Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Catalytic spectrum of the penicillin-binding protein 4 of Pseudomonas aeruginosa, a nexus for the induction of β-lactam antibiotic resistance.
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Purified PA3047 PBP4 has DD-carboxypeptidase and 4,3-specific DD-endopeptidase activities of similar efficiency.
"PBP4 catalyzes both reactions equally well."
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Cefoxitin induction increases stem pentapeptide and 4,3-cross-linked peptidoglycan, which feed the muropeptide recycling pathway that controls AmpC.
"In the presence of β-lactam antibiotics these altered cell-wall segments enter into the muropeptide recycling pathway"
In vivo functional and molecular characterization of the Penicillin-Binding Protein 4 (DacB) of Pseudomonas aeruginosa.
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In vivo, P. aeruginosa PBP4 behaves predominantly as a D,D-endopeptidase.
"LMM-PBP4 of Pseudomonas aeruginosa is a bifunctional enzyme presenting both D,D-carboxypeptidase and D,D-endopeptidase activities; the D,D-endopeptidase function is predominant."