Information on EC 1.14.14.39 - isoleucine N-monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.14.39
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RECOMMENDED NAME
GeneOntology No.
isoleucine N-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = (1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
show the reaction diagram
overall reaction
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L-isoleucine + [reduced NADPH-hemoprotein reductase] + O2 = N-hydroxy-L-isoleucine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
(1a)
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N,N-dihydroxy-L-isoleucine = (1E,2S)-2-methylbutanal oxime + CO2 + H2O
show the reaction diagram
spontaneous
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N-hydroxy-L-isoleucine + [reduced NADPH-hemoprotein reductase] + O2 = N,N-dihydroxy-L-isoleucine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
(1b)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Cyanoamino acid metabolism
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Glucosinolate biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
L-isoleucine,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
This cytochrome P-450 (heme-thiolate) enzyme, found in plants, catalyses two successive N-hydroxylations of L-isoleucine, the committed step in the biosynthesis of the cyanogenic glucoside lotaustralin. The product of the two hydroxylations, N,N-dihydroxy-L-isoleucine, is labile and undergoes dehydration followed by decarboxylation, producing the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The enzyme can also accept L-valine, but with a lower activity. cf. EC 1.14.14.38, valine N-monooxygenase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cf. EC 1.14.14.38
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-isoleucine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
show the reaction diagram
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
show the reaction diagram
higher catalytic efficiency with L-Ile as substrate than with L-Val, in agreement with lotaustralin and rhodiocyanoside A and D being the major cyanogenic and nitrile glucosides in Lotus japonicus
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?
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
show the reaction diagram
higher catalytic efficiency with L-Ile as substrate than with L-Val, in agreement with lotaustralin and rhodiocyanoside A and D being the major cyanogenic and nitrile glucosides in Lotus japonicus
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?
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 1.8
L-isoleucine
1.7 - 2.6
L-valine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 3.67
L-isoleucine
0.73 - 0.83
L-valine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 2.85
L-isoleucine
0.32 - 0.43
L-valine
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 61200, calculated, x * 62000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
recombinant protein expressed in Pichia pastoris is glycosylated
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris; expression in Pichia pastoris
expression in Saccharomyces cerevisiae; expression in Saccharomyces cerevisiae