BRENDA - Enzyme Database show
show all sequences of 1.13.12.3

Structure of the flavoprotein tryptophan 2-monooxygenase, a key enzyme in the formation of galls in plants

Gaweska, H.M.; Taylor, A.B.; Hart, P.J.; Fitzpatrick, P.F.; Biochemistry 52, 2620-2626 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli as a His-tagged fusion protein
Pseudomonas savastanoi
Crystallization (Commentary)
Crystallization
Organism
determined by X-ray diffraction methods to a resolution of 1.95 A. The overall structure of the protein shows that it has the same fold as members of the monoamine oxidase family of flavoproteins, with the greatest similarities to the L-amino acid oxidases
Pseudomonas savastanoi
Engineering
Amino acid exchange
Commentary
Organism
K365M
mutation decreases the kcat and kcat/Km (L-tryptophan) values by 60000- and 2 millionfold compared to wild-type, respectively
Pseudomonas savastanoi
W466F
mutation decreases the kcat value less than 2fold and the kcat/Km (L-tryptophan) value only 5fold compared to wild-type
Pseudomonas savastanoi
W466M
mutation results in an enzyme lacking flavin and detectable activity
Pseudomonas savastanoi
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
L-tryptophan
pH 8.3, 25°C, wild-type
Pseudomonas savastanoi
0.13
-
L-tryptophan
pH 8.3, 25°C, mutant W466F
Pseudomonas savastanoi
1.2
-
L-tryptophan
pH 8.3, 25°C, mutant K365M
Pseudomonas savastanoi
90
-
O2
pH 8.3, 25°C, wild-type
Pseudomonas savastanoi
140
-
O2
pH 8.3, 25°C, mutant W466F
Pseudomonas savastanoi
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas savastanoi
P06617
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tryptophan + O2
-
727017
Pseudomonas savastanoi
indole-3-acetamide + CO2 + H2O
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Pseudomonas savastanoi
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00022
-
L-tryptophan
pH 8.3, 25°C, cosubstrate: O2, mutant K365M
Pseudomonas savastanoi
9.2
-
L-tryptophan
pH 8.3, 25°C, cosubstrate: O2, mutant W466F
Pseudomonas savastanoi
13.2
-
L-tryptophan
pH 8.3, 25°C, cosubstrate: O2, wild-type
Pseudomonas savastanoi
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.3
-
assay at
Pseudomonas savastanoi
Cofactor
Cofactor
Commentary
Organism
Structure
flavin
-
Pseudomonas savastanoi
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli as a His-tagged fusion protein
Pseudomonas savastanoi
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
flavin
-
Pseudomonas savastanoi
Crystallization (Commentary) (protein specific)
Crystallization
Organism
determined by X-ray diffraction methods to a resolution of 1.95 A. The overall structure of the protein shows that it has the same fold as members of the monoamine oxidase family of flavoproteins, with the greatest similarities to the L-amino acid oxidases
Pseudomonas savastanoi
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K365M
mutation decreases the kcat and kcat/Km (L-tryptophan) values by 60000- and 2 millionfold compared to wild-type, respectively
Pseudomonas savastanoi
W466F
mutation decreases the kcat value less than 2fold and the kcat/Km (L-tryptophan) value only 5fold compared to wild-type
Pseudomonas savastanoi
W466M
mutation results in an enzyme lacking flavin and detectable activity
Pseudomonas savastanoi
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
L-tryptophan
pH 8.3, 25°C, wild-type
Pseudomonas savastanoi
0.13
-
L-tryptophan
pH 8.3, 25°C, mutant W466F
Pseudomonas savastanoi
1.2
-
L-tryptophan
pH 8.3, 25°C, mutant K365M
Pseudomonas savastanoi
90
-
O2
pH 8.3, 25°C, wild-type
Pseudomonas savastanoi
140
-
O2
pH 8.3, 25°C, mutant W466F
Pseudomonas savastanoi
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tryptophan + O2
-
727017
Pseudomonas savastanoi
indole-3-acetamide + CO2 + H2O
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Pseudomonas savastanoi
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.00022
-
L-tryptophan
pH 8.3, 25°C, cosubstrate: O2, mutant K365M
Pseudomonas savastanoi
9.2
-
L-tryptophan
pH 8.3, 25°C, cosubstrate: O2, mutant W466F
Pseudomonas savastanoi
13.2
-
L-tryptophan
pH 8.3, 25°C, cosubstrate: O2, wild-type
Pseudomonas savastanoi
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.3
-
assay at
Pseudomonas savastanoi
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00019
-
L-tryptophan
pH 8.3, 25°C, mutant K365M
Pseudomonas savastanoi
70
-
O2
pH 8.3, 25°C, mutant W466F
Pseudomonas savastanoi
72
-
L-tryptophan
pH 8.3, 25°C, mutant W466F
Pseudomonas savastanoi
140
-
O2
pH 8.3, 25°C, wild-type
Pseudomonas savastanoi
360
-
L-tryptophan
pH 8.3, 25°C, wild-type
Pseudomonas savastanoi
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00019
-
L-tryptophan
pH 8.3, 25°C, mutant K365M
Pseudomonas savastanoi
70
-
O2
pH 8.3, 25°C, mutant W466F
Pseudomonas savastanoi
72
-
L-tryptophan
pH 8.3, 25°C, mutant W466F
Pseudomonas savastanoi
140
-
O2
pH 8.3, 25°C, wild-type
Pseudomonas savastanoi
360
-
L-tryptophan
pH 8.3, 25°C, wild-type
Pseudomonas savastanoi
Other publictions for EC 1.13.12.3
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)
746273
Zhang
Regulation of oncogene expres ...
Agrobacterium tumefaciens, Agrobacterium tumefaciens C58
PLoS Pathog.
11
1-27
2015
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1
2
2
1
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745813
Yin
Characterization of a tryptop ...
Puccinia graminis f. sp. tritici, Puccinia graminis f. sp. tritici CRL 75-36-700-3
Mol. Plant Microbe Interact.
27
227-235
2014
-
-
1
-
-
-
-
-
-
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2
-
10
-
-
-
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2
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2
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2
2
-
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746257
Mujahid
Aniline is an inducer, and no ...
Rubrivivax benzoatilyticus, Rubrivivax benzoatilyticus JA2
PLoS ONE
9
e87503
2014
-
-
1
-
-
-
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-
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2
-
7
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2
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1
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1
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1
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2
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2
-
1
-
-
-
1
-
-
-
1
2
2
1
-
-
727017
Gaweska
Structure of the flavoprotein ...
Pseudomonas savastanoi
Biochemistry
52
2620-2626
2013
-
-
1
1
3
-
-
5
-
-
-
-
-
3
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1
-
1
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3
1
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1
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1
1
1
3
-
-
-
-
5
-
-
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-
-
-
-
-
-
-
-
-
1
-
1
-
-
3
1
-
-
-
-
-
-
-
5
5
726752
Mujahid
Production of indole-3-acetic ...
Rubrivivax benzoatilyticus
Appl. Microbiol. Biotechnol.
89
1001-1008
2011
-
-
-
-
-
-
-
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3
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1
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1
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1
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1
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1
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1
1
-
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-
672116
Ralph
Mechanistic studies of the fla ...
Pseudomonas savastanoi
Biochemistry
45
15844-15852
2006
-
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1
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2
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1
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1
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1
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1
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2
-
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-
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-
-
-
-
-
-
-
-
-
-
-
654682
Sobrado
Analysis of the role of the ac ...
Pseudomonas savastanoi
Biochemistry
42
13826-13832
2003
-
-
-
-
2
-
2
6
-
-
-
-
-
1
-
-
-
-
-
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1
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-
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3
-
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6
-
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2
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2
6
6
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-
1
-
-
-
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3
-
-
-
-
-
-
-
-
-
-
654683
Sobrado
Identification of Tyr413 as an ...
Pseudomonas savastanoi
Biochemistry
42
13833-13838
2003
-
-
-
-
2
-
2
6
-
-
-
-
-
1
-
-
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-
-
-
-
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1
-
-
-
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3
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6
-
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2
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2
6
6
-
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-
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-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
439346
Sobrado
Analysis of the roles of amino ...
Pseudomonas savastanoi
Arch. Biochem. Biophys.
402
24-30
2002
-
-
-
-
3
-
-
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-
-
-
-
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2
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1
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1
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439349
Lemcke
The ORF8 gene product of Agrob ...
Agrobacterium rhizogenes
Mol. Plant Microbe Interact.
13
787-790
2000
-
-
1
-
-
-
-
-
-
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4
-
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1
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1
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-
-
1
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439348
Gadda
Characterization of 2-oxo-3-pe ...
Pseudomonas savastanoi
Biochemistry
38
5822-5828
1999
-
-
1
-
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-
1
-
-
-
-
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-
1
-
-
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1
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1
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1
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-
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-
-
-
439347
Emanuele
Purification and characterizat ...
Pseudomonas savastanoi
Arch. Biochem. Biophys.
316
241-248
1995
-
-
1
-
-
-
16
7
-
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1
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4
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1
-
-
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1
2
7
-
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1
-
7
-
1
-
1
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1
1
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16
-
7
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1
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1
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1
2
7
-
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1
-
7
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1
-
-
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-
-
-
-
-
439343
Hutcheson
Regulation of 3-indoleacetic a ...
Pseudomonas savastanoi
J. Biol. Chem.
260
6281-6287
1985
-
-
-
-
-
1
2
1
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2
1
-
4
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1
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1
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1
1
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1
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1
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-
-
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-
439344
Yamada
Nucleotide sequences of the Ps ...
Agrobacterium tumefaciens, Pseudomonas savastanoi
Proc. Natl. Acad. Sci. USA
82
6522-6526
1985
-
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5
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439345
Comai
Cloning characterization of ia ...
Pseudomonas savastanoi
J. Bacteriol.
149
40-46
1982
-
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1
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439342
Comai
Involvement of plasmid deoxyri ...
Pseudomonas savastanoi
J. Bacteriol.
143
950-957
1980
-
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1
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439341
Kosuge
Microbial synthesis and degrad ...
Pseudomonas savastanoi
J. Biol. Chem.
241
3738-3744
1966
-
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19
-
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1
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1
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1
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1
2
5
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1
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1
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1
1
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19
-
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1
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1
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1
2
5
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1
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1
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1
1
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