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Literature summary extracted from

  • Takai, K.; Hayaishi, O.
    Purification and properties of tryptophan side chain oxidase types I and II from Pseudomonas (1987), Methods Enzymol., 142, 195-217.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.13.99.3 additional information enzyme is activated 1.5fold and 3fold in presence of 8 M urea and 0.5% SDS respectively Pseudomonas fluorescens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.99.3 CO weak Pseudomonas fluorescens
1.13.99.3 hydroxylamine almost completely at 1 mM, TSO I and II, not: dehydrogenase component Pseudomonas fluorescens
1.13.99.3 KCN almost completely at 0.2 mM, TSO I and II, not: dehydrogenase component Pseudomonas fluorescens
1.13.99.3 Sodium azide weak Pseudomonas fluorescens
1.13.99.3 Sodium nitrite almost completely at 1 mM, TSO I and II, not: dehydrogenase component Pseudomonas fluorescens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.99.3 0.0015
-
 L-tryptophan TSO I Pseudomonas fluorescens
1.13.99.3 0.01
-
 L-tryptophan TSO II Pseudomonas fluorescens
1.13.99.3 0.0154
-
 3-Methylindole TSO I Pseudomonas fluorescens
1.13.99.3 0.025
-
 3-Methylindole TSO II Pseudomonas fluorescens
1.13.99.3 0.0435
-
 3-indolemethanol TSO I Pseudomonas fluorescens
1.13.99.3 0.05 0.055 O2 + skatole or 3-indolemethanol, TSO I Pseudomonas fluorescens
1.13.99.3 0.055
-
 3-indolemethanol TSO II Pseudomonas fluorescens
1.13.99.3 0.1
-
 N-Acetyl-L-tryptophanamide TSO I Pseudomonas fluorescens
1.13.99.3 0.12
-
 N-Acetyl-L-tryptophanamide TSO II Pseudomonas fluorescens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.99.3 Fe TSO I: 4 mol of Fe per mol of enzyme Pseudomonas fluorescens
1.13.99.3 Fe TSO II: 2 mol of Fe per mol of enzyme Pseudomonas fluorescens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.99.3 28000
-
 x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE Pseudomonas fluorescens
1.13.99.3 40000
-
 x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE Pseudomonas fluorescens
1.13.99.3 48000
-
 1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE Pseudomonas fluorescens
1.13.99.3 48000
-
 x * 72000 + x * 48000, TSO II, SDS-PAGE Pseudomonas fluorescens
1.13.99.3 64000
-
 x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE Pseudomonas fluorescens
1.13.99.3 72000
-
 1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE Pseudomonas fluorescens
1.13.99.3 72000
-
 x * 72000 + x * 48000, TSO II, SDS-PAGE Pseudomonas fluorescens
1.13.99.3 150000
-
 TSO II Pseudomonas fluorescens
1.13.99.3 150000
-
 TSO II, gel filtration Pseudomonas fluorescens
1.13.99.3 280000
-
 TSO I, gel filtration Pseudomonas fluorescens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.99.3 L-tryptophan + O2 Pseudomonas fluorescens first enzyme of metabolic pathway for tryptophan 3-indoleglycolaldehyde + CO2 + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.99.3 Pseudomonas fluorescens
-
 ATCC 29574
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.99.3 TSO I and TSO II as well as dehydrogenase component and oxidase component of TSO II Pseudomonas fluorescens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.13.99.3 additional information
-
-
 Pseudomonas fluorescens

Storage Stability

EC Number Storage Stability Organism
1.13.99.3 -80°C, several months Pseudomonas fluorescens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.99.3 3-indoleacetaldehyde + O2
-
 Pseudomonas fluorescens ?
-
 ?
1.13.99.3 3-indolelactate + O2
-
 Pseudomonas fluorescens ?
-
 ?
1.13.99.3 3-indolemethanol + O2
-
 Pseudomonas fluorescens ?
-
 ?
1.13.99.3 3-indolepropionate + O2
-
 Pseudomonas fluorescens ?
-
 ?
1.13.99.3 3-indolepyruvate + O2
-
 Pseudomonas fluorescens ?
-
 ?
1.13.99.3 3-indolethanol + O2
-
 Pseudomonas fluorescens ?
-
 ?
1.13.99.3 3-methylindole + O2 O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2 Pseudomonas fluorescens 3-indolecarboxaldehyde + H2O
-
 ?
1.13.99.3 3-methylindole + O2 3-methylindole is skatole, two-step sequential reactions Pseudomonas fluorescens 3-indolecarboxaldehyde + H2O
-
 ?
1.13.99.3 5-hydroxytryptamine + O2
-
 Pseudomonas fluorescens ?
-
 ?
1.13.99.3 alpha-hydroxy-L-tryptophan + O2
-
 Pseudomonas fluorescens ?
-
 ?
1.13.99.3 D-tryptophan + O2
-
 Pseudomonas fluorescens ?
-
 ?
1.13.99.3 L-tryptophan + O2 O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2 Pseudomonas fluorescens 3-indoleglycolaldehyde + CO2 + NH3
-
 ?
1.13.99.3 L-tryptophan + O2 first enzyme of metabolic pathway for tryptophan Pseudomonas fluorescens 3-indoleglycolaldehyde + CO2 + NH3
-
 ?
1.13.99.3 Leu-Trp + O2 O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2 Pseudomonas fluorescens Leu-alpha,beta-dehydrotryptamine + CO2 + H2O
-
 ?
1.13.99.3 Leu-Trp-Leu + O2
-
 Pseudomonas fluorescens ?
-
 ?
1.13.99.3 melatonin + O2
-
 Pseudomonas fluorescens ?
-
 ?
1.13.99.3 additional information ferricyanide is highly efficient towards TSO II compared with TSO I Pseudomonas fluorescens additional information
-
 ?
1.13.99.3 additional information 2,6-dichlorophenolindophenol preferred by TSO I, TSO II less active on L-tryptophan and almost inactive when alpha-amino group of tryptophan retained Pseudomonas fluorescens additional information
-
 ?
1.13.99.3 N-acetyl-L-tryptophanamide + O2 above pH 5.8, O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2 Pseudomonas fluorescens N-acetyl-alpha,beta-didehydrotryptophanamide + H2O
-
 ?
1.13.99.3 N-acetyl-L-tryptophanamide + O2 two-step sequential reactions, below pH 5.8, O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2 Pseudomonas fluorescens beta-keto-N-acetyltryptophanamide + H2O intermediate: beta-hydroxy erythro- and threo-N-acetyl-L-tryptophanamide ?
1.13.99.3 tryptamine + O2
-
 Pseudomonas fluorescens ?
-
 ?
1.13.99.3 tryptophan + O2 internally located tryptophan, O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2 Pseudomonas fluorescens indolyloxazoline + H2O further formation of alpha,beta-didehydrotryptophan residue (after isomerization) or a diastereomeric mixture of beta-hydroxytryptophan residues (after hydration) ?

Subunits

EC Number Subunits Comment Organism
1.13.99.3 ? x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE Pseudomonas fluorescens
1.13.99.3 ? x * 72000 + x * 48000, TSO II, SDS-PAGE Pseudomonas fluorescens
1.13.99.3 dimer 1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE Pseudomonas fluorescens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.13.99.3 70
-
 TSO II, 10 min, pH 6.0, 70% loss of activity Pseudomonas fluorescens
1.13.99.3 80
-
 TSO I, 5 min, pH 6, 50% loss of activity Pseudomonas fluorescens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.99.3 3
-
 L-tryptophan Pseudomonas fluorescens
1.13.99.3 3 7 broad, TSO II with N-acetyl-L-tryptophanamide, ferricyanide reductase activity of TSO II and dehydrogenase component Pseudomonas fluorescens

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.13.99.3 2
-
 TSO I, 4°C, 4 days, 36% loss of activity Pseudomonas fluorescens
1.13.99.3 6
-
 TSO I, 4°C, 4 days, 72% loss of activity Pseudomonas fluorescens
1.13.99.3 11
-
 TSO I, 4°C, 4 days, 93% loss of activity Pseudomonas fluorescens

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.99.3 heme hemoprotein Pseudomonas fluorescens
1.13.99.3 heme TSO II: 1 mol of protoheme IX per mol of enzyme Pseudomonas fluorescens
1.13.99.3 heme TSO I: 2 mol of protoheme IX per mol of enzyme Pseudomonas fluorescens