Promden Worrawat, Vangnai Alisa S, Pongsawasdi Piamsook, Adachi Osao, Matsushita Kazunobu, Toyama Hirohide
Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, Thailand.
FEMS Microbiol Lett. 2008 Mar;280(2):203-9. doi: 10.1111/j.1574-6968.2008.01060.x. Epub 2008 Jan 19.
Pseudomonas putida HK5 produces three different quinoprotein alcohol dehydrogenases: ADH-I, ADH-IIB and ADH-IIG. Gene organization of qedA, the gene for ADH-I, and other 10 genes in the cluster was related to the genome sequences of five other Pseudomonas strains. Insertion mutations in either qedA, exaE or agmR eliminated ADH-I activity, although the mutants were still able to grow on ethanol but more slowly than the wild-type strain. Mutant analysis demonstrated the requirement of agmR and exaE in ADH-I expression, and the tentative involvement of agmR, but not exaE, in the induction of ADH-IIB and ADH-IIG activities.