Substrate and Stereochemical Control of Peptidoglycan Cross-Linking by Transpeptidation by
| Autor: | Anita C, Catherwood, Adrian J, Lloyd, Julie A, Tod, Smita, Chauhan, Susan E, Slade, Grzegorz P, Walkowiak, Nicola F, Galley, Avinash S, Punekar, Katie, Smart, Dean, Rea, Neil D, Evans, Michael J, Chappell, David I, Roper, Christopher G, Dowson |
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| Rok vydání: | 2020 |
| Předmět: |
Polyisoprenyl Phosphate Monosaccharides
Escherichia coli Proteins Polyisoprenyl Phosphate Oligosaccharides Stereoisomerism Peptidoglycan Serine-Type D-Ala-D-Ala Carboxypeptidase Substrate Specificity Kinetics Biocatalysis Escherichia coli Penicillin-Binding Proteins Peptidoglycan Glycosyltransferase Bacterial Outer Membrane Proteins Enzyme Assays |
| Zdroj: | Journal of the American Chemical Society. 142(11) |
| ISSN: | 1520-5126 |
| Popis: | Penicillin binding proteins (PBPs) catalyzing transpeptidation reactions that stabilize the peptidoglycan component of the bacterial cell wall are the targets of β-lactams, the most clinically successful antibiotics to date. However, PBP-transpeptidation enzymology has evaded detailed analysis, because of the historical unavailability of kinetically competent assays with physiologically relevant substrates and the previously unappreciated contribution of protein cofactors to PBP activity. By re-engineering peptidoglycan synthesis, we have constructed a continuous spectrophotometric assay for transpeptidation of native or near native peptidoglycan precursors and fragments by |
| Databáze: | OpenAIRE |
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