Orthologous and Paralogous AmpD Peptidoglycan Amidases from Gram-Negative Bacteria

Ivanna Rivera, Rafael Molina, Mijoon Lee, Shahriar Mobashery, Juan A Hermoso

12 Citationer (Scopus)

Abstract

Cell wall recycling and β-lactam antibiotic resistance are linked in Enterobacteriaceae and in Pseudomonas aeruginosa. This process involves a large number of murolytic enzymes, among them a cytoplasmic peptidoglycan amidase AmpD, which plays an essential role by cleaving the peptide stem from key intermediates en route to the β-lactamase production (a resistance mechanism) and cell wall recycling. Uniquely, P. aeruginosa has two additional paralogues of AmpD, designated AmpDh2 and AmpDh3, which are periplasmic enzymes. Despite the fact that AmpDh2 and AmpDh3 share a common motif for their respective catalytic domains, they are each comprised of multidomain architectures and exhibit distinct oligomerization properties. We review herein the structural and biochemical properties of orthologous and paralogous AmpD proteins and discuss their implication in cell wall recycling and antibiotic resistance processes.

OriginalsprogEngelsk
TidsskriftMicrobial Drug Resistance
Vol/bind22
Udgave nummer6
Sider (fra-til)470-6
Antal sider7
ISSN1076-6294
DOI
StatusUdgivet - sep. 2016

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