Information on EC 1.14.13.41 - tyrosine N-monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.41
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RECOMMENDED NAME
GeneOntology No.
tyrosine N-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-tyrosine + O2 + NADPH + H+ = N-hydroxy-L-tyrosine + NADP+ + H2O
show the reaction diagram
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N,N-dihydroxy-L-tyrosine = (Z)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
show the reaction diagram
second reaction; the second reaction is followed by spontaneous eliminative decarboxylation
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N-hydroxy-L-tyrosine + O2 + NADPH + H+ = N,N-dihydroxy-L-tyrosine + NADP+ + H2O
show the reaction diagram
second reaction
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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,NADPH:oxygen oxidoreductase (N-hydroxylating)
A heme-thiolate protein (P-450). This enzyme is involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along with EC 1.14.13.68, 4-hydroxyphenylacetaldehyde oxime monooxygenase and EC 2.4.1.85, cyanohydrin beta-glucosyltransferase. Some 2-(4-hydroxyphenyl)-1-nitroethane is formed as a side product.
CAS REGISTRY NUMBER
COMMENTARY hide
159447-19-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-tyrosine + NADPH + O2
N-hydroxy-L-tyrosine + NADP+ + H2O
show the reaction diagram
L-tyrosine + NADPH + O2
p-hydroxyphenylacetaldoxime + NADP+ + H2O
show the reaction diagram
L-tyrosine + O2 + NADPH + H+
4-hydroxyphenylacetaldoxime + NADP+ + CO2 + H2O
show the reaction diagram
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overall reaction, P450Tyr is a multifunctional tyrosine N-hydroxylase catalyzing the double N-hydroxylation of L-tyrosine to N,N-dihydroxy-L-tyrosine which dehydrates and decarboxylates to 4-hydroxyphenylacetaldoxime
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-
?
L-tyrosine + O2 + NADPH + H+
N,N-dihydroxy-L-tyrosine + NADP+ + H2O
show the reaction diagram
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?
additional information
?
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P450Tyr does not metabolize L-phenylalanine
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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 + NADPH + O2
N-hydroxy-L-tyrosine + NADP+ + H2O
show the reaction diagram
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
0.22
L-tyrosine
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in reconstitution experiments using Sorghum bicolor; recombinant enzyme, in 50 mM Tricine, pH 7.9, a 30°C
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
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
calculated from amino acid sequence
61890
calculated from DNA sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
no modification
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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full length clone
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