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• W19889520 endingPage "627" @default.
• W19889520 startingPage "621" @default.
• W19889520 abstract "An acyl-enzyme was isolated from certain chromosomal beta-lactamases and a penicillin. The penicillin was cloxacillin which, although it is a substrate for these enzymes, has such a low kcat. that it functions as an inhibitor. The enzymes were from the mutant of Pseudomonas aeruginosa 18 S that produces the beta-lactamase constitutively [Flett, Curtis & Richmond (1976) J. Bacteriol. 127, 1585-1586; Berks, Redhead & Abraham (1982) J. Gen. Microbiol., in the press] and from Escherichia coli K-12 (the ampC beta-lactamase) [Boman, Nordström & Normak (1974) Ann. N.Y. Acad. Sci. 235, 569-586]. The acyl-enzymes have been degraded to determine the residue labelled, and the sequence around it. The residue labelled is serine. The sequences around the labelled serine in these two beta-lactamases are exceedingly similar. However, the sequences are quite different from those around the active site serine in the beta-lactamases previously studied. There is thus more than one class of serine beta-lactamases." @default.
• W19889520 created "2016-06-24" @default.
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• W19889520 date "1982-03-01" @default.
• W19889520 modified "2023-10-11" @default.
• W19889520 title "Active sites of β-lactamases. The chromosomal β-lactamases of <i>Pseudomonas aeruginosa</i> and <i>Escherichia coli</i>" @default.
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• W19889520 doi "https://doi.org/10.1042/bj2010621" @default.
• W19889520 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1163689" @default.
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