BRENDA - Enzyme Database show
show all sequences of 1.3.3.10

Enzymatic modification of tryptophan residues by tryptophan side chain oxidase I and II from Pseudomonas

Ito, S.; Takai, K.; Tokuyama, T.; Hayaishi, O.; J. Biol. Chem. 256, 7834-7843 (1981)

Data extracted from this reference:

Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
150000
-
-
Pseudomonas sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas sp.
-
-
-
Purification (Commentary)
Commentary
Organism
gel filtration, phosphocellulose column chromatography, SDS-PAGE
Pseudomonas sp.
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.02
-
substrate tryptophanamide
Pseudomonas sp.
0.07
-
substrate tryptophan-leucine
Pseudomonas sp.
0.31
-
substrate tryptophan
Pseudomonas sp.
0.74
-
substrate leucin-tryptophan-leucin
Pseudomonas sp.
1.08
-
substrate indolepropionic acid
Pseudomonas sp.
1.42
-
substrate N-acetyltryptophanamide
Pseudomonas sp.
1.82
-
substrate N-acetyltryptophan
Pseudomonas sp.
2.32
-
substrate leucin-tryptophan
Pseudomonas sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
150000
-
-
Pseudomonas sp.
Purification (Commentary) (protein specific)
Commentary
Organism
gel filtration, phosphocellulose column chromatography, SDS-PAGE
Pseudomonas sp.
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.02
-
substrate tryptophanamide
Pseudomonas sp.
0.07
-
substrate tryptophan-leucine
Pseudomonas sp.
0.31
-
substrate tryptophan
Pseudomonas sp.
0.74
-
substrate leucin-tryptophan-leucin
Pseudomonas sp.
1.08
-
substrate indolepropionic acid
Pseudomonas sp.
1.42
-
substrate N-acetyltryptophanamide
Pseudomonas sp.
1.82
-
substrate N-acetyltryptophan
Pseudomonas sp.
2.32
-
substrate leucin-tryptophan
Pseudomonas sp.
Other publictions for EC 1.3.3.10
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
689310
Amir-Heidari
Stereochemical course of trypt ...
Streptomyces coelicolor, Streptomyces coelicolor WH101.10
Org. Lett.
9
1513-1516
2007
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4
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2
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2
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639382
Genet
L-tryptophan 2',3'-oxidase fro ...
Chromobacterium violaceum, Chromobacterium violaceum ATCC 12472
J. Biol. Chem.
270
23540-23545
1995
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1
5
8
1
1
3
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5
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1
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13
1
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1
8
1
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1
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4
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-
1
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5
4
8
1
1
3
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1
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13
1
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1
8
1
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1
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639383
Genet
Purification and partial chara ...
Chromobacterium violaceum, Chromobacterium violaceum ATCC 12472
J. Biol. Chem.
269
18177-18184
1994
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5
1
1
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3
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5
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1
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1
2
1
1
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1
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1
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1
4
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1
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5
4
1
1
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3
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1
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1
2
1
1
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1
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1
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439306
Takai
Enzymatic dehydrogenation of t ...
Pseudomonas sp.
J. Biol. Chem.
259
4452-4457
1984
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2
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1
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2
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2
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2
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439311
Ito
Enzymatic modification of tryp ...
Pseudomonas sp.
J. Biol. Chem.
256
7834-7843
1981
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1
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1
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1
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8
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1
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1
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8
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