Information on EC 1.14.14.43 - (methylsulfanyl)alkanaldoxime N-monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.14.43
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RECOMMENDED NAME
GeneOntology No.
(methylsulfanyl)alkanaldoxime N-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 1-(methylsulfanyl)-4-aci-nitroalkane + glutathione = an S-[(1E)-1-(hydroxyimino)-omega-(methylsulfanyl)alkyl]-L-glutathione + H2O
show the reaction diagram
(1b)
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an (E)-omega-(methylsulfanyl)alkanal oxime + [reduced NADPH-hemoprotein reductase] + glutathione + O2 = an S-[(1E)-1-(hydroxyimino)-omega-(methylsulfanyl)alkyl]-L-glutathione + [oxidized NADPH-hemoprotein reductase] + 2 H2O
show the reaction diagram
overall reaction
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an (E)-omega-(methylsulfanyl)alkanal oxime + [reduced NADPH-hemoprotein reductase] + O2 = a 1-(methylsulfanyl)-4-aci-nitroalkane + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
(1a)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glucosinolate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(E)-omega-(methylthio)alkananaldoxime,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
This cytochrome P-450 (heme thiolate) enzyme is involved in the biosynthesis of glucosinolates in plants. The enzyme catalyses an N-hydroxylation of the E isomer of n-(methylsulfanyl)alkanal oximes, forming an aci-nitro intermediate that reacts non-enzymically with glutathione to produce an N-alkyl-thiohydroximate adduct, the committed precursor of glucosinolates. In the absence of a thiol compound, the enzyme is suicidal, probably due to interaction of the reactive aci-nitro intermediate with active site residues.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform CYP83A1.1, presence of four CYP83A1 genes in allotetraploid Brassica juncea
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
(E)-4-hydroxyphenylacetaldoxime + O2 + [reduced NADPH-hemoprotein reductase]
1-aci-nitro-2-(4-hydroxyphenyl)-ethane + H2O + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
(E)-phenylacetaldoxime + O2 + [reduced NADPH-hemoprotein reductase]
1-aci-nitro-2-phenylethane + H2O + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
1-aci-nitro-2-(4-hydroxyphenyl)-ethane + 2-mercaptoethanol
(Z)-2-hydroxyethyl N-hydroxy-2-(4-hydroxyphenyl)ethanimidothioate + H2O
show the reaction diagram
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?
indole-3-acetaldoxime + O2 + glutathione + [reduced NADPH-hemoprotein reductase]
1-aci-nitro-2-indolyl-ethane + H2O + [oxidized NADPH-hemoprotein reductase]
show the reaction diagram
additional information
?
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isoform CYP83A1 catalyzes the initial conversion of aldoximes to thiohydroximates in the synthesis of glucosinolates not derived from tryptophan
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.065 - 0.156
(E)-4-hydroxyphenylacetaldoxime
0.188 - 0.556
(E)-phenylacetaldoxime
0.0031 - 0.15
indole-3-acetaldoxime
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23 - 0.43
(E)-4-hydroxyphenylacetaldoxime
0.42 - 0.78
(E)-phenylacetaldoxime
0.87 - 2.33
indole-3-acetaldoxime
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.76 - 3.5
(E)-4-hydroxyphenylacetaldoxime
0.75 - 4.1
(E)-phenylacetaldoxime
15 - 280
indole-3-acetaldoxime
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high expression level; high expression level
Manually annotated by BRENDA team
lower expression level than in leaf; lower expression level than in leaf
Manually annotated by BRENDA team
lower expression level than in leaf; lower expression level than in leaf
Manually annotated by BRENDA team
additional information
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
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expression in Saccharomyces cerevisiae; expression in Saccharomyces cerevisiae
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
reduced transcript abundance in response to the exogenously treated salicylic acid, iodoacetic acid, abscisic acid, 1-aminocyclopropane carboxylate
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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loss of CYP83A1 function leads to dramatically reduced parasitic growth of the biotrophic powdery mildew fungus Erysiphe cruciferarum on Arabidopsis thaliana