Information on EC 1.14.14.36 - tyrosine N-monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.14.36
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RECOMMENDED NAME
GeneOntology No.
tyrosine N-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
overall reaction
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L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase] = N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
(1a)
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N,N-dihydroxy-L-tyrosine = (E)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
show the reaction diagram
(1c)
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N-hydroxy-L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase] = N,N-dihydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
(1b)
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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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Glucosinolate biosynthesis
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
L-tyrosine,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein. The enzyme from Sorghum is involved in the biosynthesis of the cyanogenic glucoside dhurrin. In Sinapis alba (white mustard) the enzyme is involved in the biosynthesis of the glucosinolate sinalbin.
CAS REGISTRY NUMBER
COMMENTARY hide
159447-19-5
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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
1-nitro-2-(4-hydroxyphenyl)ethane + O2 + [reduced NADPH-hemoprotein reductase]
N,N-dihydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
involvement of 1-nitro-2-(4-hydroxyphenyl)ethane or more likely its aci-nitro tautomer as an intermediate between N-hydroxytyrosine and 4-hydroxyphenylacetaldehyde oxime
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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
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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-
overall reaction
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
N,N-dihydroxy-L-tyrosine
(E)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
show the reaction diagram
N-hydroxy-L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
N,N-dihydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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-
-
-
?
N-hydroxy-L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N,N-dihydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
show the reaction diagram
-
-
overall reaction
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
N,N-dihydroxy-L-tyrosine
(E)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
show the reaction diagram
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-
-
-
?
N-hydroxy-L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N,N-dihydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutathione
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3 mM glutathione stimulates activity of the reconstituted enzyme; at 3 mM, activation rate differs between experiments
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
1-nitro-2-(4-hydroxyphenyl)ethane
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pH 7.9, 30°C
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0.14 - 0.22
L-tyrosine
0.3
NADH
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0.013
NADPH
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.82 - 5.83
L-tyrosine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0233
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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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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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57000
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SDS-PAGE
61700
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calculated from amino acid sequence; SDS-PAGE
61760
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calculated from amino acid sequence
61890
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calculated from DNA sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
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no posttranslational modifications at the N- and C-terminal ends except for the N-terminal methionine removal
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9.5
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390078
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 40
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
fairly stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
combined use of Renex 690, CHAPS and RTX-100 is optimal for maximal recovery and avoidance of conversion into cytochrome P-420
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DEAE-Speharose column chromatography and Reactive Red-120 agarose column chromatography; homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 cells; various N-terminal modifications
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expression in Escherichia coli; expression in Escherichia coli
expression in Nicotiana tabacum
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full length clone
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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mutant 1: first codons of Escherichia coli mRNA are enriched for A's and T's, second codon is changed into GCT, first 8 codons of P450 sequence are replaced with the N-terminal sequence of bovine P45017alpha, mutant 2: deletion of 14 amino acids, mutant 3: deletion of 25 amino acids, mutant 4: deletion of 75 amino acids
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
lipid micelles made from L-alpha-dilauroyl phosphatidylcholine are more than twice as effective in reconstituting cytochrome P-450Tyr activity as compared to other lipids
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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
biotechnology