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See searches and references containing FMN REDUCTASE!FMN REDUCTASE
Enzyme
enzymology, an FMN reductase (EC 1.5.1.29) is an enzyme that catalyzes the chemical reaction FMNH2 + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } FMN + NAD(P)H
FMN_reductase
Enzyme
FMN reductase (NADH) (EC 1.5.1.42, NADH-FMN reductase) is an enzyme with systematic name FMNH2:NAD+ oxidoreductase. This enzyme catalyses the following
FMN_reductase_(NADH)
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)
Enzyme
FMN reductase (NAD(P)H) (EC 1.5.1.39, FRG) is an enzyme with systematic name FMNH2:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical
FMN_reductase_(NAD(P)H)
mononucleotide (FMN) reductase, FMN reductase (NADPH), NADPH-dependent FMN reductase, NADPH-flavin reductase, NADPH-FMN reductase, NADPH-specific FMN reductase, NADPH2
Flavin_reductase
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
biosynthesis. Morphinone reductase is a dimeric flavoenzyme comprising two 8-fold α/β-barrel domains, each with a non-covalently bound FMN prosthetic group located
Morphinone_reductase
Riboflavin reductase (NAD(P)H) (EC 1.5.1.41, NAD(P)H-FMN reductase, Fre) is an enzyme with systematic name riboflavin:NAD(P)+ oxidoreductase. This enzyme
Riboflavin reductase (NAD(P)H)
Riboflavin_reductase_(NAD(P)H)
Enzyme with systematic name hydrogen-sulfide:NADP+ oxidoreductase
\rightleftharpoons } sulfite + 3 NADPH + 3 H+ Sulfite reductase is an iron flavoprotein (FAD and FMN). Hilz H, Kittler M, Knape G (1959). "[The reduction
Sulfite_reductase_(NADPH)
Topics referred to by the same term
1990–present) West Germany (the Federal Republic of Germany, 1949–1990) FMN reductase (NAD(P)H) Friendship Radiosport Games Functional renormalization group
FRG
Group of chemical compounds
of a bond between a cysteine residue in its peptide sequence and a bound FMN. The biochemical source of flavin is the yellow B vitamin riboflavin. The
Flavin_group
Protein-coding gene in the species Homo sapiens
apparent K(m) of 2.5 μM for the ferric iron. The ferric reductase reaction requires NAD(P)H and FMN. This activity is intriguing, as haem cleavage in the
Biliverdin_reductase_B
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)
Index of enzymes associated with the same name
Riboflavin:NAD(P)+ oxidoreductase may refer to: Riboflavin reductase (NAD(P)H), a riboflavin reduction enzyme FMN reductase, a flavin mononucleotide reduction enzyme This
Riboflavin:NAD(P)+ oxidoreductase
Riboflavin:NAD(P)+_oxidoreductase
Coenzyme
cytochrome P-450 reductase (CPR) that contains both an FAD and an FMN. The two electrons on reduced FAD (FADH2) are transferred one at a time to FMN and then
Flavin_adenine_dinucleotide
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
EC 1.5.1.36: flavin reductase (NADH) EC 1.5.1.37: FAD reductase (NADH) EC 1.5.1.38: FMN reductase (NADPH) EC 1.5.1.39: FMN reductase (NAD(P)H) EC 1.5.1
List_of_EC_numbers_(EC_1)
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 + FMN + 3 H+ ⇌ {\displaystyle
Cob(II)yrinic acid a,c-diamide reductase
Cob(II)yrinic_acid_a,c-diamide_reductase
Vitamin
activity of glutathione reductase, an essential enzyme in the formation of the endogenous antioxidant, glutathione. Riboflavin, FMN, and FAD are involved
Riboflavin
Protein family
some of the most-studied families of enzymes. Flavoproteins have either FMN (flavin mononucleotide) or FAD (flavin adenine dinucleotide) as a prosthetic
Flavoprotein
mononucleotide (FMN) cofactor. Ferric reductases are present in some unicellular eukaryotes, including pathogenic yeast which utilize ferric reductases during
Ferric-chelate_reductase
Class of enzymes
Nitrate reductases are molybdoenzymes that reduce nitrate (NO− 3) to nitrite (NO− 2). This reaction is critical for the production of protein in most crop
Nitrate_reductase
Enzyme
(1997). "Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes". Proc. Natl. Acad. Sci. U.S.A. 94
NADPH—hemoprotein_reductase
Class of enzymes
2,4 Dienoyl-CoA reductase also known as DECR1 is an enzyme which in humans is encoded by the DECR1 gene which resides on chromosome 8. This enzyme catalyzes
2,4_Dienoyl-CoA_reductase
Protein complex involved in cellular respiration
flavin mononucleotide (FMN) prosthetic group of the enzyme, creating FMNH2. The electron acceptor – the isoalloxazine ring – of FMN is identical to that
Respiratory_complex_I
Class of enzymes
Shimizu S, Yamada H (1992). "Purification and characterization of a novel FMN-dependent enzyme Membrane-bound L-(+)-pantoyl lactone dehydrogenase from
(R)-pantolactone dehydrogenase (flavin)
(R)-pantolactone_dehydrogenase_(flavin)
Class of enzymes
mononucleotide (FMN) that is non-covalently bonded to the enzyme and their catalytic mechanism is now well understood. In the natural cycle, the cofactor (FMN) is
Ene-reductase
Class of enzymes
systems which employ adrenodoxin reductase and adrenodoxin (a ferrodoxin) to transfer electrons from NADPH to P450. FMN/Fd/P450 systems: originally found
Cytochrome_P450
singular Flavin mononucleotide, also known as FMN. This motif is present for example in Cytochrome P450 reductase, lactate dehydrogenase (PDB: 1A5Z), phosphoglycerate
Flavodoxin_fold
Metabolic pathway
prosthetic group attached to the complex, flavin mononucleotide (FMN). The addition of electrons to FMN converts it to its reduced form, FMNH2. The electrons are
Oxidative_phosphorylation
Protein family
plants and E.coli and lacks a flavin reductase domain. It depends on a separate reductase enzyme to reduce the FMN. PDB: 1ZTB Dias; et al. (2006). "Structure
Chorismate_synthase
Class of enzymes
mononucleotide (FMN) and the adenylylation of FMN into flavin adenine dinucleotide (FAD). It consists of a C-terminal riboflavin kinase and an N-terminal FMN-adenylyltransferase
Prokaryotic riboflavin biosynthesis protein
Prokaryotic_riboflavin_biosynthesis_protein
Class of enzymes
multi-domain C-terminal reductase, which is homologous to NADPH:cytochrome P450 reductase (EC 1.6.2.4) and other flavoproteins. The FMN binding domain is homologous
Nitric_oxide_synthase
is fused to the reductase domain that shows sequence similarity to phthalate dioxygenase reductase and consists, in its turn, of FMN-binding domain and
P450-containing_systems
Class of enzymes
Azobenzene reductase also known as azoreductase (EC 1.7.1.6) is an enzyme that catalyzes the chemical reaction: 4-(dimethylamino)azobenzene + 2 NADPH
Azobenzene_reductase
Genus of Gram-positive bacteria
preQ1(34)S-adenosylmethionine ribosyltransferase-isomerase QueA, DNA primase, FMN reductase (NADPH), UvrABC system protein C, sensor histidine kinase YycG, hypothetical
Metalysinibacillus
Class of enzymes
monooxygenases use NADH or NADPH as substrates (and use the flavins FAD or FMN as prosthetic groups), this enzyme is part of a two-component system, in
4-Hydroxyphenylacetate 3-monooxygenase
4-Hydroxyphenylacetate_3-monooxygenase
Marine bacterium
Bioluminescence in bacteria is due to the reaction: FMNH− + H+ + RCHO + O2 → FMN + RCOOH + H2O + hν and is catalyzed by the enzyme luciferase. A new luciferase
Vibrio_campbellii
– testosterone 5-alpha-Reductase MeSH D08.811.682.662.162 – dihydropteridine reductase MeSH D08.811.682.662.171 – FMN reductase MeSH D08.811.682.662.217
List_of_MeSH_codes_(D08)
Chemical compound
biosynthesis pathway. Riboflavin is later used to produce flavin cofactors such as FMN and FAD. In rice, this part of the pathway involves bifunctional RibA proteins
2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine
2,5-Diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine
Chemical compound
Ostreococcus tauri also use Coenzyme FO. F420 is structurally similar to FMN, but catalytically it is similar to NAD and NADP: it has low redox potential
Coenzyme_F420
system, phthalate dioxygenase reductase (PDR) has the same function. PDR is a single protein comprising FMN-binding reductase and plant-type ferredoxin domains
Aromatic-ring-hydroxylating dioxygenases
Aromatic-ring-hydroxylating_dioxygenases
Class of enzymes
electron acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN. Like all catalysts, they catalyze reverse as well as forward reactions,
Dehydrogenase
Class of enzymes
cofactors (FAD and FMN) by the actions of riboflavin kinase, which converts it into FMN, and FAD synthetase (EC 2.7.7.2), which adenylates FMN to FAD. Eukaryotes
Riboflavin_kinase
Class of photoreceptor proteins in plants
regulated domains (LOV1, LOV2) that each bind flavin mononucleotide (FMN). The FMN is noncovalently bound to a LOV domain in the dark, but becomes covalently
Phototropin
Protein-coding gene in the species Homo sapiens
of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1". Eur J Biochem. 270 (6):
NDOR1
Mammalian protein found in humans
single domain flavodoxin protein. The reductase protein is responsible for transfer of an electron from a reduced FMN cofactor to the inactive Cob(II), which
Methionine_synthase
American biochemist
(1997-08-05). "Three-dimensional structure of NADPH–cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes". Proceedings of the National Academy
Bettie_Sue_Masters
Protein-coding gene in the species Homo sapiens
contain only one flavin mononucleotide (FMN) in each dimer, but now iodotyrosine deiodinase is believed to have two FMN molecules for each homodimer. The enzyme
Iodotyrosine_deiodinase
Bacteria that produce light through chemiluminescence
-> FMN + H2O + R-COOH + Light (~ 495 nm) Molecular oxygen reacts with FMNH2 (reduced flavin mononucleotide) and a long-chain aldehyde to produce FMN (flavin
Bioluminescent_bacteria
Human chromosome
CREBZF encoding protein CREB/ATF bZIP transcription factor DAK: Triokinase/FMN cyclase DDI1: encoding protein DNA-damage inducible 1 homolog 1 (S. cerevisiae)
Chromosome_11
acting on NADH or NADPH with other acceptors. It has 2 cofactors: FAD, and FMN. The systematic name of this enzyme class is NADPH:acceptor oxidoreductase
NADPH_dehydrogenase
Species of bacterium
comprising a reductase module similar to the one of Complex I. The [Ni-Fe] active site oxidized hydrogen gas which transfers electrons to a FMN-a cofactor
Cupriavidus_necator
Chemical compound acting as a vitamin
tetrahydrofolate, a second biologically active vitamer, by dihydrofolate reductase. The liver has a limited capacity to metabolize folic acid into tetrahydrofolate
Vitamer
Protein-coding gene in the species Homo sapiens
transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series
NDUFA9
Species of bacterium
by diatomic oxygen. The reaction is summarized as: FMNH2 + O2 + R-CHO → FMN + R-COOH + H2O + light. The reduced flavin mononucleotide (FMNH) is provided
Aliivibrio_fischeri
Enzyme family
flavin mononucleotide cofactor and belongs to the NADH oxidase/flavin reductase superfamily. In starvation or severe somatic stress, deiodinase type 1
Deiodinase
1997). "Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes". Proceedings of the National Academy
Cytochrome P450 aromatic O-demethylase
Cytochrome_P450_aromatic_O-demethylase
Chemical compound
oxide synthases. Chemically, its structure is that of a (dihydropteridine reductase) reduced pteridine derivative (quinonoid dihydrobiopterin).[citation needed]
Tetrahydrobiopterin
Large biological molecule that acts as a catalyst
adenosine triphosphate (ATP). Some coenzymes, such as flavin mononucleotide (FMN), flavin adenine dinucleotide (FAD), thiamine pyrophosphate (TPP), and tetrahydrofolate
Enzyme
Mitochondrial gene coding for a protein involved in the respiratory chain
transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series
MT-ND4
Non-protein chemical compound or metallic ion
pterins (a derivative of vitamin B9), flavins (FAD, flavin mononucleotide = FMN), and riboflavin (vitamin B2). Changes in coenzymes. A computational method
Cofactor_(biochemistry)
Mitochondrial gene coding for a protein involved in the respiratory chain
transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series
MT-ND1
Protein-coding gene in humans
(February 2016). "Cytochrome P450 17A1 Interactions with the FMN Domain of Its Reductase as Characterized by NMR". The Journal of Biological Chemistry
CYP17A1
Protein and coding gene in humans
constituted by a reductase domain, which displays binding sites for nicotinamide adenine dinucleotide phosphate (NADPH), flavin mononucleotide (FMN), and flavin
Endothelial_NOS
Functions of nitric oxide in organisms
nitrate-nitrite-nitric oxide pathway, the reduction of nitrate to nitrite (by nitrate reductase, a bacterial enzyme) occurs in the mouth, by commensal bacteria, an obligatory
Biological functions of nitric oxide
Biological_functions_of_nitric_oxide
Chemical compound or substance produced by a living organism, found in nature
from ribulose 5-phosphate and guanosine triphosphate, is a precursor to FMN and FAD, which are crucial for various redox reactions. Vitamin B3 (nicotinic
Natural_product
Protein-coding gene in the species Homo sapiens
electron donors: flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), NADPH, and tetrahydrobiopterin. It has been implicated in asthma, schizophrenia
NOS1
The anion form of nitrogen dioxide
described, including enzymatic reduction by xanthine oxidoreductase, nitrite reductase, and NO synthase (NOS), as well as nonenzymatic acidic disproportionation
Nitrite
Polyatomic ion (NO3, charge –1) found in explosives and fertilisers
drink more water per body weight, they have a lower NADH-cytochrome b5 reductase activity, and they have a higher level of fetal hemoglobin which converts
Nitrate
Membrane proteins that adhere temporarily to membranes with which they are associated
1016/s0969-2126(00)00077-0. ISSN 0969-2126. PMID 10673429. "Pfam entry: FMN-dependent dehydrogenase". Archived from the original on 2007-09-29. Retrieved
Peripheral_membrane_protein
Protein kinase
Precursors: L-Arginine Nω-Hydroxy-L-arginine (NOHA) Cofactors: NADPH FAD FMN Heme BH4 CaM O2 Ca2+ Indirect/downstream NO modulators: ACE inhibitors/AT-II
CGMP-dependent_protein_kinase
Protein-coding gene in the species Homo sapiens
data BioGPS More reference expression data Gene ontology Molecular function FMN binding protein homodimerization activity flavin adenine dinucleotide binding
Nitric oxide synthase 2 (inducible)
Nitric_oxide_synthase_2_(inducible)
EC 2.7.1.179: kanosamine kinase EC 2.7.1.180: FAD:protein FMN transferase EC 2.7.1.181: polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol
List_of_EC_numbers_(EC_2)
Chemical compound
oxide synthases can react with glutathione to form GSNO. The enzyme GSNO reductase (GSNOR) reduces S-nitrosoglutathione (GSNO) to an unstable intermediate
S-Nitrosoglutathione
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FMN REDUCTASE
FMN REDUCTASE
FMN REDUCTASE
FMN REDUCTASE
FMN REDUCTASE
FMN REDUCTASE
FMN REDUCTASE
FMN REDUCTASE
FMN REDUCTASE
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