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Disruption of quinoprotein ethanol dehydrogenase gene and adjacent genes in Pseudomonas putida HK5. 2008
Worrawat Promden, and
Alisa S Vangnai, and
Piamsook Pongsawasdi, and
Osao Adachi, and
Kazunobu Matsushita, and
Hirohide Toyama
Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, Thailand.
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.
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