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- W2013904750 abstract "X-ray crystallography has been used to examine the binding of three members of the beta-lactam family of antibiotics to the D-alanyl-D-alanine peptidase from Streptomyces R61, a target of penicillins. Cephalosporin C, the monobactam analog of penicillin G and (2,3)-alpha-methylene benzylpenicillin have been mapped at 2.3 A resolution in the form of acyl-enzyme complexes bound to serine 62. On the basis of the positions of these inhibitors, the binding of a tripeptide substrate for the enzyme, L-lysyl-D-alanyl-D-alanine, has been modeled in the active site. The binding of both inhibitors and substrate is facilitated by hydrogen-bonding interactions with a conserved beta-strand (297-303), which is antiparallel to the beta-lactam's acylamide linkage or the substrate's peptide bond. The active site is similar to that in beta-lactamases." @default.
- W2013904750 created "2016-06-24" @default.
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- W2013904750 date "1989-09-01" @default.
- W2013904750 modified "2023-09-24" @default.
- W2013904750 title "Crystallographic mapping of β-lactams bound to a d-alanyl-d-alanine peptidase target enzyme" @default.
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- W2013904750 doi "https://doi.org/10.1016/0022-2836(89)90277-5" @default.
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