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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
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, tsoii,
more
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indole-3-alkane alpha-hydroxylase
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indolyl-3-alkane alpha-hydroxylase
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oxidase, tryptophan side-chain alpha,beta-
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oxidase, tryptophan side-chain alpha,beta-, II
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tryptophan side chain oxidase
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tryptophan side chain oxidase II
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tryptophan side chain oxidase type I
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tryptophan side-chain alpha,beta-oxidase
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tryptophan side-chain oxidase
tryptophan side-chain oxidase
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tryptophan side-chain oxidase
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L-tryptophan + O2 = (indol-3-yl)glycolaldehyde + CO2 + NH3
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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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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3-indoleacetaldehyde + O2
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?
3-indoleacetamide + O2
?
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?
3-indolemethanol + ferricyanide
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r
3-indolemethanol + O2
?
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?
3-indolepropionate + O2
?
3-indolepyruvate + O2
?
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?
3-methylindole + O2
3-indolecarboxaldehyde + H2O
5-hydroxy-L-tryptophan + O2
?
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?
5-hydroxytryptamine + O2
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5-methyl-DL-tryptophan + O2
?
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?
alpha-hydroxy-L-tryptophan + O2
?
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?
DL-5-fluorotryptophan + O2
?
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?
hormone-releasing factor + O2
?
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?
indole-3-butyric acid + O2
?
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?
L-Trp-L-Phe + O2 + O2
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?
L-Trp-L-Trp + O2
?
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?
L-tryptophan + O2
(indol-3-yl)glycolaldehyde + CO2 + NH3
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?
L-tryptophan + O2
3-indoleglycolaldehyde + CO2 + NH3
L-tryptophan methyl ester + O2
?
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?
Leu-Trp + O2
Leu-alpha,beta-dehydrotryptamine + CO2 + H2O
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
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N-acetyl-L-tryptophan + O2
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?
N-acetyl-L-tryptophanamide + O2
beta-keto-N-acetyltryptophanamide + H2O
N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O
N-acetylacetamide + O2
?
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?
Trp-Leu + O2
threo-beta-hydroxytryptophan + erythro-beta-hydroxytryptophan + ?
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?
tryptophan + O2
indolyloxazoline + H2O
additional information
additional information
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3-indolelactate + O2
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?
3-indolelactate + O2
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3-indolepropionate + O2
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?
3-indolepropionate + O2
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3-indolepropionate + O2
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3-indolethanol + O2
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3-indolethanol + O2
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3-methylindole + O2
3-indolecarboxaldehyde + H2O
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intermediate: 3-indolemethanol, under anaerobic conditions with ferricyanide
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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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3-methylindole + O2
3-indolecarboxaldehyde + H2O
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D-tryptophan + O2
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D-tryptophan + O2
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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
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L-tryptophan + O2
3-indoleglycolaldehyde + CO2 + NH3
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first enzyme of metabolic pathway for tryptophan
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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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Leu-Trp + O2
Leu-alpha,beta-dehydrotryptamine + CO2 + H2O
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Leu-Trp + O2
Leu-alpha,beta-dehydrotryptamine + CO2 + H2O
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O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2
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Leu-Trp-Leu + O2
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Leu-Trp-Leu + O2
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melatonin + O2
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melatonin + O2
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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
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N-acetyl-L-tryptophanamide + O2
beta-keto-N-acetyltryptophanamide + H2O
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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
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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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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
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N-acetyl-L-tryptophanamide + O2
N-acetyl-alpha,beta-didehydrotryptophanamide + H2O
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tryptamine + O2
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tryptamine + O2
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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)
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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)
?
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
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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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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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L-tryptophan + O2
(indol-3-yl)glycolaldehyde + CO2 + NH3
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?
L-tryptophan + O2
3-indoleglycolaldehyde + CO2 + NH3
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first enzyme of metabolic pathway for tryptophan
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?
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heme
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hemoprotein
heme
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contains 1.1 mol of heme per mol of enzyme
heme
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dehydrogenase component: 0.73 mol protoheme IX per mol of component
heme
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TSO II: 1 mol of protoheme IX per mol of enzyme
heme
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TSO I: 2 mol of protoheme IX per mol of enzyme
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Fe
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TSO I: 4 mol of Fe per mol of enzyme
Fe
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dehydrogenase component: 0.67 atoms of iron per mol of component
Fe
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TSO II: 2 mol of Fe per mol of enzyme
Fe
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contains 0.8 mol of iron per mol of enzyme
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indole-3-methanol
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inhibits oxidation of skatole
skatole
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inhibits oxidation of indole-3-methanol
Sodium nitrite
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almost completely at 1 mM, TSO I and II, not: dehydrogenase component
CO
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weak
hydroxylamine
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almost completely at 1 mM, TSO I and II, not: dehydrogenase component
KCN
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almost completely at 0.2 mM, TSO I and II, not: dehydrogenase component
Sodium azide
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weak
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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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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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Neoplasms
The synthesis of L-tryptophan degrading bioreactors.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Depletion of patients' plasma tryptophan using tryptophan side-chain oxidase columns.
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0.0435 - 0.055
3-indolemethanol
0.0154 - 0.025
3-Methylindole
0.48
indole-3-methanol
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0.0015 - 0.01
L-tryptophan
0.1 - 0.12
N-Acetyl-L-tryptophanamide
0.0435
3-indolemethanol
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0.0435
3-indolemethanol
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TSO I
0.055
3-indolemethanol
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TSO II
0.055
3-indolemethanol
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cosubstrate O2
0.0154
3-Methylindole
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TSO I
0.0154
3-Methylindole
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+ skatole
0.025
3-Methylindole
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TSO II
0.0015
L-tryptophan
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at pH 6.0
0.0015
L-tryptophan
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TSO I
0.004
L-tryptophan
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at pH 3.0
0.01
L-tryptophan
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TSO II
0.1
N-Acetyl-L-tryptophanamide
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TSO I
0.12
N-Acetyl-L-tryptophanamide
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TSO II
0.05
O2
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cosubstrate 3-methylindole, i.e. skatole
0.05 - 0.055
O2
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+ skatole or 3-indolemethanol, TSO I
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additional information
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3 - 7
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broad, TSO II with N-acetyl-L-tryptophanamide, ferricyanide reductase activity of TSO II and dehydrogenase component
3
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L-tryptophan
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25
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assay at
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5.7
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calculated from amino acid sequence
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
ATCC 29574
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brenda
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physiological function
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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
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250000
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sedimentation equilibrium ultracentrifugation
28000
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x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE
40000
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x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE
64000
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x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE
150000
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TSO II
150000
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TSO II, gel filtration
280000
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gel filtration
280000
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TSO I, gel filtration
48000
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1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE
48000
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x * 72000 + x * 48000, TSO II, SDS-PAGE
72000
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1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE
72000
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x * 72000 + x * 48000, TSO II, SDS-PAGE
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?
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x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE
?
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x * 72000 + x * 48000, TSO II, SDS-PAGE
dimer
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1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE
dimer
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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
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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
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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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11
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TSO I, 4°C, 4 days, 93% loss of activity
439304
2
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TSO I, 4°C, 4 days, 36% loss of activity
439304
6
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TSO I, 4°C, 4 days, 72% loss of activity
439304
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70
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TSO II, 10 min, pH 6.0, 70% loss of activity
80
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TSO I, 5 min, pH 6, 50% loss of activity
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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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-80C, several months
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affinity column chromatography
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dehydrogenase component and oxidase component
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TSO I and TSO II as well as dehydrogenase component and oxidase component of TSO II
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medicine
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use for tryptophan depletion in patients with refractory acute lymphocytic leukemia
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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
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