 FMN Reductase
"FMN Reductase" 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.
An enzyme that utilizes NADH or NADPH to reduce FLAVINS. It is involved in a number of biological processes that require reduced flavin for their functions such as bacterial bioluminescence. Formerly listed as EC 1.6.8.1 and EC 1.5.1.29.
| Descriptor ID |
D038181
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| MeSH Number(s) |
D08.811.682.662.171
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| Concept/Terms |
FMN Reductase- FMN Reductase
- Reductase, FMN
- FMN Oxidoreductase
- Oxidoreductase, FMN
- NAD(P)H Dehydrogenase (FMN)
- NAD(P)H-Flavin Oxidoreductase
- NADH-Flavin Oxidoreductase
- Oxidoreductase, NADH-Flavin
- NADH-FMN Oxidoreductase
- NADH FMN Oxidoreductase
- Oxidoreductase, NADH-FMN
- NADPH-Flavin Reductase
- NADPH Flavin Reductase
- Reductase, NADPH-Flavin
- Flavin Mononucleotide Reductase
- Mononucleotide Reductase, Flavin
- Reductase, Flavin Mononucleotide
- NAD(P)H-FMN Oxidoreductase
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Below are MeSH descriptors whose meaning is more general than "FMN Reductase".
Below are MeSH descriptors whose meaning is more specific than "FMN Reductase".
This graph shows the total number of publications written about "FMN Reductase" by people in this website by year, and whether "FMN Reductase" 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 |
|---|
| 2003 | 1 | 0 | 1 | | 2004 | 2 | 0 | 2 | | 2005 | 1 | 0 | 1 | | 2006 | 2 | 0 | 2 | | 2007 | 1 | 0 | 1 | | 2008 | 1 | 0 | 1 | | 2012 | 1 | 0 | 1 |
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Below are the most recent publications written about "FMN Reductase" by people in Profiles.
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Chung HW, Tu SC. Structure-function relationship of Vibrio harveyi NADPH-flavin oxidoreductase FRP: essential residues Lys167 and Arg15 for NADPH binding. Biochemistry. 2012 Jun 19; 51(24):4880-7.
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Jawanda N, Ebalunode J, Gribenko A, Briggs J, Lee JC, Tu SC. A single-residue mutation destabilizes Vibrio harveyi flavin reductase FRP dimer. Arch Biochem Biophys. 2008 Apr 01; 472(1):51-7.
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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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Li X, Chow DC, Tu SC. Thermodynamic analysis of the binding of oxidized and reduced FMN cofactor to Vibrio harveyi NADPH-FMN oxidoreductase FRP apoenzyme. Biochemistry. 2006 Dec 12; 45(49):14781-7.
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Li X, Tu SC. Activity coupling of Vibrio harveyi luciferase and flavin reductase (FRP): oxygen as a probe. Arch Biochem Biophys. 2006 Oct 01; 454(1):26-31.
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Lei B, Wang H, Yu Y, Tu SC. Redox potential and equilibria in the reductive half-reaction of Vibrio harveyi NADPH-FMN oxidoreductase. Biochemistry. 2005 Jan 11; 44(1):261-7.
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Russell TR, Tu SC. Aminobacter aminovorans NADH:flavin oxidoreductase His140: a highly conserved residue critical for NADH binding and utilization. Biochemistry. 2004 Oct 12; 43(40):12887-93.
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Russell TR, Demeler B, Tu SC. Kinetic mechanism and quaternary structure of Aminobacter aminovorans NADH:flavin oxidoreductase: an unusual flavin reductase with bound flavin. Biochemistry. 2004 Feb 17; 43(6):1580-90.
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Jeffers CE, Nichols JC, Tu SC. Complex formation between Vibrio harveyi luciferase and monomeric NADPH:FMN oxidoreductase. Biochemistry. 2003 Jan 21; 42(2):529-34.
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