 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 |
|---|
| 1997 | 1 | 1 | 2 | | 1998 | 1 | 0 | 1 | | 2000 | 0 | 2 | 2 | | 2001 | 1 | 0 | 1 | | 2003 | 0 | 1 | 1 | | 2006 | 2 | 0 | 2 | | 2008 | 2 | 1 | 3 | | 2011 | 2 | 1 | 3 | | 2012 | 1 | 0 | 1 | | 2013 | 2 | 1 | 3 | | 2014 | 2 | 1 | 3 | | 2015 | 1 | 0 | 1 | | 2016 | 1 | 0 | 1 | | 2020 | 1 | 0 | 1 | | 2021 | 0 | 1 | 1 | | 2023 | 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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Ravindran Menon D, Hammerlindl H, Gimenez G, Hammerlindl S, Zuegner E, Torrano J, Bordag N, Emran AA, Giam M, Denil S, Pavelka N, Tan AC, Sturm RA, Haass NK, Rancati G, Herlyn M, Magnes C, Eccles MR, Fujita M, Schaider H. H3K4me3 remodeling induced acquired resistance through O-GlcNAc transferase. Drug Resist Updat. 2023 Nov; 71:100993.
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Wang H, Wang L, Zheng Q, Lu Z, Chen Y, Shen D, Xue D, Jiang M, Ding L, Zhang J, Wu H, Xia L, Qian J, Li G, Lu J. Oncometabolite L-2-hydroxyglurate directly induces vasculogenic mimicry through PHLDB2 in renal cell carcinoma. Int J Cancer. 2021 04 01; 148(7):1743-1755.
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Ismail JN, Ghannam M, Al Outa A, Frey F, Shirinian M. Ten-eleven translocation proteins and their role beyond DNA demethylation - what we can learn from the fly. Epigenetics. 2020 11; 15(11):1139-1150.
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Bissaro B, Streit B, Isaksen I, Eijsink VGH, Beckham GT, DuBois JL, R?hr ?K. Molecular mechanism of the chitinolytic peroxygenase reaction. Proc Natl Acad Sci U S A. 2020 01 21; 117(3):1504-1513.
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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 (Reading). 2018 05; 164(5):790-800.
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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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Vermaas JV, Crowley MF, Beckham GT, Payne CM. Effects of lytic polysaccharide monooxygenase oxidation on cellulose structure and binding of oxidized cellulose oligomers to cellulases. J Phys Chem B. 2015 May 21; 119(20):6129-43.
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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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Gudmundsson M, Kim S, Wu M, Ishida T, Momeni MH, Vaaje-Kolstad G, Lundberg D, Royant A, St?hlberg J, Eijsink VG, Beckham GT, Sandgren M. Structural and electronic snapshots during the transition from a Cu(II) to Cu(I) metal center of a lytic polysaccharide monooxygenase by X-ray photoreduction. J Biol Chem. 2014 Jul 04; 289(27):18782-92.
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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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