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Literature summary extracted from

  • Ushiro, H.; Takai, K.; Narumiya, S.; Ito, S.; Hayaishi, O.
    Isolation and reconstitution of two electron transfer components of tryptophan side chain oxidase (1979), J. Biol. Chem., 254, 11794-11797.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.99.3 hydroxylamine
-
Pseudomonas fluorescens
1.13.99.3 indole-3-methanol inhibits oxidation of skatole Pseudomonas fluorescens
1.13.99.3 KCN
-
Pseudomonas fluorescens
1.13.99.3 skatole inhibits oxidation of indole-3-methanol Pseudomonas fluorescens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.99.3 0.48
-
indole-3-methanol
-
Pseudomonas fluorescens
1.13.99.3 0.67
-
ferricyanide
-
Pseudomonas fluorescens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.99.3 Fe dehydrogenase component: 0.67 atoms of iron per mol of component Pseudomonas fluorescens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.99.3 48000
-
1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE Pseudomonas fluorescens
1.13.99.3 72000
-
1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE Pseudomonas fluorescens

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 dehydrogenase component and oxidase component 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 29.2
-
-
Pseudomonas fluorescens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.99.3 3-indolemethanol + ferricyanide
-
Pseudomonas fluorescens ?
-
r
1.13.99.3 3-indolemethanol + O2
-
Pseudomonas fluorescens ?
-
?
1.13.99.3 additional information 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 Pseudomonas fluorescens additional information
-
?

Subunits

EC Number Subunits Comment Organism
1.13.99.3 dimer 1 * 72000 (dehydrogenase component) + 1 * 48000 (oxidase component), TSO II, SDS-PAGE Pseudomonas fluorescens
1.13.99.3 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 Pseudomonas fluorescens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.99.3 25
-
assay at Pseudomonas fluorescens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.99.3 3.5
-
-
Pseudomonas fluorescens

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.99.3 heme hemoprotein Pseudomonas fluorescens
1.13.99.3 heme dehydrogenase component: 0.73 mol protoheme IX per mol of component Pseudomonas fluorescens