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Type: Journal article
Title: Secreted enzymes of Aeromonas
Author: Pemberton, J.M.
Kidd, S.P.
Schmidt, R.
Citation: FEMS Microbiology Letters, 1997; 152(1):1-10
Publisher: Oxford University Press
Issue Date: 1997
ISSN: 0378-1097
Statement of
John M Pemberton, Stephen P Kidd, Radomir Schmidt
Abstract: A hallmark characteristic of species of Aeromonas is their ability to secrete a wide variety of enzymes associated with pathogenicity and environmental adaptability. Among the most intensively studied are β-lactamases, lipases, hemolytic enterotoxins, proteases, chitinases, nucleases and amylases. Multiple copies of genes encoding each type of enzyme provide additional biological diversity. Except for the chitinases, these multiple copies show little evolutionary relatedness at the DNA level and only limited similarity at the protein level. Indeed a number of the genes, such as nuclease H of A. hydrophila, have no similarity to known prokaryotic or eukaryotic sequences. The challenge is to determine how these genes evolved, where they originated and why Aeromonas possesses them in such abundance and variety.
Keywords: Secretion; Aeromonas; Extracellular enzyme; Pathogenicity; Evolution
Rights: © 1997 Federation of European Microbiological Societies
DOI: 10.1111/j.1574-6968.1997.tb10401.x
Appears in Collections:Aurora harvest 7
Molecular and Biomedical Science publications

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