Information on EC 1.14.14.38 - valine N-monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.14.38
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RECOMMENDED NAME
GeneOntology No.
valine N-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
overall reaction
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-
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L-valine + [reduced NADPH-hemoprotein reductase] + O2 = N-hydroxy-L-valine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
(1a)
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-
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N,N-dihydroxy-L-valine = (E)-2-methylpropanal oxime + CO2 + H2O
show the reaction diagram
spontaneous
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-
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N-hydroxy-L-valine + [reduced NADPH-hemoprotein reductase] + O2 = N,N-dihydroxy-L-valine + [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-valine,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses two successive N-hydroxylations of L-valine, the committed step in the biosynthesis of the cyanogenic glucoside linamarin in Manihot esculenta (cassava). The product of the two hydroxylations, N,N-dihydroxy-L-valine, is labile and undergoes dehydration and decarboxylation that produce the (E) isomer of the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The enzyme can also accept L-isoleucine as substrate, with a lower activity. It is different from EC 1.14.14.39, isoleucine N-monooxygenase, which prefers L-isoleucine.
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 [reduced NADPH-hemoprotein reductase] + 2 O2
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
show the reaction diagram
L-isoleucine + O2 + NADPH + H+
(Z)-2-methylbutanal oxime + NADP+ + CO2 + H2O
show the reaction diagram
-
-
-
?
L-valine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
show the reaction diagram
L-valine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O (overall reaction)
show the reaction diagram
-
-
-
?
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
L-valine + O2 + NADPH + H+
(Z)-2-methylpropanal oxime + NADP+ + CO2 + H2O
show the reaction diagram
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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
L-isoleucine + O2 + NADPH + H+
(Z)-2-methylbutanal oxime + NADP+ + CO2 + H2O
show the reaction diagram
Q9M7B7, Q9M7B8
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-
-
?
L-valine + O2 + NADPH + H+
(Z)-2-methylpropanal oxime + NADP+ + CO2 + H2O
show the reaction diagram
Q9M7B7, Q9M7B8
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-
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphenyleneiodonium chloride
;
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
L-isoleucine
pH 7.9, 30C
1.7 - 2.6
L-valine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.103
L-isoleucine
pH 7.9, 30C
0.16 - 1.23
L-valine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
L-isoleucine
pH 7.9, 30C
0.074 - 0.43
L-valine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.9
assay at; assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at; assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
exclusively expressed in aerial parts
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
x * 62000, SDS-PAGE and calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 61200, calculated, x * 62000, SDS-PAGE; x * 62000, SDS-PAGE and calculated
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
glycosylation of the asparagine residues at the N-terminus; recombinant protein expressed in Pichia pastoris is glycosylated
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, reconstitution in lipid micelles; recombinant enzyme, reconstitution in lipid micelles
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Arabidopsis thaliana
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expression in Lotus japonicus
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expression in Pichia pastoris; expression in Pichia pastoris
expression in Saccharomyces cerevisiae; expression in Saccharomyces cerevisiae
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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expression of CYP79D2 from cassava in Arabidopsis thaliana results in the production of valine- and isoleucine-derived glucosinolates not normally found in this ecotype. The transgenic lines show no morphological phenotype, and the level of endogenous glucosinolates is not affected. The novel glucosinolates constitute up to 35% of the total glucosinolate content in mature rosette leaves and up to 48% in old leaves. At increased concentrations of these glucosinolates, the proportion of Val-derived glucosinolates decreases. As the isothiocyanates produced from the Val- and isoleucine-derived glucosinolates are volatile, metabolically engineered plants producing these glucosinolates have acquired novel properties with great potential for improvement of resistance to herbivorous insects and for biofumigation
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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expression of CYP79D2 from cassava in Arabidopsis thaliana results in the production of valine- and isoleucine-derived glucosinolates not normally found in this ecotype. The transgenic lines show no morphological phenotype, and the level of endogenous glucosinolates is not affected. The novel glucosinolates constitute up to 35% of the total glucosinolate content in mature rosette leaves and up to 48% in old leaves. At increased concentrations of these glucosinolates, the proportion of Val-derived glucosinolates decreases. As the isothiocyanates produced from the Val- and isoleucine-derived glucosinolates are volatile, metabolically engineered plants producing these glucosinolates have acquired novel properties with great potential for improvement of resistance to herbivorous insects and for biofumigation