Information on EC 1.14.13.125 - tryptophan N-monooxygenase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
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1.14.13.125
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RECOMMENDED NAME
GeneOntology No.
tryptophan N-monooxygenase
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REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
L-tryptophan + 2 O2 + 2 NADPH + 2 H+ = (E)-indol-3-ylacetaldoxime + 2 NADP+ + CO2 + 3 H2O
show the reaction diagram
overall reaction
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L-tryptophan + O2 + NADPH + H+ = N-hydroxy-L-tryptophan + NADP+ + H2O
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(1a)
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N,N-dihydroxy-L-tryptophan = (E)-indol-3-ylacetaldoxime + CO2 + H2O
show the reaction diagram
(1c)
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N-hydroxy-L-tryptophan + O2 + NADPH + H+ = N,N-dihydroxy-L-tryptophan + NADP+ + H2O
show the reaction diagram
(1b)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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Glucosinolate biosynthesis
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Tryptophan metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan,NADPH:oxygen oxidoreductase (N-hydroxylating)
A heme-thiolate protein (P-450). This enzyme catalyses two successive N-hydroxylations of L-tryptophan, the first steps in the biosynthesis of both auxin and the indole alkaloid phytoalexin camalexin. The product of the two hydroxylations, N,N-dihydroxy-L-tryptophan, is extremely labile and dehydrates spontaneously. The dehydrated product is then subject to a decarboxylation that produces an oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-tryptophan + NADPH + H+
indole-3-acetaldoxime + NADP+ + CO2 + H2O
show the reaction diagram
L-tryptophan + NADPH + H+ + O2
indole-3-acetaldoxime + NADP+ + CO2 + H2O
show the reaction diagram
additional information
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CYP79B1 is not able to metabolize L-phenylalanine or L-tyrosine
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COFACTOR
ORGANISM
UNIPROT
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LITERATURE
IMAGE
NADPH
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INHIBITORS
ORGANISM
UNIPROT
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LITERATURE
IMAGE
1-aminobenzotriazole
the activity of CYP79B2 is inhibited 18 and 75% by 0.4 mM and 4 mM 1-aminobenzotriazole
2,4-Dichlorophenol
800 mM 2,4-dichlorophenol added to the CYP79B2 reconstitution assay inhibits the activity by 72%
H2O2
100 mM H2O2 added to the CYP79B2 reconstitution assay inhibits the activity by 96%
MnCl2
1 mM MnCl2 added to the CYP79B2 reconstitution assay inhibits the activity by 34%
tetcyclasis
the activity of CYP79B2 is inhibited 54 and 76% by 0.02 and 0.2 mM tetcyclasis
additional information
CYP79B2 is not inhibited by Me2SO of a maximum concentration of 4% (v/v); the combination of 100 mM H2O2, 1 mM MnCl2, and 800 mM 2,4-dichlorophenol added to the reconstitution assay inhibits the CYP79B2 activity by 99%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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LITERATURE
IMAGE
0.021 - 0.029
L-tryptophan
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pH OPTIMUM
ORGANISM
UNIPROT
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LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
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LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
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LITERATURE
SOURCE
highest expression in roots
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
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LITERATURE
61000
estimated from amino acid sequence
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C43(DE3) cells
expressed in Escherichia coli C43(DE3) cells, reconstitution of CYP79B1 monooxygenase requires a NADPH:cytochrome P450 reductase
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expressed in Escherichia coli; expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CYP79B2 expression is induced up to 1.5fold by wounding, 2.8fold by 0.25 mM methyl jasmonate in combination with 2.5 mM 1-aminocyclopropane-1-carboxylate, and 4.6fold after methyl jasmonate treatment alone. CYP79B3 is induced 3.5fold by methyl jasmonate and up to 1.7fold by methyl jasmonate in combination with 1-aminocyclopropane-1-carboxylate, and the induction levels are lower than those observed for CYP79B2. After treatment with 0.0002 mM 2,4-dichloro-phenoxyacetic acid, expression of CYP79B2 and CYP79B3 is induced 1.6 and 1.3fold, respectively
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CYP79B2 is wound-inducible
induction of the CYP79B2 mRNA levels is observed 12.5 h after infection by virulent strain Pseudomonas syringae pv. maculicola
the basal expression level of CYP79B3 is suppressed to 0.6fold that of control levels by 1-aminocyclopropane-1-carboxylate treatment
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the transcript level of CYP79B2, but not CYP79B3, is increased 3fold upon induction of camalexin by silver nitrate
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.125)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)