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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

Reaction

L-tryptophan
+
O2
=
N-formyl-L-kynurenine

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

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.11 tryptophan 2,3-dioxygenase

Engineering

Engineering on EC 1.13.11.11 - tryptophan 2,3-dioxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F140A
site-directed mutagenesis, the mutant shows 0.25% of wild-type activity
F72A
site-directed mutagenesis, inactive mutant
H328A
site-directed mutagenesis, inactive mutant
H76A,
site-directed mutagenesis, inactive mutant
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