Literature summary for 1.14.12.11 extracted from

Wissner, J.L.; Ludwig, J.; Escobedo-Hinojosa, W.; Hauer, B.
An enhanced toluene dioxygenase platform for the production of cis-1,2-dihydrocatechol in Escherichia coli BW25113 lacking glycerol dehydrogenase activity (2021), J. Biotechnol., 325, 380-388 .

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Application

Application	Comment	Organism
synthesis	Escherichia coli BW25113 DELTAgldA strain harboring pBAD18-TDO system is a suitable platform for the production of the valuable compound cis-1,2-dihydrocatechol at gram scale. The DHC scaffold finds extensive application in the production of a variety of fine chemicals and bioactive compounds	Pseudomonas putida

Cloned(Commentary)

Cloned (Comment)	Organism
expression into Escherichia coli BW25113 DELTAgldA. A strongly regulated toluene dioxygenase plasmid system for the dearomatizing cis-1,2-dihydroxylation of benzene is developed. Escherichia coli BW25113 DELTAgldA strain harboring pBAD18-TDO system is a suitable platform for the production of the valuable compound cis-1,2-dihydrocatechol (DHC) at gram scale	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	A5W4F2 AND A5W4F1	A5W4F2: toluene 2,3-dioxygenase subunit alpha, A5W4F1: toluene 2,3-dioxygenase subunit beta	-

Synonyms

Synonyms	Comment	Organism
TDO	-	Pseudomonas putida

General Information

General Information	Comment	Organism
metabolism	the native glycerol dehydrogenase in Escherichia coli is identified as the main responsible enzyme for catechol generation	Pseudomonas putida

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Release 2023.1 (January 2023)