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Flavin reductase a class of enzymes. There are a variety of flavin reductases, (i.e. FRP, FRE, FRG, etc.) which bind free flavins and through hydrogen
Flavin_reductase
Protein-coding gene in the species Homo sapiens
for isozymes I and II is 8.2. Flavin reductase/biliverdin-IXbeta reductase has also been shown to exhibit ferric reductase activity, with an apparent K(m)
Biliverdin_reductase_B
siderophores. Non-specific bacterial flavin reductase has been well researched within E. coli, which is the NAD(P)H: flavin oxidoreductase (Fre). In E. coli
Ferric-chelate_reductase
Flavin reductase (NADH) (EC 1.5.1.36, NADH-dependent flavin reductase, flavin:NADH oxidoreductase) is an enzyme with systematic name flavin:NAD+ oxidoreductase
Flavin_reductase_(NADH)
Coenzyme
In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic
Flavin_adenine_dinucleotide
Enzyme
reducing environment of the cell. Glutathione reductase functions as dimeric disulfide oxidoreductase and uses flavin adenine dinucleotide and nicotinamide adenine
Glutathione_reductase
reduced flavin is released from flavin reductase. If this mechanism is indeed correct, it suggests that the reduction of flavin by flavin reductase is dependent
Riboflavin reductase (NAD(P)H)
Riboflavin_reductase_(NAD(P)H)
Class of enzymes
Ene-reductases are classified as oxidoreductases (EC 1), they can be divided in two broad categories based on the performed reduction mechanism: Flavin-dependent
Ene-reductase
Enzyme
mononucleotide reductase, flavine mononucleotide reductase, riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide, (phosphate)) reductase, flavin mononucleotide
FMN_reductase
Topics referred to by the same term
gene Flavin group, a group of organic compounds Flavin mononucleotide, a biomolecule produced from riboflavin Flavin reductase, an enzyme Flavin, Aveyron
Flavin
Condition of elevated methemoglobin in the blood
1980). "Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes". Journal of Biochemistry
Methemoglobinemia
Enzyme involved in redox reactions
FMN reductase (NADPH) (EC 1.5.1.38, FRP, flavin reductase P, SsuE) is an enzyme with systematic name FMNH2:NADP+ oxidoreductase. This enzyme catalyses
FMN_reductase_(NADPH)
Type of enzyme
thus require either excess FADH2 or the presence of a flavin reductase. Since flavin reductase is itself NAD(P)H-dependent, a recent work studying RebH
Tryptophan_7-halogenase
Enzyme converting fumarate to succinate
B as hydrogen donors. Fumarate reductase (quinol) (EC 1.3.5.1) The membrane-bound enzyme covalently linked to flavin cofactors, which is composed of
Fumarate_reductase
Class of enzymes
In enzymology, a ferredoxin-NADP+ reductase (EC 1.18.1.2) abbreviated FNR, is an enzyme that catalyzes the chemical reaction 2 reduced ferredoxin + NADP+
Ferredoxin—NADP(+)_reductase
a substrate. Studies have shown that the mechanism of flavin reduction in morphinone reductase involve the rapid formation of an E-NADHCT charge-transfer
Morphinone_reductase
Class of enzymes
oxidoreductase (flavin-containing). Other names in common use include 2-dehydropantolactone reductase (flavin), 2-dehydropantoyl-lactone reductase (flavin), and
(R)-pantolactone dehydrogenase (flavin)
(R)-pantolactone_dehydrogenase_(flavin)
FAD reductase (NADH) (EC 1.5.1.37, NADH-FAD reductase, NADH-dependent FAD reductase) is an enzyme with systematic name FADH2:NAD+ oxidoreductase. This
FAD_reductase_(NADH)
Rate-limiting enzyme in the methyl cycle
reductase (MTHFR) is the rate-limiting enzyme in the methyl cycle, and it is encoded by the MTHFR gene. Methylenetetrahydrofolate reductase catalyzes
Methylenetetrahydrofolate reductase
Methylenetetrahydrofolate_reductase
Protein-coding gene in the species Homo sapiens
Methionine synthase reductase, also known as MSR, is an enzyme in humans that is encoded by the M1T3R gene. It functions as the obligate reductase for methionine
MTRR_(gene)
Marine bacterium
Janewit; Wongratana Chutintorn (March 2008). "LuxG Is a Functioning Flavin Reductase for Bacterial Luminescence". Journal of Bacteriology. 190 (5): 1531–1538
Vibrio_campbellii
domain, ferredoxin or cytochrome b5 transfer electrons between the flavin reductase (protein or domain) and P450. While P450-containing systems are found
P450-containing_systems
Class of photoreceptors in plants and animals
light. The PMTR was inhibited in CRY gene knockouts and decreased when flavin reductase was inhibited, but remained intact with the addition of melanopsin
Cryptochrome
Index of enzymes associated with the same name
oxidoreductase may refer to: Riboflavin reductase (NAD(P)H), a riboflavin reduction enzyme FMN reductase, a flavin mononucleotide reduction enzyme This set
Riboflavin:NAD(P)+ oxidoreductase
Riboflavin:NAD(P)+_oxidoreductase
Group of chemical compounds
prosthetic group in flavoproteins. Flavin adenine dinucleotide is a group bound to many enzymes including ferredoxin-NADP+ reductase, monoamine oxidase, D-amino
Flavin_group
Bacteria that produce light through chemiluminescence
Photorhabdus operon type, all variants of the lux operon contain the flavin reductase-encoding luxG gene. Most of the Aliivibrio/Shewanella type operons
Bioluminescent_bacteria
Enzyme
In enzymology, a NADPH—hemoprotein reductase is an enzyme that catalyzes the chemical reaction NADPH + H+ + n oxidized hemoprotein ⇌ {\displaystyle \rightleftharpoons
NADPH—hemoprotein_reductase
Protein family
second form of flavin utilised by enzymes. The flavoprotein family contains a diverse range of enzymes, including: Adrenodoxin reductase that is involved
Flavoprotein
Class of enzymes
In enzymology, a 4-hydroxybenzoyl-CoA reductase (EC 1.3.7.9) is an enzyme found in some bacteria and archaea that catalyzes the chemical reaction benzoyl-CoA
4-hydroxybenzoyl-CoA reductase
4-hydroxybenzoyl-CoA_reductase
Protein-coding gene in the species Homo sapiens
selenocysteine or cysteine for catalysis, is part of the NADH oxidase/flavin reductase superfamily, and removes iodide when the substrate is a single amino
Iodotyrosine_deiodinase
Class of enzymes
enzyme is also called enoate reductase. This enzyme participates in phenylalanine metabolism. It has cofactors: flavin adenine dinucleotide and iron–sulfur
2-enoate_reductase
Vitamin
of flavins to be converted between oxidized, half-reduced and fully reduced forms. FAD is also required for the activity of glutathione reductase, an
Riboflavin
(riboflavin reductase [NAD(P)H]) EC 1.5.1.30: flavin reductase (NADPH) EC 1.5.1.31: berberine reductase EC 1.5.1.32: vomilenine reductase EC 1.5.1.33:
List_of_EC_numbers_(EC_1)
Energy-producing metabolic pathway
succinate-CoQ reductase; EC 1.3.5.1) additional electrons are delivered into the quinone pool (Q) originating from succinate and transferred (via flavin adenine
Electron_transport_chain
Enzyme family
Iodotyrosine deiodinase employs a flavin mononucleotide cofactor and belongs to the NADH oxidase/flavin reductase superfamily. In starvation or severe
Deiodinase
Class of enzymes
called orotate reductase (NADH). This enzyme participates in pyrimidine metabolism. It has 2 cofactors: flavin adenine dinucleotide, and flavin mononucleotide
Orotate_reductase_(NADH)
Enzyme
with monooxygenases. Duane W, Hastings JW (January 1975). "Flavin mononucleotide reductase of luminous bacteria". Molecular and Cellular Biochemistry
FMN_reductase_(NADH)
In enzymology, a cob(II)yrinic acid a,c-diamide reductase (EC 1.16.8.1) is an enzyme that catalyzes the chemical reaction 2 cob(I)yrinic acid a,c-diamide
Cob(II)yrinic acid a,c-diamide reductase
Cob(II)yrinic_acid_a,c-diamide_reductase
Protein family
NAD(P)H-dependent flavin reductase domain. Monofunctional chorismate synthase is found in plants and E.coli and lacks a flavin reductase domain. It depends
Chorismate_synthase
Enzyme
(designated as type E). It forms a two-component system with a reductase (StyB, StyA2B). The reductase utilizes solely nicotinamide adenine dinucleotide to reduce
Styrene_monooxygenase
A, Del Campo FF, Ramírez JM, Losada M (September 1965). "Flavin nucleotide nitrate reductase from spinach". Biochimica et Biophysica Acta (BBA) - Biophysics
Nitrate_reductase_(NAD(P)H)
Class of enzymes
which a flavin oxidoreductase partner (EC 1.5.1.37) regenerates FADH2 by oxidizing NADH to NAD+. hpaB and hpaC, the 4-HPA oxygenase and reductase partner
4-Hydroxyphenylacetate 3-monooxygenase
4-Hydroxyphenylacetate_3-monooxygenase
Mammalian protein found in humans
P450 reductase (also known as NADPH:ferrihemoprotein oxidoreductase, NADPH:hemoprotein oxidoreductase, NADPH:P450 oxidoreductase, P450 reductase, POR
Cytochrome_P450_reductase
Class of enzymes
hemoprotein that combines reductase and oxygenase catalytic domains in one dimer, bear both flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN)
Nitric_oxide_synthase
Class of chemical compounds
is done by catalysis using RebH in vitro halogenation and RebF (a flavin reductase) to provide FADH2 for the halogenase. RebO (a tryptophan oxidase) then
Indolocarbazole
Class of enzymes
JT, Peck HD (May 1970). "A flavin-sulfite adduct as an intermediate in the reaction catalyzed by adenylyl sulfate reductase from Desulfovibrio vulgaris"
Adenylyl-sulfate_reductase
Mammalian protein found in humans
24-Dehydrocholesterol reductase is a protein that in humans is encoded by the DHCR24 gene. This gene encodes a flavin adenine dinucleotide (FAD)-dependent
24-Dehydrocholesterol reductase
24-Dehydrocholesterol_reductase
synthases (NRPS) coded by genes XndA and XndB, as well as upstream NADH flavin reductase, and a D-aminopeptidase. The first NRPS (XndA) consists of a condensation
Xenortide
Class of enzymes
In enzymology, a leghemoglobin reductase (EC 1.6.2.6) is an enzyme that catalyzes the chemical reaction NAD(P)H + H+ + 2 ferrileghemoglobin ⇌ {\displaystyle
Leghemoglobin_reductase
Protein family
Flavocytochrome c sulfide dehydrogenase, also known as Sulfide-cytochrome-c reductase (flavocytochrome c) (EC 1.8.2.3), is an enzyme with systematic name
Flavocytochrome c sulfide dehydrogenase
Flavocytochrome_c_sulfide_dehydrogenase
Protein-coding gene in the species Homo sapiens
CR (Feb 2000). "Cloning and characterization of a novel human dual flavin reductase". J Biol Chem. 275 (2): 1471–8. doi:10.1074/jbc.275.2.1471. PMID 10625700
NDOR1
Protein complex involved in cellular respiration
NADH:ubiquinone oxidoreductase (complex I), Coenzyme Q – cytochrome c reductase (complex III), and cytochrome c oxidase (complex IV). Complex I is the
Respiratory_complex_I
American biochemist
freeze-quench EPR methods, as tools to study the mechanisms of enzymes containing flavin, iron, cobalamin, or pyridoxal phosphate cofactors. Many of these studies
David_Ballou
Class of enzymes
12-oxophytodienoate reductase (OPRs) is an enzyme of the family of Old Yellow Enzymes (OYE). OPRs are grouped into two groups: OPRI and OPRII – the second
12-oxophytodienoate_reductase
Protein-coding gene in the species Homo sapiens
Thacker C, et al. (2003). "Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and Hint-related 7meGMP-directed hydrolase, DCS-1". J. Biol
DCPS_(gene)
Class of enzymes
oxygen-insensitive NAD(P)H nitroreductase (flavin mononucleotide-dependent nitroreductase) (6,7-dihydropteridine reductase) (EC 1.5.1.34) and NADH dehydrogenase
Nitroreductase
Protein family
species. Fumarate reductase complexes include four subunits. Subunit A contains the site of fumarate reduction and a covalently bound flavin adenine dinucleotide
Fumarate_reductase_(quinol)
Enzyme family
Sulfite reductases (EC 1.8.99.1) are enzymes that participate in sulfur metabolism. They catalyze the reduction of sulfite to hydrogen sulfide and water
Sulfite_reductase
Chemical compound
in plants that is involved in flavin cofactor production. In some archaea, compound (1) is first acted on by the reductase, 2,5-diamino-6-(ribosylamino
2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine
2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine
Non-protein chemical compound or metallic ion
loosely bound thiamine pyrophosphate (TPP), covalently bound lipoamide and flavin adenine dinucleotide (FAD), cosubstrates nicotinamide adenine dinucleotide
Cofactor_(biochemistry)
Archaeoglobus fulgidus shares structural features with bacterial flavin reductases but lacks sequence similarity, implying convergent evolution or horizontal
Dissimilatory iron reducing bacteria
Dissimilatory_iron_reducing_bacteria
reveal that trypanothione reductase forms homodimers in solution with each of the two individual subunits comprising an flavin adenine dinucleotide-binding
Trypanothione-disulfide reductase
Trypanothione-disulfide_reductase
Enzyme
"Specificities and properties of three reduced pyridine nucleotide-flavin mononucleotide reductases coupling to bacterial luciferase". Molecular and Cellular Biochemistry
FMN_reductase_(NAD(P)H)
Enzyme
Succinate dehydrogenase (SDH) - succinate-coenzyme Q reductase (SQR) - respiratory complex II is an enzyme complex, found in many bacterial cells and
Succinate_dehydrogenase
Protein-coding gene in the species Homo sapiens
Thioredoxin reductase 1, cytoplasmic is an enzyme that in humans is encoded by the TXNRD1 gene. This gene encodes a member of the family of pyridine nucleotide
TXNRD1
Flavodoxins contain a singular Flavin mononucleotide, also known as FMN. This motif is present for example in Cytochrome P450 reductase, lactate dehydrogenase
Flavodoxin_fold
which follows the enzymes, nitrite reductase and glutamine synthase. An ammonium produced by the nitrite reductase reaction will be incorporated into
Glutamate_synthase_(NADH)
Class of enzymes
oxidizes a substrate by reducing an electron acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN. Like all catalysts, they catalyze reverse as
Dehydrogenase
Protein family
cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases". Biochemistry. 32 (43):
Glucose-methanol-choline oxidoreductase family
Glucose-methanol-choline_oxidoreductase_family
oxidoreductase. Other names in common use include menadione reductase, phylloquinone reductase, quinone reductase, dehydrogenase, reduced nicotinamide adenine dinucleotide
NAD(P)H dehydrogenase (quinone)
NAD(P)H_dehydrogenase_(quinone)
Class of enzymes
In enzymology, a 2-methyl-branched-chain-enoyl-CoA reductase (EC 1.3.8.5) is an enzyme that catalyzes the chemical reaction 2-methylbutanoyl-CoA + electron
2-methyl-branched-chain-enoyl-CoA reductase
2-methyl-branched-chain-enoyl-CoA_reductase
Family of enzymes
and was named tyramine oxidase. The MAOs belong to the protein family of flavin-containing amine oxidoreductases. MAOs are important in the breakdown of
Monoamine_oxidase
Class of enzymes
oxidised NADP+, water, and nitrous acid. It is a flavoprotein that uses flavin adenine dinucleotide as a cofactor. Zhang JJ, Liu H, Xiao Y, Zhang XE, Zhou
4-Nitrophenol_4-monooxygenase
Active region of an enzyme
properly. One example of the coenzyme is Flavin. It contains a distinct conjugated isoalloxazine ring system. Flavin has multiple redox states and can be
Active_site
Metabolic pathway
addition to ubiquinone. Within proteins, electrons are transferred between flavin cofactors, iron–sulfur clusters and cytochromes. There are several types
Oxidative_phosphorylation
Protein-coding gene in the species Homo sapiens
NADH-cytochrome b5 reductase 3 is an enzyme that in humans is encoded by the CYB5R3 gene. The CYB5R3 gene is located on the 22nd chromosome, with its
CYB5R3
Bangladeshi scientist, writer, and politician
1985 for the research paper entitled, 'Monodehydroascorbate reductase from cucumber is a flavin adenine dinucleotide enzyme' which was adjudged as the best
M._Anwar_Hossain
Iron–sulfur proteins
ferredoxin is the last electron acceptor thus reducing the enzyme NADP+ reductase. It accepts electrons produced from sunlight-excited chlorophyll and transfers
Ferredoxin
ubiquinone dihydroxyacetone phosphate + ubiquinol This flavin-dependent dehydrogenase is a membrane enzyme. It participates in glycolysis
Glycerol-3-phosphate dehydrogenase (quinone)
Glycerol-3-phosphate_dehydrogenase_(quinone)
Chemical compound
attached via a 2-phospho-L-lactate bridge. F420 is so named because it is a flavin derivative with an absorption maximum at 420 nm. F420 was originally discovered
Coenzyme_F420
Class of enzymes
oxidised NAD+, water, and nitrous acid. It is a flavoprotein that uses flavin adenine dinucleotide as a cofactor. Kadiyala V, Spain JC (July 1998). "A
4-Nitrocatechol 4-monooxygenase
4-Nitrocatechol_4-monooxygenase
Biochemical cofactor and antioxidant
ubiquinone reductase (complex I), and succinate ubiquinone reductase (complex II), the fatty acids and branched-chain amino acids oxidation (through flavin-linked
Coenzyme_Q10
Large biological molecule that acts as a catalyst
and adenosine triphosphate (ATP). Some coenzymes, such as flavin mononucleotide (FMN), flavin adenine dinucleotide (FAD), thiamine pyrophosphate (TPP)
Enzyme
Enzyme Commission (EC) numbering system: Dehydrogenase Luciferase DMSO reductase Category:EC 1.1.1 (with NAD+ or NADP+ as acceptor) Alcohol Dehydrogenase
List_of_enzymes
Post-translational modification
farnesyl pyrophosphate are products of the HMG-CoA reductase pathway. The product of HMG CoA reductase is mevalonate. By combining precursors with 5 carbons
Prenylation
Mammalian protein found in Homo sapiens
This enzyme contains a loosely bound FAD flavin and obtains electrons from NADPH-cytochrome P450 reductase, rather than binding NADPH directly. The alternative
Squalene_monooxygenase
menaquinone, followed by a transfer of electrons to fumarate reductase or nitrate reductase. Especially for proteins that contain more than one disulfide
Oxidative_folding
Enzyme
4-dichlorobenzoate degradation. It is an Iron-sulfur protein which uses flavin mononucleotide as a cofactor. Enzyme 1.14.12.7 at KEGG Pathway Database
Phthalate_4,5-dioxygenase
Class of enzymes
catalyzes the phosphorylation of riboflavin into flavin mononucleotide (FMN) and the adenylylation of FMN into flavin adenine dinucleotide (FAD). It consists of
Prokaryotic riboflavin biosynthesis protein
Prokaryotic_riboflavin_biosynthesis_protein
Medical condition
caused by deficiency of cytochrome P450 oxidoreductase (POR). POR is a 2-flavin protein that is responsible for the transfer of electrons from NADPH to
Cytochrome P450 oxidoreductase deficiency
Cytochrome_P450_oxidoreductase_deficiency
Functional group of organic compounds
crotonyl-coenzyme A. They arise by the action of acyl-CoA dehydrogenases. Flavin adenine dinucleotide (FAD) is a required co-factor. Since α,β-unsaturated
Α,β-Unsaturated carbonyl compound
Α,β-Unsaturated_carbonyl_compound
Use of natural catalysts to perform chemical transformations
Hydrogen Atom Transfer: Discovery of Catalytic Promiscuity in Flavin-Dependent 'Ene'-Reductases". Journal of the American Chemical Society. 139 (33): 11313–11316
Biocatalysis
Chemical compound
methyl-THMPT (5-CH3-H 4MPT), catalyzed by F420-dependent methylene-THMPT reductase. 5-Methyl-THMPT is the methyl donor to coenzyme M, a conversion mediated
Tetrahydromethanopterin
Protein-coding gene in the species Homo sapiens
reductase activity oxidoreductase activity growth factor activity protein binding thiol oxidase activity flavin adenine dinucleotide binding flavin-linked
GFER
Protein-coding gene in the species Homo sapiens
Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred
NDUFA9
Human chromosome
kinase 6 MEAF6: MYST/ESA1 associated factor 6 MECR: Trans-2-enoyl-CoA reductase, mitochondrial MFAP2: Microfibrillar-associated protein 2 MIB2 (1p36)
Chromosome_1
Class of plant-based pigments
Schubert M, Smythe C (1 December 1936). "Potentiometric Study of the Flavins". J. Biol. Chem. 116 (2): 587–607. doi:10.1016/S0021-9258(18)74634-6. Jack
Anthocyanin
in the following steps: (i) thioredoxin reductase transfers electrons from NADPH to thioredoxin via a flavin carrier (ii) glutaredoxin is also able to
Oxidation_response
Covalently bonded non-protein part of an enzyme
complex IV of the respiratory chain) and molybdenum (for example in nitrate reductase). The table below contains a list of some of the most common prosthetic
Prosthetic_group
Class of enzymes
sequential action of a ketoreductase (KR), dehydratase (DH), and enoyl reductase (ER). The growing fatty acid chain is carried between these active sites
Fatty_acid_synthase
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FLAVIN REDUCTASE
FLAVIN REDUCTASE
FLAVIN REDUCTASE
FLAVIN REDUCTASE
FLAVIN REDUCTASE
FLAVIN REDUCTASE
FLAVIN REDUCTASE
FLAVIN REDUCTASE
FLAVIN REDUCTASE
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