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Information on EC 1.13.99.3 - tryptophan 2'-dioxygenase
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1.13.99.3 tryptophan 2'-dioxygenaseIUBMB Comments
A hemoprotein. Acts on a number of indole-3-alkane derivatives, oxidizing the 3-side-chain in the 2'-position. Best substrates were L-tryptophan and 5-hydroxy-L-tryptophan.
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Word Map
- 1.13.99.3
-
indole-3-acetic
-
diastereoisomeric
- pyrrolnitrin
- tryptamine
- indole-3-carboxaldehyde
- 2,4-diacetylphloroglucinol
-
3-substituted
- indole-3-acetamide
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
indolyl-3-alkane alpha-hydroxylase, tryptophan side chain oxidase, tryptophan side-chain oxidase, tryptophan side chain oxidase ii, tso i, tso ii, tryptophan side chain oxidase type i, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tryptophan + O2 = (indol-3-yl)glycolaldehyde + CO2 + NH3
primary reaction is hydroxylation of the side chain carbon adjacent to the indole ring, decarboxylation (of tryptophan only) is secondary
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L-tryptophan + O2 = (indol-3-yl)glycolaldehyde + CO2 + NH3
model of mechanism
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L-tryptophan + O2 = (indol-3-yl)glycolaldehyde + CO2 + NH3
primary reaction is hydroxylation of the side chain carbon adjacent to the indole ring, decarboxylation (of tryptophan only) is secondary
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L-tryptophan + O2 = (indol-3-yl)glycolaldehyde + CO2 + NH3
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:oxygen 2'-oxidoreductase (side-chain-cleaving)
A hemoprotein. Acts on a number of indole-3-alkane derivatives, oxidizing the 3-side-chain in the 2'-position. Best substrates were L-tryptophan and 5-hydroxy-L-tryptophan.
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CAS REGISTRY NUMBER
COMMENTARY
64295-81-4
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90371-50-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Leu-Trp-Leu + O2
Leu-beta-hydroxy-Trp-Leu + Leu-beta-hydroxy-Trp-Leu + Leu-alpha,beta-dehydro-Trp-Leu + ?
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ratio of products depends on pH and ionic strength
?
Trp-Leu + O2
threo-beta-hydroxytryptophan + erythro-beta-hydroxytryptophan + ?
-
-
-
?
3-methylindole + O2
3-indolecarboxaldehyde + H2O
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intermediate: 3-indolemethanol, under anaerobic conditions with ferricyanide
?
3-methylindole + O2
3-indolecarboxaldehyde + H2O
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O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
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?
3-methylindole + O2
3-indolecarboxaldehyde + H2O
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3-methylindole is skatole, two-step sequential reactions
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?
L-tryptophan + O2
3-indoleglycolaldehyde + CO2 + NH3
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-
-
?
L-tryptophan + O2
3-indoleglycolaldehyde + CO2 + NH3
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O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
-
?
L-tryptophan + O2
3-indoleglycolaldehyde + CO2 + NH3
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first enzyme of metabolic pathway for tryptophan
-
?
Leu-Trp + O2
Leu-alpha,beta-dehydrotryptamine + CO2 + H2O
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O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
-
?
N-acetyl-L-tryptophanamide + O2
beta-keto-N-acetyltryptophanamide + H2O
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two-step sequential reactions, below pH 5.8, O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
intermediate: beta-hydroxy erythro- and threo-N-acetyl-L-tryptophanamide
?
N-acetyl-L-tryptophanamide + O2
beta-keto-N-acetyltryptophanamide + H2O
-
-
-
?
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O
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above pH 5.8, O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
-
?
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O
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-
-
?
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O
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-
-
?
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O
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main product, intermediate is 5-(3-indolyl)-2-methyl-2-oxazoline-4-carboxamide
?
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O
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-
-
?
tryptophan + O2
indolyloxazoline + H2O
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internally located tryptophan, O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
further formation of alpha,beta-didehydrotryptophan residue (after isomerization) or a diastereomeric mixture of beta-hydroxytryptophan residues (after hydration)
?
tryptophan + O2
indolyloxazoline + H2O
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internally located tryptophan, O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
further formation of alpha,beta-didehydrotryptophan residue (after isomerization) or a diastereomeric mixture of beta-hydroxytryptophan residues (after hydration)
?
additional information
additional information
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substrate: yeast mating hormone (alpha-factor)
with any substrate 3-indolecarboxaldehyde is a sole detectable by-product
?
additional information
additional information
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ferricyanide is highly efficient towards TSO II compared with TSO I
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?
additional information
additional information
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2,6-dichlorophenolindophenol preferred by TSO I, TSO II less active on L-tryptophan and almost inactive when alpha-amino group of tryptophan retained
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?
additional information
additional information
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dehydrogenase component abstracts electrons from the substrate and transfers them to oxidation-reduction dyes (e.g. potassium ferricyanide, 2,6-dichlorophenolindophenol) but not to molecular oxygen, the oxidase component transfers electrons from the former component to oxygen
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?
additional information
additional information
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overview: specificity
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?
additional information
additional information
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overview: specificity
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?
additional information
additional information
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substrate: tryptophan containing di- and oligopeptides
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?
additional information
additional information
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substrates: tryptophan residues in human alpha- and beta-globins
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?
additional information
additional information
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overview: specificity
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?
additional information
additional information
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substrate: tryptophan containing di- and oligopeptides
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-tryptophan + O2
3-indoleglycolaldehyde + CO2 + NH3
-
first enzyme of metabolic pathway for tryptophan
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
dehydrogenase component: 0.73 mol protoheme IX per mol of component
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Fe
-
dehydrogenase component: 0.67 atoms of iron per mol of component
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Sodium nitrite
-
almost completely at 1 mM, TSO I and II, not: dehydrogenase component
hydroxylamine
-
almost completely at 1 mM, TSO I and II, not: dehydrogenase component
KCN
-
almost completely at 0.2 mM, TSO I and II, not: dehydrogenase component
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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enzyme is activated 1.5fold and 3fold in presence of 8 M urea and 0.5% SDS respectively
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additional information
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enzyme is activated 1.5fold and 3fold in presence of 8 M urea and 0.5% SDS respectively
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Depletion of patients' plasma tryptophan using tryptophan side-chain oxidase columns.
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KM VALUE [mM]
SUBSTRATE
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
3 - 7
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broad, TSO II with N-acetyl-L-tryptophanamide, ferricyanide reductase activity of TSO II and dehydrogenase component
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
28000
-
x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE
280000
40000
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x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE
48000
64000
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x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE
72000
48000
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1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE
72000
-
1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
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1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE
dimer
-
dehydrogenase component abstracts electrons from the substrate and transfers them to oxidation-reduction dyes e.g. potassium ferricyanide, 2,6-dichlorophenolindophenol, but not to molecular oxygen, the oxidase component transfers electrons from the former component to oxygen
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
isolation of a spontaneous mutant with reduced production of indole-3-acetic acid due to reduction of enzymic activity to about 10% of wild-type, biocontrol properties of the mutant strain are not affected
additional information
-
isolation of a spontaneous mutant with reduced production of indole-3-acetic acid due to reduction of enzymic activity to about 10% of wild-type, biocontrol properties of the mutant strain are not affected
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, several months
0°C, pH 6, stable in presence of either 80% ethyl alcohol, 6 M urea or 0.5% SDS for at least 6 h
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TSO I and TSO II as well as dehydrogenase component and oxidase component of TSO II
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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use for tryptophan depletion in patients with refractory acute lymphocytic leukemia
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takai, K.; Hayaishi, O.
Purification and properties of tryptophan side chain oxidase types I and II from Pseudomonas
Methods Enzymol.
142
195-217
1987
Pseudomonas fluorescens
brenda
Noda, Y.; Takai, K.; Tokuyama, T.; Narumiya, S.; Ushiro, H.; Hayaishi, O.
Enzymatic oxidation of acetyltryptophanamide- and tryptophan-containing peptides. Formation of dehydrotryptophan
J. Biol. Chem.
252
4413-4415
1977
Pseudomonas sp.
brenda
Takai, K.; Sasai, Y.; Morimoto, H.; Yamazaki, H.; Yoshii, H.; Inoue, S.
Enzymatic dehydrogenation of tryptophan residues of human globins by tryptophan side chain oxidase II
J. Biol. Chem.
259
4452-4457
1984
Pseudomonas sp.
brenda
Takai, K.; Ushiro, H.; Noda, Y.; Narumiya, S.; Tokuyama, T.; Hayaishi, O.
cristalline hemoprotein from Pseudomonas that catalyzes oxidation of side chain of tryptophan and other indole derivatives
J. Biol. Chem.
252
2638-2656
1977
Pseudomonas sp.
-
brenda
Narumiya, S.; Takai, K.; Tokuyama, T.; Noda, Y.; Ushiro, H.; Hayaishi, O.
A new metabolic pathway of tryptophan initiated by tryptophan side chain oxidase
J. Biol. Chem.
254
7007-7015
1979
Pseudomonas fluorescens
brenda
Roberts, J.; Rosenfeld, H.J.
Isolation, crystallization, and properties of indolyl-3-alkane alpha-hydroxylase. A novel tryptophan-metabolizing enzyme
J. Biol. Chem.
252
2640-2647
1977
Pseudomonas sp., Pseudomonas sp. XA
brenda
Zavala, F.; Takai, K.; Hayaishi, O.
Isolation and characterization of the common intermediate in dichotomous reaction catalyzed by tryptophan side chain oxidase
J. Biol. Chem.
258
344-351
1983
Pseudomonas sp.
brenda
Ito, S.; Takai, K.; Tokuyama, T.; Hayaishi, O.
Enzymatic modification of tryptophan residues by tryptophan side chain oxidase I and II from Pseudomonas
J. Biol. Chem.
256
7834-7843
1981
Pseudomonas fluorescens
brenda
Ushiro, H.; Takai, K.; Narumiya, S.; Ito, S.; Hayaishi, O.
Isolation and reconstitution of two electron transfer components of tryptophan side chain oxidase
J. Biol. Chem.
254
11794-11797
1979
Pseudomonas fluorescens
brenda
Ushiro, H.; Takai, K.; Noda, Y.; Narumiya, S.; Tokuyama, T.; Hayaishi, O.
Tryptophan side chain oxidase from Pseudomonas. Oxidation of skatole to indole-3-carboxaldehyde via indole-3-methanol
J. Biol. Chem.
253
9002-9008
1978
Pseudomonas fluorescens
brenda
Noda, Y.; Takai, K.; Tokuyama, T.; Narumiya, S.; Ushiro, H.; Hayaishi, O.
Tryptophan side chain oxidase from Pseudomonas. pH-Dependent formation of alpha,beta-didehydro, beta-hydroxy, and beta-keto derivatives of N-acetyltryptophanamide
J. Biol. Chem.
253
4819-4822
1978
Pseudomonas sp.
brenda
Ho, D.H.; Covington, W.P.; Wallerstein, R.O.; Hester, J.P.; Lin, J.R.; Brown, N.S.; Newman, R.A.; Krakoff, I.H.; Freireich, E.J.
Depletion of patients' plasma tryptophan using tryptophan side-chain oxidase columns
Cancer Invest.
11
252-257
1993
Homo sapiens
brenda
Suzuki, S.; He, Y.; Oyaizu, H.
Indole-3-Acetic acid production in Pseudomonas fluorescens HP72 and its association with suppression of creeping bentgrass brown patch
Curr. Microbiol.
47
138-143
2003
Pseudomonas fluorescens, Pseudomonas fluorescens HP72
brenda
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