Information on EC 1.14.13.117 - isoleucine N-monooxygenase

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The expected taxonomic range for this enzyme is: Lotus japonicus

EC NUMBER
COMMENTARY hide
1.14.13.117
-
RECOMMENDED NAME
GeneOntology No.
isoleucine N-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-isoleucine + 2 O2 + 2 NADPH + 2 H+ = (E)-2-methylbutanal oxime + 2 NADP+ + CO2 + 3 H2O
show the reaction diagram
overall reaction
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L-isoleucine + O2 + NADPH + H+ = N-hydroxy-L-isoleucine + NADP+ + H2O
show the reaction diagram
(1a)
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N,N-dihydroxy-L-isoleucine = (E)-2-methylbutanal oxime + CO2 + H2O
show the reaction diagram
spontaneous
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N-hydroxy-L-isoleucine + O2 + NADPH + H+ = N,N-dihydroxy-L-isoleucine + NADP+ + H2O
show the reaction diagram
(1b)
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-
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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,NADPH:oxygen oxidoreductase (N-hydroxylating)
A heme-thiolate protein (P-450). This enzyme catalyses two successive N-hydroxylations of L-isoleucine, the first committed steps in the biosynthesis of the cyanogenic glucoside lotaustralin in the plant Lotus japonicus. The product of the two hydroxylations, N,N-dihydroxy-L-isoleucine, is extremely labile and dehydrates spontaneously. The dehydrated product is then subject to a decarboxylation that produces the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The product, (E)-2-methylbutanal oxime, undergoes a spontaneous isomerization to the (Z) form. The enzyme can also accept L-valine as substrate, with a lower activity. It is different from EC 1.14.13.118 (valine N-monooxygenase), which prefers L-valine.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme is part of the biosynthetic pathway leading to nitrile glucosides rhodiocyanoside A and rhodiocyanoside D as well as the cyanogenic glucosides linamarin and lotaustralin. Lotaustralin, rhodiocyanoside A, and rhodiocyanoside D are derived from the amino acid L-Ile, whereas linamarin is derived from L-Val; enzyme is part of the biosynthetic pathway leading to nitrile glucosides rhodiocyanoside A and rhodiocyanoside D as well as the cyanogenic glucosides linamarin and lotaustralin. Lotaustralin, rhodiocyanoside A, and rhodiocyanoside D are derived from the amino acid L-Ile, whereas linamarin is derived from L-Val
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 NADPH + 2 H+
(E)-2-methylbutanal oxime + 2 NADP+ + 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 O2 + 2 NADPH + 2 H+
(E)-2-methylpropanal oxime + 2 NADP+ + 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
2 - 3.67
L-isoleucine
0.73 - 0.83
L-valine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.03 - 2.85
L-isoleucine
311
0.32 - 0.43
L-valine
246
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
apical leaf, highest enzymic activity among the tissues tested. Also present in the second leaf from top, no transcripts in older leaves
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae; expression in Saccharomyces cerevisiae