Orthologous and Paralogous AmpD Peptidoglycan Amidases from Gram-Negative Bacteria.
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.
1 Department of Crystallography and Structural Biology, Institute of Química-Física "Rocasolano," CSIC, Madrid, Spain .
Ivanna
I
Rivera
1 Department of Crystallography and Structural Biology, Institute of Química-Física "Rocasolano," CSIC, Madrid, Spain .
Rafael
R
Molina
2 Department of Chemistry and Biochemistry, University of Notre Dame , Notre Dame, Indiana.
Mijoon
M
Lee
2 Department of Chemistry and Biochemistry, University of Notre Dame , Notre Dame, Indiana.
Shahriar
S
Mobashery
1 Department of Crystallography and Structural Biology, Institute of Química-Física "Rocasolano," CSIC, Madrid, Spain .
Juan A
JA
Hermoso
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020134:Catalytic Domain; D002473:Cell Wall / Q000737:chemistry / Q000201:enzymology*; D004352:Drug Resistance, Microbial / Q000235:genetics; D004755:Enterobacteriaceae / Q000201:enzymology* / Q000235:genetics; D015870:Gene Expression; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D045726:Metalloproteases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010457:Peptidoglycan / Q000378:metabolism; D019897:Periplasm / Q000737:chemistry / Q000201:enzymology*; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000235:genetics; D040681:Structural Homology, Protein; D037521:Virulence Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D007527:Isoenzymes; D010457:Peptidoglycan; D037521:Virulence Factors; C586328:AmpDh2 protein, Pseudomonas aeruginosa; D045726:Metalloproteases; C062460:AmpD protein, Bacteria; D009238:N-Acetylmuramoyl-L-alanine Amidase