Chem. 2012 Oct 05; 287(41):34179-88.
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Hlouchova K, Rudolph J, Pietari JM, Behlen LS, Copley SD. Pentachlorophenol hydroxylase, a poorly functioning enzyme required for degradation of pentachlorophenol by Sphingobium chlorophenolicum. Biochemistry. 2012 May 08; 51(18):3848-60.
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Horne BD, Lenzini PA, Wadelius M, Jorgensen AL, Kimmel SE, Ridker PM, Eriksson N, Anderson JL, Pirmohamed M, Limdi NA, Pendleton RC, McMillin GA, Burmester JK, Kurnik D, Stein CM, Caldwell MD, Eby CS, Rane A, Lindh JD, Shin JG, Kim HS, Angchaisuksiri P, Glynn RJ, Kronquist KE, Carlquist JF, Grice GR, Barrack RL, Li J, Gage BF. Pharmacogenetic warfarin dose refinements remain significantly influenced by genetic factors after one week of therapy. Thromb Haemost. 2012 Feb; 107(2):232-40.
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