Information on EC 1.14.14.37 - 4-hydroxyphenylacetaldehyde oxime monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.14.37
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RECOMMENDED NAME
GeneOntology No.
4-hydroxyphenylacetaldehyde oxime monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2 = (S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
show the reaction diagram
overall reaction
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(E)-4-hydroxyphenylacetaldehyde oxime = (Z)-4-hydroxyphenylacetaldehyde oxime
show the reaction diagram
(1a)
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(Z)-4-hydroxyphenylacetaldehyde oxime = 4-hydroxyphenylacetonitrile + H2O
show the reaction diagram
(1b)
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4-hydroxyphenylacetonitrile + [reduced NADPH-hemoprotein reductase] + O2 = (S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
(1c)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Cyanoamino acid metabolism
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
(E)-4-hydroxyphenylacetaldehyde oxime,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase
This cytochrome P-450 (heme thiolate) enzyme is involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum. It catalyses three different activities - isomerization of the (E) isomer to the (Z) isomer, dehydration, and C-hydroxylation.
CAS REGISTRY NUMBER
COMMENTARY hide
213017-82-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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-Hydroxyphenylacetaldehyde oxime
(Z)-4-Hydroxyphenylacetaldehyde oxime
show the reaction diagram
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(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
show the reaction diagram
(E)-phenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-mandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
show the reaction diagram
oxime dervied from phenylalanine, 35% of the activity with (E)-4-hydroxyphenylacetaldehyde oxime
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(Z)-3-methylbutanaloxime + [reduced NADPH-hemoprotein reductase] + O2
2-hydroxy-3-methylbutyronitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
show the reaction diagram
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?
(Z)-4-hydroxyphenylacetaldehyde oxime
4-hydroxyphenylacetonitrile + H2O
show the reaction diagram
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2-hydroxy(p-hydroxyphenyl)acetaldoxime
4-hydroxymandelonitrile + H2O
show the reaction diagram
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poor substrate
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?
4-hydroxyphenylacetonitrile + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
show the reaction diagram
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additional information
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CYP71E1 metabolizes aromatic oximes efficiently, whereas aliphatic oximes are slowly metabolized
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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
(E)-4-Hydroxyphenylacetaldehyde oxime
(Z)-4-Hydroxyphenylacetaldehyde oxime
show the reaction diagram
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?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
show the reaction diagram
(Z)-3-methylbutanaloxime + [reduced NADPH-hemoprotein reductase] + O2
2-hydroxy-3-methylbutyronitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
show the reaction diagram
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(Z)-4-hydroxyphenylacetaldehyde oxime
4-hydroxyphenylacetonitrile + H2O
show the reaction diagram
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4-hydroxyphenylacetonitrile + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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less effective than NADPH
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-hydroxy(p-hydroxyphenyl)acetaldoxime
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in higher concentrations
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
p-hydroxyphenylacetaldoxime
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0.35
p-hydroxyphenylacetonitrile
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.003
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conversion of p-hydroxyphenylacetaldoxime to p-hydrobenzaldehyde
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8 - 8.4
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formation of p-hydroxybenzaldehyde from L-tyrosine in microsomal fractions
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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the site of dhurrin synthesis shifts from leaves to stem during plant development. At all stages, the content of dhurrin correlates well with the activity of the two biosynthetic enzymes, CYP79A1 and CYP71E1, and with the protein and mRNA level for the two enzymes
Manually annotated by BRENDA team
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maximal activity after 1 day of germination
Manually annotated by BRENDA team
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the site of dhurrin synthesis shifts from leaves to stem during plant development. At all stages, the content of dhurrin correlates well with the activity of the two biosynthetic enzymes, CYP79A1 and CYP71E1, and with the protein and mRNA level for the two enzymes
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 55000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
CYP71E1 is labile and prone to rapid denaturation at room temperature. CYP71E1 is isolated in the low spin form.
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification of heterologous expressed protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Nicotiana tabacum
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in Escherichia coli strain JM109
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution with NADPH-P450 oxidoreductase in micelles of L-alpha-dilauroyl phosphatidylcholine
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
analysis
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direct electrochemical investigation of plant cytochrome P450s by nanodisc technology. Full length CYP79A1, CYP71E1 and NADPH P450 oxidoreductase of the dhurrin pathway are reconstituted individually in nanoscale lipid patches, nanodiscs, and directly immobilized on unmodified gold electrodes. Cyclic voltammograms of CYP79A1 and CYP71E1 reveal reversible redox peaks with average midpoint potentials of 80 mV and 72 mV vs. Ag/AgCl, respectively. NADPH P450 oxidoreductase yields two pairs of redox peaks with midpoint potentials of 90 mV and -300 mV, respectively. The average heterogeneous electron transfer rate constant is calculated to be 1.5 per s
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