Information on EC 1.14.14.30 - isobutylamine N-monooxygenase

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The expected taxonomic range for this enzyme is: Streptomyces viridifaciens

EC NUMBER
COMMENTARY hide
1.14.14.30
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RECOMMENDED NAME
GeneOntology No.
isobutylamine N-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-methylpropan-1-amine + FADH2 + O2 = N-(2-methylpropanoyl)hydroxylamine + FAD + H2O
show the reaction diagram
(1)
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2-methylpropan-1-amine + FMNH2 + O2 = N-(2-methylpropanoyl)hydroxylamine + FMN + H2O
show the reaction diagram
(2)
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SYSTEMATIC NAME
IUBMB Comments
2-methylpropan-1-amine,FADH2:O2 N-oxidoreductase
The enzyme, characterized from the bacterium Streptomyces viridifaciens, is part of a two component system that also includes a flavin reductase, which provides reduced flavin mononucleotide for this enzyme. The enzyme, which is involved in the biosynthesis of the azoxy antibiotic valanimycin, has a similar activity with either FMNH2 or FADH2. It exhibits broad specificity, and also accepts propan-1-amine, butan-1-amine, butan-2-amine and benzylamine.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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oxidation of isobutylamine to isobutylhydroxylamine is catalyzed by a two-component enzyme system consisting of isobutylamine hydroxylase vlmH, and flavin reductase vlmR. In combination with isobutylamine hydroxylase, flavin reductase catalyzes the conversion of isobutylamine to isobutylhydroxylamine. The flavin reductase protein utilizes FAD and NADPH in preference to FMN, riboflavin, and NADH
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-butylamine + FADH2 + O2
N-(2-butyl)hydroxylamine + FAD + H2O
show the reaction diagram
2-methylpropanamine + FADH2 + O2
N-hydroxy-2-methylpropan-1-amine + FAD + H2O
show the reaction diagram
2-methylpropanamine + FMNH2 + O2
N-hydroxy-2-methylpropan-1-amine + FMN + H2O
show the reaction diagram
benzylamine + FADH2 + O2
N-(benzyl)hydroxylamine + FAD + H2O
show the reaction diagram
n-butylamine + FADH2 + O2
N-(butyl)hydroxylamine + FAD + H2O
show the reaction diagram
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87% of the activity with 2-methylpropanamine
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?
propan-1-amine + FADH2 + O2
N-(propyl)hydroxylamine + FAD + H2O
show the reaction diagram
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125% of the activity with 2-methylpropanamine
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-methylpropanamine + FADH2 + O2
N-hydroxy-2-methylpropan-1-amine + FAD + H2O
show the reaction diagram
2-methylpropanamine + FMNH2 + O2
N-hydroxy-2-methylpropan-1-amine + FMN + H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51.1
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pH 7.5, 30°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
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isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
73000
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gel filtration, 100 mM NarTes (pH 7.5)
112000
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gel filtration, 100 mM sodium phosphate buffer (pH 7.5)
126000
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gel filtration, 50 mM sodium phosphate buffer (pH 7.0) containing 15% (w/v) glycerol
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE