Information on EC 1.13.12.3 - tryptophan 2-monooxygenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.13.12.3
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RECOMMENDED NAME
GeneOntology No.
tryptophan 2-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + O2 = (indol-3-yl)acetamide + CO2 + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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oxidative decarboxylation
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-
-
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redox reaction
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-
-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
indole-3-acetate biosynthesis III (bacteria)
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IAA biosynthesis
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Tryptophan metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:oxygen 2-oxidoreductase (decarboxylating)
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CAS REGISTRY NUMBER
COMMENTARY hide
37256-65-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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
5-hydroxytryptophan + O2
5-hydroxyindole-3-acetamide + CO2 + H2O
show the reaction diagram
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at 17% the rate of that for L-tryptophan
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?
5-methyltryptophan + O2
5-methylindole-3-acetamide + CO2 + H2O
show the reaction diagram
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-
-
-
?
D,L-3-phenyl-2-hydrazinopropanoic acid + O2
2-phenylacetohydrazide + CO2 + H2O
show the reaction diagram
-
-
-
-
?
D,L-3-pyridylalanine + O2
2-pyridylacetamide + CO2 + H2O
show the reaction diagram
-
-
-
-
?
D,L-N-methyl-phenylalanine + O2
N-methyl-2-phenylacetamide + CO2 + H2O
show the reaction diagram
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-
-
-
?
L-alanine + O2
acetamide + CO2 + H2O
show the reaction diagram
L-methionine + O2
3-(methylthio)propanamide + CO2 + H2O
show the reaction diagram
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-
-
-
?
L-phenylalanine + O2
phenylacetamide + CO2 + H2O
show the reaction diagram
L-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
show the reaction diagram
L-tryptophan + O2
?
show the reaction diagram
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oxidative decarboxylation of L-tryptophan during the biosynthesis of indoleacetic acid
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?
L-tryptophan + O2
indole-3-acetamide + CO2 + H2O
show the reaction diagram
L-tyrosine + O2
4-hydroxyphenylacetamide + CO2 + H2O
show the reaction diagram
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weak activity
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?
additional information
?
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no activity with: indole-3-pyruvate, indole-3-acetaldehyde, alpha-methyltryptophan, indole-3-acetic acid
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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-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
show the reaction diagram
L-tryptophan + O2
?
show the reaction diagram
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oxidative decarboxylation of L-tryptophan during the biosynthesis of indoleacetic acid
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?
L-tryptophan + O2
indole-3-acetamide + CO2 + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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weak
2-methyl methanethiolsulfonate
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2-Oxo-3-pentynoate
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3-Indoleacetamide
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3-indolepyruvate
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CaCl2
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little or no effect
D-methionine
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competitive inhibition
D-phenylalanine
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competitive inhibition
D-tryptophan
Diethylpyrocarbonate
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diethylthiocarbonate
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EDTA
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little or no effect
Hydrocinnamic acid
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competitive inhibition
hydroxylamine
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Indole-3-acetaldehyde
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weak
Indole-3-acetamide
indole-3-acetic acid
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Indole-3-pyruvate
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iodoacetamide
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K3Fe(CN)6
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weak
KCN
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little or no effect
L-glutathione
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reduced
N-ethylmaleimide
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phenylacetamide
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competitive inhibition
Phenylethylamine
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competitive inhibition
phenyllactic acid
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competitive inhibition
phenylpyruvic acid
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competitive inhibition
Quinacrine
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weak
Semicarbazide
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tryptamine
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competitive inhibition
Vinylglycine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
D,L-3-phenyl-2-hydrazinopropanoic acid
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32
D,L-3-pyridylalanine
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22.6
D,L-N-methyl-phenylalanine
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22.6
L-alanine
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22.4
L-methionine
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2.4
L-phenylalanine
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0.036 - 1.48
L-tryptophan
0.067 - 140
O2
0.04 - 30
tryptophan
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000167
D,L-3-phenyl-2-hydrazinopropanoic acid
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0.00075
D,L-3-pyridylalanine
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0.000317
D,L-N-methyl-phenylalanine
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0.000317
L-alanine
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0.00155
L-methionine
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0.00305
L-phenylalanine
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0.00022 - 13.2
L-tryptophan
0.21 - 13.2
tryptophan
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00019 - 360
L-tryptophan
70 - 140
O2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16 - 45
3-Indoleacetamide
40 - 670
3-indolepyruvate
0.69 - 13.2
Indole-3-acetamide
0.69 - 13.2
Indole-3-pyruvate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 10
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pH 5.5: about 50% of activity maximum, pH 10: about 55% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61780
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calculation from nucleotide sequence
62000
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amino acid composition
85000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 62000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
determined by X-ray diffraction methods to a resolution of 1.95 A. The overall structure of the protein shows that it has the same fold as members of the monoamine oxidase family of flavoproteins, with the greatest similarities to the L-amino acid oxidases
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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pH 7.4, protein concentration above 4 mg/ml, 2 min, stable, 40% loss of activity after 5 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
FAD has no effect on stability
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10C, protein concentration 4 mg/ml, 2 months, less than 10% loss of activity
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-10C, protein concentration less than 0.3 mg/ml, 40% loss of activity after 24 h
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-20C, several weeks without significant loss in activity
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4C, several weeks without significant loss in activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
evidence for extrachromosomal nature of gene involved in indole-3-acetic acid synthesis
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expressed in Escherichia coli as a His-tagged fusion protein
expression in Escherichia coli
gene IaaM, the gene is constitutively expressed in plant host Arabidopsis thaliana via Ti plasmid-encoded T-DNA insertion in tranfected cells, and no transcription factor further activates its promoter IGR1b, that contains cis-regulatory binding elements. Genetic organization, overview. Transcription factor ARR1 can regulate transcription of the IaaH or IaaM genes. Promoter IGR1 drives expression of IaaH and IaaM and contains only one Wbox and AuxRE sequence motif, and this is more closely localized upstream of the IaaM than that of the IaaH TATA box
gene PGTG_11658 or Pgt-IaaM, transgenic expression of gene Pgt-IaaM in Arabidopsis thaliana haustoria causes a typical auxin expression phenotype and promotes susceptibility to the bacterial pathogen Pseudomonas syringae pv. tomato DC3000, transgenic expression of gene Pgt-IaaM in Triticum aestivum leaves, phenotypes, overview. Silencing of Pgt-IaaM by wheat host-induced gene silencing reduces the pathogenicity of Puccinia graminis. Expression of Pgt-IaaM in Arabidopsis thaliana displays pleiotropic auxin-related phenotypes
quantitative real time RT-PCR enzyme expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
aniline (stress) stimulates tryptophan/indoles synthesis via the shikimate pathway, including tryptophan 2-monooxygenase activity, by possibly modulating the metabolic pathway
gene IaaM is constitutively expressed and no transcription factor further activates its promoter
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C339A
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slight decrease in activity with tryptophan or methionine
C511S
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high decrease in activity with tryptophan or methionine
H338N
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slight decrease in activity with tryptophan or methionine
K365M
mutation decreases the kcat and kcat/Km (L-tryptophan) values by 60000- and 2 millionfold compared to wild-type, respectively
R98A
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decrease in Vmax, increase in Km-value of tryptophan
R98K
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decrease in Vmax, increase in Km-value of tryptophan
W466F
mutation decreases the kcat value less than 2fold and the kcat/Km (L-tryptophan) value only 5fold compared to wild-type
W466M
mutation results in an enzyme lacking flavin and detectable activity
Y413A
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200fold reduction in first-order rate constant for reduction, 33fold decrease in rate constant for oxidation, conversion of enzyme to oxidase
Y413F
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35fold reduction in first-order rate constant for reduction, 11fold decrease in rate constant for oxidation, conversion of enzyme to oxidase
Show AA Sequence (151 entries)
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