Literature summary for 1.14.12.11 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.

Search for more literature for 1.14.12.11

Cloned(Commentary)

Cloned (Comment)	Organism
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

Protein Variants	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Pseudomonas putida	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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 + ?	-	?
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

Cofactor	Comment	Organism	Structure
NADH	-	Pseudomonas putida

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Release 2023.1 (January 2023)