Reactions of the three AmpD enzymes of Pseudomonas aeruginosa.
-
AmpDh2 and AmpDh3 prefer cell-wall peptidoglycan surrogates over the anhydromuramyl recycling metabolites.
"Hence, it is clear that AmpDh2 and AmpDh3 have evolved as enzymes for processing of the peptidoglycan components of the cell wall in the periplasmic space."
-
Purified ampDh2 removes stem peptides from P. aeruginosa sacculus.
"Overnight incubation of the polymeric sacculus with AmpDh2 produced products with oligomeric cell-wall sugars without the peptide stem."
-
The location of the paralogues was taken from earlier work or proposed, not assayed in this paper.
"If AmpDh2 and AmpDh3 were to be periplasmic enzymes, as proposed in this report"
-
The marginal anhydromuropeptide activity is proposed to explain the stepwise AmpC derepression seen genetically.
"Nonetheless, the marginal activity in turnover of metabolite 1 with AmpDh2 and AmpDh3 explains the stepwise effect observed in augmenting derepression of AmpC β-lactamase by eliminations of these enzymes one-by-one."
Cell-wall remodeling by the zinc-protease AmpDh3 from Pseudomonas aeruginosa.
-
AmpDh2 is an outer-membrane-inserted dimer that hydrolyses the sacculus.
"AmpDh2 is a dimeric protein that inserts itself into the inner leaflet of the outer membrane, where it interacts and hydrolyzes the amide bond between the stem peptide and the NAM moiety of the sacculus."
-
AmpDh2 and AmpDh3 together remodel the cell wall.
"The present study documents that AmpDh2 and AmpDh3 complement each other in remodeling of the cell wall."
Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
UniProtKB Q9HT86 flat file