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URN: urn:nbn:de:swb:90-627916
DOI: 10.1186/s12858-016-0063-z
Zitationen: 5
Web of Science
Zitationen: 4

Substrate specificity and function of acetylpolyamine amidohydrolases from Pseudomonas aeruginosa

Krämer, Andreas; Herzer, Jan; Overhage, Jörg; Meyer-Almes, Franz-Josef

Background: 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 of P. aeruginosa and particularly the deacetylation of acetylpolyamines has been little studied up to now. Results with other bacterial pathogens e.g., Y. pestis suggest that polyamines may be involved in the formation of biofilms or confer resistance against certain antibiotics.
Results: To elucidate the role of acetylpolyamines and their enzymatic deacetylation in more detail, all three putative acetylpolyamine amidohydrolases (APAHs) from P. aeruginosa have been expressed in enzymatic active form. The APAHs PA0321 and PA1409 are shown to be true polyamine deacetylases, whereas PA3774 is not able to deacetylate acetylated polyamines. Every APAH can hydrolyze trifluoroacetylated lysine-derivatives, but only PA1409 and much more efficiently PA3774 can also process the plain acetylated lysine substrate. P. aeruginosa is able to utilize acetylcad ... mehr

Zugehörige Institution(en) am KIT Institut für Funktionelle Grenzflächen (IFG)
Publikationstyp Zeitschriftenaufsatz
Jahr 2016
Sprache Englisch
Identifikator ISSN: 1471-2091
KITopen ID: 1000062791
HGF-Programm 47.02.06; LK 01
Erschienen in BMC biochemistry
Band 17
Heft 1
Seiten Art.Nr.: 63
Schlagworte Acetylpolyamine amidohydrolases, Pseudomonas aeruginosa, Substrate specificity, Acetylpolyamines, Polyamine metabolism
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