Substrate specificity and function of acetylpolyamine amidohydrolases from Pseudomonas aeruginosa

摘要: Pseudomonas aeruginosa, a Gram-negative, aerobic coccobacillus bacterium is an opportunistic human pathogen and worldwide the fourth most common cause of hospital-acquired infections which are often high mortality such as ventilator-associated pneumoniae. The polyamine metabolism P. aeruginosa particularly deacetylation acetylpolyamines has been little studied up to now. Results with other bacterial pathogens e.g., Y. pestis suggest that polyamines may be involved in formation biofilms or confer resistance against certain antibiotics. To elucidate role their enzymatic more detail, all three putative acetylpolyamine amidohydrolases (APAHs) from have expressed active form. APAHs PA0321 PA1409 shown true deacetylases, whereas PA3774 not able deacetylate acetylated polyamines. Every APAH can hydrolyze trifluoroacetylated lysine-derivatives, but only much efficiently also process plain lysine substrate. utilize acetylcadaverine acetylputrescine carbon source under glucose starvation. If either gene disrupted, growth reduced delayed. In addition, we were show inhibitors SAHA SATFMK induce biofilm both PA14 PAO1 wildtype strains. two functional APAHs, enable utilization for aeruginosa. contrast, physiological predicted APAH, PA3774, remains elucidated. Its ability synthetic substrates points protein functionality yet unknown substrates.