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Information on EC 1.13.12.3 - tryptophan 2-monooxygenase
for references in articles please use BRENDA:EC1.13.12.3
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EC Tree 1 Oxidoreductases
1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)
1.13.12.3 tryptophan 2-monooxygenase
IUBMB Comments
The enzyme, studied from phytopathogenic bacteria such as Pseudomonas savastanoi, is involved in a pathway for the production of (indol-3-yl)acetate (IAA), the main auxin hormone in plants.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 1.13.12.3
- flavoproteins
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indole-3-acetic
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indoleacetamide
- savastanoi
- indole-3-acetamide
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indoleacetic
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l-amino
- gall
- rhizogenes
- indolepyruvate
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oleander
showSynonyms
tryptophan 2-monooxygenase, tryptophan monooxygenase, pgt-iaam, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IaaM
oxygenase, tryptophan 2-mono-
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Pgt-IaaM
PGTG_11658
TMO
tryptophan monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + O2 = (indol-3-yl)acetamide + CO2 + H2O
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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oxidative decarboxylation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
indole-3-acetate biosynthesis III (bacteria)
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:oxygen 2-oxidoreductase (decarboxylating)
The enzyme, studied from phytopathogenic bacteria such as Pseudomonas savastanoi, is involved in a pathway for the production of (indol-3-yl)acetate (IAA), the main auxin hormone in plants.
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CAS REGISTRY NUMBER
COMMENTARY
37256-65-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5-hydroxytryptophan + O2
5-hydroxyindole-3-acetamide + CO2 + H2O
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Substrates: at 17% the rate of that for L-tryptophan
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5-methyltryptophan + O2
5-methylindole-3-acetamide + CO2 + H2O
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Substrates: -
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D,L-3-phenyl-2-hydrazinopropanoic acid + O2
2-phenylacetohydrazide + CO2 + H2O
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Substrates: -
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D,L-3-pyridylalanine + O2
2-pyridylacetamide + CO2 + H2O
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Substrates: -
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D,L-N-methyl-phenylalanine + O2
N-methyl-2-phenylacetamide + CO2 + H2O
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Substrates: -
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L-methionine + O2
3-(methylthio)propanamide + CO2 + H2O
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Substrates: -
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L-tryptophan + O2
?
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Substrates: oxidative decarboxylation of L-tryptophan during the biosynthesis of indoleacetic acid
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L-tyrosine + O2
4-hydroxyphenylacetamide + CO2 + H2O
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Substrates: weak activity
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additional information
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Substrates: no activity with: indole-3-pyruvate, indole-3-acetaldehyde, alpha-methyltryptophan, indole-3-acetic acid
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L-alanine + O2
acetamide + CO2 + H2O
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Substrates: oxidation of alanine occurs through a hydride transfer mechanism
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L-phenylalanine + O2
phenylacetamide + CO2 + H2O
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Substrates: -
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L-phenylalanine + O2
phenylacetamide + CO2 + H2O
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Substrates: weak activity
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L-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
Substrates: -
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L-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
Substrates: -
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L-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
Substrates: -
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L-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
Substrates: -
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L-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
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Substrates: -
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L-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
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Substrates: -
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L-tryptophan + O2
indole-3-acetamide + CO2 + H2O
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Substrates: -
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L-tryptophan + O2
indole-3-acetamide + CO2 + H2O
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Substrates: -
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L-tryptophan + O2
indole-3-acetamide + CO2 + H2O
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Substrates: -
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L-tryptophan + O2
indole-3-acetamide + CO2 + H2O
Substrates: -
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L-tryptophan + O2
indole-3-acetamide + CO2 + H2O
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Substrates: specific for L-isomer of tryptophan
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L-tryptophan + O2
indole-3-acetamide + CO2 + H2O
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Substrates: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-tryptophan + O2
?
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Substrates: oxidative decarboxylation of L-tryptophan during the biosynthesis of indoleacetic acid
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L-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
Substrates: -
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L-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
Substrates: -
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L-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
Substrates: -
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L-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
Substrates: -
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L-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
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Substrates: -
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L-tryptophan + O2
(indol-3-yl)acetamide + CO2 + H2O
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Substrates: -
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L-tryptophan + O2
indole-3-acetamide + CO2 + H2O
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Substrates: -
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L-tryptophan + O2
indole-3-acetamide + CO2 + H2O
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Substrates: -
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L-tryptophan + O2
indole-3-acetamide + CO2 + H2O
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Substrates: specific for L-isomer of tryptophan
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
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enzyme contains 0.73 FAD molecules per subunit, addition of FAD to partially purified preparation has no effect on activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00022
L-tryptophan
pH 8.3, 25°C, cosubstrate: O2, mutant K365M
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 10
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pH 5.5: about 50% of activity maximum, pH 10: about 55% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme is a product of the T-DNA tns-1 gene of the octopine-type plasmid pTiAGNC
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brenda
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brenda
evidence for extrachromosomal nature of gene involved in indole-3-acetic acid synthesis
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brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
transient silencing of the tryptophan 2-monooxygenase-encoding gene iaaM in infected wheat plants indicates that it is required for full pathogenicity
malfunction
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transient silencing of the tryptophan 2-monooxygenase-encoding gene iaaM in infected wheat plants indicates that it is required for full pathogenicity
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metabolism
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identification of indole 3-acetamide and tryptophan monooxygenase activity suggests indole 3-acetamide routed indole 3-acetic acid (IAA) biosynthesis in Rubrivivax benzoatilyticus JA2
metabolism
the enzyme is involved in the biosynthesis of auxin
metabolism
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tryptophan aminotransferase (TAT) and tryptophan 2-monooxygenase (TMO) participate in first step of tryptophan catabolism leading to the formation of indole acetic acid. Indole biosynthesis in strain JA2 occurs via the de novo shikimate pathway. Induction of tryptophan aminotransferase and tryptophan 2-monooxygenase activities corroborates well with indole 3-acetic acid levels, suggesting that tryptophan catabolism occurs simultaneously in aniline exposed cells. Aniline (stress) stimulates tryptophan/indoles synthesis via the shikimate pathway by possibly modulating the metabolic pathway
metabolism
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tryptophan aminotransferase (TAT) and tryptophan 2-monooxygenase (TMO) participate in first step of tryptophan catabolism leading to the formation of indole acetic acid. Indole biosynthesis in strain JA2 occurs via the de novo shikimate pathway. Induction of tryptophan aminotransferase and tryptophan 2-monooxygenase activities corroborates well with indole 3-acetic acid levels, suggesting that tryptophan catabolism occurs simultaneously in aniline exposed cells. Aniline (stress) stimulates tryptophan/indoles synthesis via the shikimate pathway by possibly modulating the metabolic pathway
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physiological function
Crown gall development requires the expression of agrobacterial genes in the plant host, e.g. Arabidopsis thaliana. These genes are transferred by the T-DNA of the plant pathogen Agrobacterium tumefaciens and include the oncogenes IaaH, IaaM and Ipt, which, according to the tumor-inducing principle, are essential for crown gall development. Virulent Agrobacterium tumefaciens strains integrate their T-DNA into the plant genome where the encoded agrobacterial oncogenes are expressed and cause crown gall disease. Essential for crown gall development are IaaH (indole-3-acetamide hydrolase), IaaM (tryptophan monooxygenase) and Ipt (isopentenyl transferase), which encode enzymes for the biosynthesis of auxin (IaaH, IaaM) and cytokinin (Ipt). The oncogenes are involved in auxin and cytokinin production. The intergenic regions (IGRs) between the coding sequences (CDS) of the three oncogenes function as promoters in plant cells, but gene IaaM is constitutively expressed and no transcription factor further activates its promoter. With increasing auxin levels triggered by ubiquitous expression of IaaH and IaaM, ARF5 is activated and interacts with WRKY40 to potentiate Ipt expression and balance cytokinin and auxin levels for further cell proliferation. Transcriptional regulation of the Agrobacterium tumefaciens genes IaaH, IaaM and Ipt in the host plant, detailed overview
physiological function
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tryptophan 2-monooxygenase (TMO) participate in first step of tryptophan catabolism leading to the formation of indole acetic acid. Metabolic profiling reveals tryptophan accumulation only in aniline exposed cells along with indole 3-acetic acid and indole 3-aldehyde, the two major catabolites of tryptophan. Deuterium labelled aniline feeding studies reveal that while fumarate is the precursor of indole biosynthesis, aniline is not a precursor of indoles in strain JA2, but is an indole biosynthesis stimulator
physiological function
tryptophan 2-monooxygenase from Puccinia graminis f. sp. tritici produces the auxin precursor indole-3-acetamide (IAM) and is involved in auxin biosynthesis and rust pathogenicity. Auxin acts as a regulator of plant growth and development but its production can also affect plantmicrobe interactions. Expression of Pgt-IaaM in Arabidopsis thaliana haustoria causes a typical auxin expression phenotype and promotes susceptibility to the bacterial pathogen Pseudomonas syringae pv. tomato DC3000
physiological function
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tryptophan 2-monooxygenase (TMO) participate in first step of tryptophan catabolism leading to the formation of indole acetic acid. Metabolic profiling reveals tryptophan accumulation only in aniline exposed cells along with indole 3-acetic acid and indole 3-aldehyde, the two major catabolites of tryptophan. Deuterium labelled aniline feeding studies reveal that while fumarate is the precursor of indole biosynthesis, aniline is not a precursor of indoles in strain JA2, but is an indole biosynthesis stimulator
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physiological function
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tryptophan 2-monooxygenase from Puccinia graminis f. sp. tritici produces the auxin precursor indole-3-acetamide (IAM) and is involved in auxin biosynthesis and rust pathogenicity. Auxin acts as a regulator of plant growth and development but its production can also affect plantmicrobe interactions. Expression of Pgt-IaaM in Arabidopsis thaliana haustoria causes a typical auxin expression phenotype and promotes susceptibility to the bacterial pathogen Pseudomonas syringae pv. tomato DC3000
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physiological function
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Crown gall development requires the expression of agrobacterial genes in the plant host, e.g. Arabidopsis thaliana. These genes are transferred by the T-DNA of the plant pathogen Agrobacterium tumefaciens and include the oncogenes IaaH, IaaM and Ipt, which, according to the tumor-inducing principle, are essential for crown gall development. Virulent Agrobacterium tumefaciens strains integrate their T-DNA into the plant genome where the encoded agrobacterial oncogenes are expressed and cause crown gall disease. Essential for crown gall development are IaaH (indole-3-acetamide hydrolase), IaaM (tryptophan monooxygenase) and Ipt (isopentenyl transferase), which encode enzymes for the biosynthesis of auxin (IaaH, IaaM) and cytokinin (Ipt). The oncogenes are involved in auxin and cytokinin production. The intergenic regions (IGRs) between the coding sequences (CDS) of the three oncogenes function as promoters in plant cells, but gene IaaM is constitutively expressed and no transcription factor further activates its promoter. With increasing auxin levels triggered by ubiquitous expression of IaaH and IaaM, ARF5 is activated and interacts with WRKY40 to potentiate Ipt expression and balance cytokinin and auxin levels for further cell proliferation. Transcriptional regulation of the Agrobacterium tumefaciens genes IaaH, IaaM and Ipt in the host plant, detailed overview
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Show AA Sequence and Transmembrane Helices (396 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K365M
mutation decreases the kcat and kcat/Km (L-tryptophan) values by 60000- and 2 millionfold compared to wild-type, respectively
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE