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Information on EC 1.14.13.8 - flavin-containing monooxygenase and Organism(s) Schizosaccharomyces pombe and UniProt Accession Q9HFE4

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IUBMB Comments
A flavoprotein. A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines [3,4]. This enzyme is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate [4,5]. This microsomal enzyme generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites. For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) [2,6]
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Schizosaccharomyces pombe
UNIPROT: Q9HFE4
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The taxonomic range for the selected organisms is: Schizosaccharomyces pombe
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
fmo, flavin-containing monooxygenase, flavin monooxygenase, flavin-dependent monooxygenase, flavin-containing monooxygenase 3, fad-containing monooxygenase, flavoprotein monooxygenase, hfmo3, flavin-containing mono-oxygenase, flavin-containing monooxygenase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimethylaniline monooxygenase (N-oxide-forming)
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dimethylaniline N-oxidase
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dimethylaniline oxidase
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DMA oxidase
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FAD-containing monooxygenase
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flavin monooxygenase
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flavin-containing monooxygenase
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FMO
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FMO 1A1
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FMO 1B1
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FMO 1C1
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FMO 1D1
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FMO 1E1
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FMO-I
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FMO-II
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FMO1
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FMO2
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FMO3
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FMO5
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mixed-function amine oxidase
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N,N-dimethylaniline monooxygenase
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oxygenase, dimethylaniline mono- (N-oxide-forming)
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oxygenase, methylphenyltetrahydropyridine N-mono-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
show the reaction diagram
catalytic reaction mechanism via 4alpha-hydroperoxyflavin transient intermediate
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
N,N-dimethylaniline,NADPH:oxygen oxidoreductase (N-oxide-forming)
A flavoprotein. A broad spectrum monooxygenase that accepts substrates as diverse as hydrazines, phosphines, boron-containing compounds, sulfides, selenides, iodide, as well as primary, secondary and tertiary amines [3,4]. This enzyme is distinct from other monooxygenases in that the enzyme forms a relatively stable hydroperoxy flavin intermediate [4,5]. This microsomal enzyme generally converts nucleophilic heteroatom-containing chemicals and drugs into harmless, readily excreted metabolites. For example, N-oxygenation is largely responsible for the detoxification of the dopaminergic neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) [2,6]
CAS REGISTRY NUMBER
COMMENTARY hide
117910-56-2
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148848-55-9
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37256-46-5
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37256-73-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
methimazole + NADPH + O2
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show the reaction diagram
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
methimazole + NADPH + O2
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show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
the prosthetic group FAD is an integral part of the protein, the active FMO exists in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor, binding structure, overview
NADPH
dependent on, the active FMO exists in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor, binding structure, overview
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in complex with FAD, and NADPH or methimazole, sitting drop vapor diffusion method, purified protein in 10 mM HEPES, pH 7.0, and 150 mM NaCl, versus reservoir solution containing 20% PEG 4000, 0.1 M sodium citrate buffer, pH 5.8, and 1,6-diaminohexane, cryoprotection by 10% v/v glycerol, X-ray diffraction structure determination and analysis at 2.1-2.4 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eswaramoorthy, S.; Bonanno, J.B.; Burley, S.K.; Swaminathan, S.
Mechanism of action of a flavin-containing monooxygenase
Proc. Natl. Acad. Sci. USA
103
9832-9837
2006
Schizosaccharomyces pombe (Q9HFE4), Schizosaccharomyces pombe
Manually annotated by BRENDA team