1.13.11.11: tryptophan 2,3-dioxygenase
This is an abbreviated version!
For detailed information about tryptophan 2,3-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.11
-
1.13.11.11
-
indoleamine
-
kynurenine
-
immunotherapy
-
heme
-
serotonin
-
checkpoint
-
l-trp
-
n-formylkynurenine
-
quinolinic
-
tolerogenic
-
3-monooxygenase
-
3,4-dioxygenase
-
heme-containing
-
2,3-dioxygenase-1
-
tryptophan-degrading
-
3-hydroxyanthranilate
-
indoleamine-2,3-dioxygenase
-
picolinic
-
tryptophan-catabolizing
-
pyrrolase
-
3-hydroxykynurenine
-
medicine
-
drug development
- 1.13.11.11
- indoleamine
- kynurenine
-
immunotherapy
- heme
- serotonin
-
checkpoint
- l-trp
- n-formylkynurenine
-
quinolinic
-
tolerogenic
-
3-monooxygenase
-
3,4-dioxygenase
-
heme-containing
-
2,3-dioxygenase-1
-
tryptophan-degrading
- 3-hydroxyanthranilate
- indoleamine-2,3-dioxygenase
-
picolinic
-
tryptophan-catabolizing
-
pyrrolase
- 3-hydroxykynurenine
- medicine
- drug development
Reaction
Synonyms
33737, BRAFLDRAFT_210874, C28H8.11, EC 1.11.1.4, hTDO, IDO-1, IDO-2, IDO1, IDO2, indoleamine 2,3-dioxygenase 1, indoleamine 2,3-dioxygenase 2, TDO, TDO2, TDOa, tryptophan 2,3-dioxygenase, tryptophan 2,3-dioxygenase 2, tryptophan 2,3-dioxygenase-2, tryptophan-2,3-dioxygenase, v1g157887, vCG5163, XcTDO
ECTree
Advanced search results
Engineering
Engineering on EC 1.13.11.11 - tryptophan 2,3-dioxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
F140A
site-directed mutagenesis, the mutant shows 0.25% of wild-type activity
R144A
site-directed mutagenesis, the mutant shows 0.88% of wild-type activity
S151A
site-directed mutagenesis, the mutant shows 9.08% of wild-type activity
Y175G
site-directed mutagenesis, the mutation leads to a 6fold slower multiple turnover velocity. In addition, pre-incubation of the Y175G mutant with 8 mM NFK retards the formation of the ternary complex by about 100fold and impedes Trp binding
Y42A
site-directed mutagenesis, the mutant shows 0.5% of wild-type activity
Y45A
site-directed mutagenesis, the mutant shows 1.13% of wild-type activity
2 F51S/T254S
-
variant synthesizes monooxigenation product 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid in a ratio of 6.2:1 to wild-type product N-formyl-L-kynurenine
3 F51Q/G255S
-
variant synthesizes monooxigenation product 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid in a ratio of 3.1:1 to wild-type product N-formyl-L-kynurenine
4 F51M/Q127Y/T254S
-
variant synthesizes monooxigenation product 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid in a ratio of 2.6:1 to wild-type product N-formyl-L-kynurenine
F51I/Q127Y
-
mutant F51M/Q127Y shows higher 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid productivity than mutant F51I/Q127Y and mutant F51L/Q127Y, suggesting that the F51M and Q127Y substitutions imposed a cooperative effect on the enzyme activity
F51L/Q127Y
-
mutant F51M/Q127Y shows higher 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid productivity than mutant F51I/Q127Y and mutant F51L/Q127Y, suggesting that the F51M and Q127Y substitutions imposed a cooperative effect on the enzyme activity
F51M/Q127Y
F51M/Q127Y/T254S
-
mutations result in a decrease in the turnover numbers for production of 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid
F51Q/G255S
-
mutation enhances the 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid/N'-formylkynurenine ratio to 3.1:1
F51X
-
F51X mutant plasmids that express enzyme proteins with turnover numbers greater than 250 are used as templates to further improve production of 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid
TDOF51S/T254S
-
mutation enhances the 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid/N'-formylkynurenine ratio to 6.2:1
additional information
-
mutant F51M/Q127Y shows higher 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid productivity than mutant F51I/Q127Y and mutant F51L/Q127Y, suggesting that the F51M and Q127Y substitutions imposed a cooperative effect on the enzyme activity
F51M/Q127Y
-
variant synthesizes monooxigenation product 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid in a ratio of 2.0:1 to wild-type product N-formyl-L-kynurenine
full-length hTDO is unstable, and various truncations are constructed. A truncation containing amino acids 19-388 is found to have good solubility and stability, the truncated mutant shows 80.45% of wild-type activity
additional information
-
full-length hTDO is unstable, and various truncations are constructed. A truncation containing amino acids 19-388 is found to have good solubility and stability, the truncated mutant shows 80.45% of wild-type activity
additional information
construction of TDO-knockout mice, phenotype, overview. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low
additional information
-
construction of TDO-knockout mice, phenotype, overview. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low
-
additional information
-
directed evolution of a tryptophan 2,3-dioxygenase for the diastereoselective monooxygenation of tryptophans