Any feedback?
No. of entries
Information on EC 1.13.99.3 - tryptophan 2'-dioxygenase
for references in articles please use BRENDA:EC1.13.99.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
1.13.99 Miscellaneous
1.13.99.3 tryptophan 2'-dioxygenase
IUBMB 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.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.13.99.3
-
indole-3-acetic
- tryptamine
- pyrrolnitrin
- indole-3-acetamide
- 2,4-diacetylphloroglucinol
-
diastereoisomeric
- indole-3-carboxaldehyde
-
3-substituted
- medicine
showSynonyms
indolyl-3-alkane alpha-hydroxylase, tryptophan side chain oxidase, tryptophan side-chain oxidase, tryptophan side chain oxidase ii, tsoii, tso i, tso ii, tryptophan side chain oxidase type i, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
indole-3-alkane alpha-hydroxylase
-
-
-
-
indolyl-3-alkane alpha-hydroxylase
-
-
-
-
oxidase, tryptophan side-chain alpha,beta-
-
-
-
-
oxidase, tryptophan side-chain alpha,beta-, II
-
-
-
-
tryptophan side chain oxidase
-
-
-
-
tryptophan side chain oxidase II
-
-
-
-
tryptophan side chain oxidase type I
-
-
-
-
tryptophan side-chain alpha,beta-oxidase
-
-
-
-
tryptophan side-chain oxidase
TSO
-
-
-
-
TSO I
-
-
-
-
TSO II
-
-
-
-
tryptophan side-chain oxidase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
L-tryptophan + O2 = (indol-3-yl)glycolaldehyde + CO2 + NH3
model of mechanism
-
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
-
-
L-tryptophan + O2 = (indol-3-yl)glycolaldehyde + CO2 + NH3
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-tryptophan degradation V (side chain pathway)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
64295-81-4
-
90371-50-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-tryptophan + O2
(indol-3-yl)glycolaldehyde + CO2 + NH3
Pseudomonas sp. ATCC 29574
-
Substrates: -
Products: -
Products: -
?
Leu-Trp-Leu + O2
Leu-beta-hydroxy-Trp-Leu + Leu-beta-hydroxy-Trp-Leu + Leu-alpha,beta-dehydro-Trp-Leu + ?
-
Substrates: -
Products: ratio of products depends on pH and ionic strength
Products: ratio of products depends on pH and ionic strength
?
Trp-Leu + O2
threo-beta-hydroxytryptophan + erythro-beta-hydroxytryptophan + ?
-
Substrates: -
Products: -
Products: -
?
3-methylindole + O2
3-indolecarboxaldehyde + H2O
-
Substrates: -
Products: intermediate: 3-indolemethanol, under anaerobic conditions with ferricyanide
Products: intermediate: 3-indolemethanol, under anaerobic conditions with ferricyanide
?
3-methylindole + O2
3-indolecarboxaldehyde + H2O
-
Substrates: O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
Products: -
Products: -
?
3-methylindole + O2
3-indolecarboxaldehyde + H2O
-
Substrates: 3-methylindole is skatole, two-step sequential reactions
Products: -
Products: -
?
3-methylindole + O2
3-indolecarboxaldehyde + H2O
-
Substrates: -
Products: -
Products: -
?
L-tryptophan + O2
3-indoleglycolaldehyde + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
L-tryptophan + O2
3-indoleglycolaldehyde + CO2 + NH3
-
Substrates: O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
Products: -
Products: -
?
L-tryptophan + O2
3-indoleglycolaldehyde + CO2 + NH3
-
Substrates: first enzyme of metabolic pathway for tryptophan
Products: -
Products: -
?
L-tryptophan + O2
3-indoleglycolaldehyde + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
L-tryptophan + O2
3-indoleglycolaldehyde + CO2 + NH3
-
Substrates: -
Products: -
Products: -
?
Leu-Trp + O2
Leu-alpha,beta-dehydrotryptamine + CO2 + H2O
-
Substrates: -
Products: -
Products: -
?
Leu-Trp + O2
Leu-alpha,beta-dehydrotryptamine + CO2 + H2O
-
Substrates: O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
Products: -
Products: -
?
N-acetyl-L-tryptophanamide + O2
beta-keto-N-acetyltryptophanamide + H2O
-
Substrates: two-step sequential reactions, below pH 5.8, O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
Products: intermediate: beta-hydroxy erythro- and threo-N-acetyl-L-tryptophanamide
Products: intermediate: beta-hydroxy erythro- and threo-N-acetyl-L-tryptophanamide
?
N-acetyl-L-tryptophanamide + O2
beta-keto-N-acetyltryptophanamide + H2O
-
Substrates: -
Products: -
Products: -
?
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O
-
Substrates: above pH 5.8, O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
Products: -
Products: -
?
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O
-
Substrates: -
Products: -
Products: -
?
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O
-
Substrates: -
Products: main product, intermediate is 5-(3-indolyl)-2-methyl-2-oxazoline-4-carboxamide
Products: main product, intermediate is 5-(3-indolyl)-2-methyl-2-oxazoline-4-carboxamide
?
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O
-
Substrates: -
Products: -
Products: -
?
tryptophan + O2
indolyloxazoline + H2O
-
Substrates: internally located tryptophan, O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
Products: further formation of alpha,beta-didehydrotryptophan residue (after isomerization) or a diastereomeric mixture of beta-hydroxytryptophan residues (after hydration)
Products: further formation of alpha,beta-didehydrotryptophan residue (after isomerization) or a diastereomeric mixture of beta-hydroxytryptophan residues (after hydration)
?
tryptophan + O2
indolyloxazoline + H2O
-
Substrates: internally located tryptophan, O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
Products: further formation of alpha,beta-didehydrotryptophan residue (after isomerization) or a diastereomeric mixture of beta-hydroxytryptophan residues (after hydration)
Products: further formation of alpha,beta-didehydrotryptophan residue (after isomerization) or a diastereomeric mixture of beta-hydroxytryptophan residues (after hydration)
?
additional information
additional information
-
-
Substrates: substrate: yeast mating hormone (alpha-factor)
Products: with any substrate 3-indolecarboxaldehyde is a sole detectable by-product
Products: with any substrate 3-indolecarboxaldehyde is a sole detectable by-product
?
additional information
additional information
-
-
Substrates: ferricyanide is highly efficient towards TSO II compared with TSO I
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: 2,6-dichlorophenolindophenol preferred by TSO I, TSO II less active on L-tryptophan and almost inactive when alpha-amino group of tryptophan retained
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: 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
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: -
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: overview: specificity
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: overview: specificity
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: substrate: tryptophan containing di- and oligopeptides
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: substrates: tryptophan residues in human alpha- and beta-globins
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: overview: specificity
Products: -
Products: -
?
additional information
additional information
-
-
Substrates: substrate: tryptophan containing di- and oligopeptides
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(indol-3-yl)glycolaldehyde + CO2 + NH3
Pseudomonas sp. ATCC 29574
-
Substrates: -
Products: -
Products: -
?
L-tryptophan + O2
3-indoleglycolaldehyde + CO2 + NH3
-
Substrates: first enzyme of metabolic pathway for tryptophan
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
dehydrogenase component: 0.73 mol protoheme IX per mol of component
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Fe
-
dehydrogenase component: 0.67 atoms of iron per mol of component
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme is activated 1.5fold and 3fold in presence of 8 M urea and 0.5% SDS respectively
-
additional information
-
enzyme is activated 1.5fold and 3fold in presence of 8 M urea and 0.5% SDS respectively
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Depletion of patients' plasma tryptophan using tryptophan side-chain oxidase columns.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7
-
broad, TSO II with N-acetyl-L-tryptophanamide, ferricyanide reductase activity of TSO II and dehydrogenase component
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
physiological function
Pseudomonas sp. ATCC 29574
-
the enzyme has inhibitory effects on the proliferation and migration of HCCLM3 (human hepatocarcinoma cell line) and HepG2 cells. The enzyme can inhibit proliferation and promotes apoptosis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
28000
-
x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE
280000
40000
-
x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE
48000
64000
-
x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE
72000
48000
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, 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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TSO I and TSO II as well as dehydrogenase component and oxidase component of TSO II
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
use for tryptophan depletion in patients with refractory acute lymphocytic leukemia
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Ai, Y.; Wang, B.; Xiao, S.; Luo, S.; Wang, Y.
Tryptophan side-chain oxidase enzyme suppresses hepatocellular carcinoma growth through degradation of tryptophan
Int. J. Mol. Sci.
22
12428
2021
Pseudomonas sp. ATCC 29574
brenda