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In order to get insights into the molecular mechanisms underlying the ability of <jats:italic>Pseudomonas sp.<\/jats:italic> M1 to catabolize \u03b2\u2010myrcene, an expression proteomics approach was used in this study. Results indicate that the catabolic enzyme machinery for \u03b2\u2010myrcene utilization (MyrB, MyrC, and MyrD and other uncharacterized proteins) is strongly induced when \u03b2\u2010myrcene is present in the growth medium. Since an M1 mutant, lacking a functional 2\u2010methylisocitrate dehydratase, is not able to grow in mineral medium with \u03b2\u2010myrcene or propionic acid as the sole C\u2010source, and also based on the expression proteomic analysis carried out in this study, it is suggested that the \u03b2\u2010myrcene catabolic intermediate propionyl\u2010CoA is channeled into the central metabolism <jats:italic>via<\/jats:italic> the 2\u2010methylcitrate cycle. Results also suggest that the major alteration occurring in the central carbon metabolism of cells growing in \u03b2\u2010myrcene\u2010containing media is related with the redistribution of the metabolic fluxes leading to increased oxaloacetate production. Other up\u2010regulated proteins are believed to prevent protein misfolding and aggregation or to play important structural roles, contributing to the adaptive alteration of cell wall and membrane organization and integrity, which are essential features to allow the bacterium to cope with the highly lipophilic \u03b2\u2010myrcene as C\u2010source.<\/jats:p>","DOI":"10.1002\/pmic.200900325","type":"journal-article","created":{"date-parts":[[2009,10,1]],"date-time":"2009-10-01T11:30:02Z","timestamp":1254396602000},"page":"5101-5111","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Adaptation to \u03b2\u2010myrcene catabolism in <i>Pseudomonas<\/i> sp. 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