Reactions of the Three AmpD Enzymes of Pseudomonas aeruginosa

A group of Gram-negative bacteria, including the problematic pathogen Pseudomonas aeruginosa, has linked the steps in cell-wall recycling with the ability to manifest resistance to β-lactam antibiotics. A key step at the crossroads of the two events is performed by the protease AmpD, which hydrolyze...

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Published inJournal of the American Chemical Society Vol. 135; no. 13; pp. 4950 - 4953
Main Authors Zhang, Weilie, Lee, Mijoon, Hesek, Dusan, Lastochkin, Elena, Boggess, Bill, Mobashery, Shahriar
Format Journal Article
LanguageEnglish
Published WASHINGTON American Chemical Society 03.04.2013
Amer Chemical Soc
Subjects
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Chemistry
Chemistry, Multidisciplinary
Chromatography, High Pressure Liquid
Metalloproteases - chemistry
Metalloproteases - metabolism
Physical Sciences
Pseudomonas aeruginosa - enzymology
Science & Technology
Virulence Factors - chemistry
Virulence Factors - metabolism
BETA-LACTAM RESISTANCE
BACTERIA
TURNOVER
ESCHERICHIA-COLI
KINETIC MECHANISM
LYTIC TRANSGLYCOSYLASES
LEVEL
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Summary:A group of Gram-negative bacteria, including the problematic pathogen Pseudomonas aeruginosa, has linked the steps in cell-wall recycling with the ability to manifest resistance to β-lactam antibiotics. A key step at the crossroads of the two events is performed by the protease AmpD, which hydrolyzes the peptide in the metabolite that influences these events. In contrast to other organisms that harbor this elaborate system, the genomic sequences of P. aeruginosa reveal it to have three paralogous genes for this protease, designated as ampD, ampDh2, and ampDh3. The recombinant gene products were purified to homogeneity, and their functions were assessed by the use of synthetic samples of three bacterial metabolites in cell-wall recycling and of three surrogates of cell-wall peptidoglycan. The results unequivocally identify AmpD as the bona fide recycling enzyme and AmpDh2 and AmpDh3 as enzymes involved in turnover of the bacterial cell wall itself. These findings define for the first time the events mediated by these three enzymes that lead to turnover of a key cell-wall recycling metabolite as well as the cell wall itself in its maturation.
Bibliography:NIH RePORTER
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ISSN:0002-7863
1520-5126
DOI:10.1021/ja400970n