Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | enzyme is activated 1.5fold and 3fold in presence of 8 M urea and 0.5% SDS respectively | Pseudomonas fluorescens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
CO | weak | Pseudomonas fluorescens | |
hydroxylamine | almost completely at 1 mM, TSO I and II, not: dehydrogenase component | Pseudomonas fluorescens | |
KCN | almost completely at 0.2 mM, TSO I and II, not: dehydrogenase component | Pseudomonas fluorescens | |
Sodium azide | weak | Pseudomonas fluorescens | |
Sodium nitrite | almost completely at 1 mM, TSO I and II, not: dehydrogenase component | Pseudomonas fluorescens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0015 | - |
L-tryptophan | TSO I | Pseudomonas fluorescens | |
0.01 | - |
L-tryptophan | TSO II | Pseudomonas fluorescens | |
0.0154 | - |
3-Methylindole | TSO I | Pseudomonas fluorescens | |
0.025 | - |
3-Methylindole | TSO II | Pseudomonas fluorescens | |
0.0435 | - |
3-indolemethanol | TSO I | Pseudomonas fluorescens | |
0.05 | 0.055 | O2 | + skatole or 3-indolemethanol, TSO I | Pseudomonas fluorescens | |
0.055 | - |
3-indolemethanol | TSO II | Pseudomonas fluorescens | |
0.1 | - |
N-Acetyl-L-tryptophanamide | TSO I | Pseudomonas fluorescens | |
0.12 | - |
N-Acetyl-L-tryptophanamide | TSO II | Pseudomonas fluorescens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe | TSO I: 4 mol of Fe per mol of enzyme | Pseudomonas fluorescens | |
Fe | TSO II: 2 mol of Fe per mol of enzyme | Pseudomonas fluorescens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
28000 | - |
x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE | Pseudomonas fluorescens |
40000 | - |
x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE | Pseudomonas fluorescens |
48000 | - |
1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE | Pseudomonas fluorescens |
48000 | - |
x * 72000 + x * 48000, TSO II, SDS-PAGE | Pseudomonas fluorescens |
64000 | - |
x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE | Pseudomonas fluorescens |
72000 | - |
1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE | Pseudomonas fluorescens |
72000 | - |
x * 72000 + x * 48000, TSO II, SDS-PAGE | Pseudomonas fluorescens |
150000 | - |
TSO II | Pseudomonas fluorescens |
150000 | - |
TSO II, gel filtration | Pseudomonas fluorescens |
280000 | - |
TSO I, gel filtration | Pseudomonas fluorescens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-tryptophan + O2 | Pseudomonas fluorescens | first enzyme of metabolic pathway for tryptophan | 3-indoleglycolaldehyde + CO2 + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas fluorescens | - |
ATCC 29574 | - |
Purification (Comment) | Organism |
---|---|
TSO I and TSO II as well as dehydrogenase component and oxidase component of TSO II | Pseudomonas fluorescens |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
- |
Pseudomonas fluorescens |
Storage Stability | Organism |
---|---|
-80°C, several months | Pseudomonas fluorescens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-indoleacetaldehyde + O2 | - |
Pseudomonas fluorescens | ? | - |
? | |
3-indolelactate + O2 | - |
Pseudomonas fluorescens | ? | - |
? | |
3-indolemethanol + O2 | - |
Pseudomonas fluorescens | ? | - |
? | |
3-indolepropionate + O2 | - |
Pseudomonas fluorescens | ? | - |
? | |
3-indolepyruvate + O2 | - |
Pseudomonas fluorescens | ? | - |
? | |
3-indolethanol + O2 | - |
Pseudomonas fluorescens | ? | - |
? | |
3-methylindole + O2 | O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2 | Pseudomonas fluorescens | 3-indolecarboxaldehyde + H2O | - |
? | |
3-methylindole + O2 | 3-methylindole is skatole, two-step sequential reactions | Pseudomonas fluorescens | 3-indolecarboxaldehyde + H2O | - |
? | |
5-hydroxytryptamine + O2 | - |
Pseudomonas fluorescens | ? | - |
? | |
alpha-hydroxy-L-tryptophan + O2 | - |
Pseudomonas fluorescens | ? | - |
? | |
D-tryptophan + O2 | - |
Pseudomonas fluorescens | ? | - |
? | |
L-tryptophan + O2 | O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2 | Pseudomonas fluorescens | 3-indoleglycolaldehyde + CO2 + NH3 | - |
? | |
L-tryptophan + O2 | first enzyme of metabolic pathway for tryptophan | Pseudomonas fluorescens | 3-indoleglycolaldehyde + CO2 + NH3 | - |
? | |
Leu-Trp + O2 | O2 required, 2,6-dichlorophenolindophenol and ferricyanide replace O2 | Pseudomonas fluorescens | Leu-alpha,beta-dehydrotryptamine + CO2 + H2O | - |
? | |
Leu-Trp-Leu + O2 | - |
Pseudomonas fluorescens | ? | - |
? | |
melatonin + O2 | - |
Pseudomonas fluorescens | ? | - |
? | |
additional information | ferricyanide is highly efficient towards TSO II compared with TSO I | Pseudomonas fluorescens | additional information | - |
? | |
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 | - |
? | |
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 | - |
? | |
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 | ? | |
tryptamine + O2 | - |
Pseudomonas fluorescens | ? | - |
? | |
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 | Comment | Organism |
---|---|---|
? | x * 64000 + x * 40000 + x + 35000 + x * 28000, TSO I, SDS-PAGE | Pseudomonas fluorescens |
? | x * 72000 + x * 48000, TSO II, SDS-PAGE | Pseudomonas fluorescens |
dimer | 1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE | Pseudomonas fluorescens |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
70 | - |
TSO II, 10 min, pH 6.0, 70% loss of activity | Pseudomonas fluorescens |
80 | - |
TSO I, 5 min, pH 6, 50% loss of activity | Pseudomonas fluorescens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
3 | - |
L-tryptophan | Pseudomonas fluorescens |
3 | 7 | broad, TSO II with N-acetyl-L-tryptophanamide, ferricyanide reductase activity of TSO II and dehydrogenase component | Pseudomonas fluorescens |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
2 | - |
TSO I, 4°C, 4 days, 36% loss of activity | Pseudomonas fluorescens |
6 | - |
TSO I, 4°C, 4 days, 72% loss of activity | Pseudomonas fluorescens |
11 | - |
TSO I, 4°C, 4 days, 93% loss of activity | Pseudomonas fluorescens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | hemoprotein | Pseudomonas fluorescens | |
heme | TSO II: 1 mol of protoheme IX per mol of enzyme | Pseudomonas fluorescens | |
heme | TSO I: 2 mol of protoheme IX per mol of enzyme | Pseudomonas fluorescens |