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Literature summary extracted from

  • Sakamoto, T.; Joern, J.M.; Arisawa, A.; Arnold, F.H.
    Laboratory evolution of toluene dioxygenase to accept 4-picoline as a substrate (2001), Appl. Environ. Microbiol., 67, 3882-3887.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.12.11 expression of mutant enzyme TDO 2-B38, in which the wild-type stop codon is replaced with a codon encoding Thr Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.14.12.11 additional information Escherichia coli expressed mutant enzyme TDO 2-B38, in which the wild-type stop codon is replaced with a codon encoding threonine, exhibits 5.6times higher activity towards 4-picoline and about 20% more activity towards toluene than the wild-type enzyme Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.14.12.11 Pseudomonas putida
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.12.11 4-picoline + NADH + O2 E. coli expressed mutant enzyme TDO 2-B38, in which the wild-type stop codon is replaced with a codon encoding threonine, exhibits 5.6-times higher activity towards 4-picoline than the wild-type enzyme Pseudomonas putida 3-hydroxy-4-picoline + ?
-
 ?
1.14.12.11 toluene + NADH + O2 E. coli expressed mutant enzyme TDO 2-B38, in which the wild-type stop codon is replaced with a codon encoding threonine, exhibits about 20% more activity towards toluene than the wild-type enzyme Pseudomonas putida (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + NAD+
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.12.11 NADH
-
 Pseudomonas putida