Krzeslak, Joanna and Wahjudi, Mariana and Quax, Wim J. (2007) Quorum-Quenching Acylases in Pseudomonas aeruginosa. In: Pseudomonas: A Model System in Biology. Springer, Spain, pp. 27-45. ISBN 978-1-4020-6097-7
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Abstract
The β-lactam acylases, mostly found by screening samples from natural sources, represent a unique family of heterodimeric N-terminal nucleophile hydrolases. Interestingly, most of the strains found producing β-lactam acylases are Pseudomonas species. We have shown that these enzymes show high selectivity towards the acid side chain, but are far more promiscuous with regard to the amine moiety of the substrate. It is therefore highly unlikely that the industrially relevant deacylation of β-lactam compounds has evolved specifically in nature. Interestingly, no less than four putative acylases of the N-terminal nucleophile family have been identified in the Pseudomonas aeruginosa PAO1 genome. We have investigated these four putative acylases of which one could be expressed in Escherichia coli. Interestingly, the enzyme was found to catalyse the hydrolysis of acylhomoserine- lactones as reported for Ralstonia acylase suggesting a role in quorum quenching...
| Item Type: | Book Section |
|---|---|
| Subjects: | Q Science > QR Microbiology |
| Divisions: | Faculty of Technobiology > Department of Biology |
| Depositing User: | Eko Setiawan 194014 |
| Date Deposited: | 26 Sep 2014 05:51 |
| Last Modified: | 24 Mar 2021 16:29 |
| URI: | http://repository.ubaya.ac.id/id/eprint/20925 |
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