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Literature summary for 1.13.11.11 extracted from

  • Wei, Y.; Lu, C.; Jiang, S.; Zhang, Y.; Li, Q.; Bai, W.J.; Wang, X.
    Directed evolution of a tryptophan 2,3-dioxygenase for the diastereoselective monooxygenation of tryptophans (2020), Angew. Chem. Int. Ed. Engl., 59, 3043-3047 .
    View publication on PubMed
Search for more literature for 1.13.11.11

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Xanthomonas campestris

Protein Variants

Protein Variants Comment Organism
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 Xanthomonas campestris
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 Xanthomonas campestris
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 Xanthomonas campestris
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 Xanthomonas campestris
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 Xanthomonas campestris
F51M/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 Xanthomonas campestris
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 Xanthomonas campestris
F51M/Q127Y/T254S mutations result in a decrease in the turnover numbers for production of 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid Xanthomonas campestris
F51Q/G255S mutation enhances the 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid/N'-formylkynurenine ratio to 3.1:1 Xanthomonas campestris
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 Xanthomonas campestris
additional information directed evolution of a tryptophan 2,3-dioxygenase for the diastereoselective monooxygenation of tryptophans Xanthomonas campestris
TDOF51S/T254S mutation enhances the 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid/N'-formylkynurenine ratio to 6.2:1 Xanthomonas campestris

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-tryptophan + O2 Xanthomonas campestris
-
 N-formyl-L-kynurenine
-
 ?

Organism

Organism UniProt Comment Textmining
Xanthomonas campestris
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan + O2
-
 Xanthomonas campestris N-formyl-L-kynurenine
-
 ?
L-tryptophan + O2
-
 Xanthomonas campestris 3alpha-hydroxyhexahydropyrrolo[2,3-b]indole-2-carboxylic acid
-
 ?