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- W2002668704 abstract "β-lactams inhibit peptidoglycan polymerization by acting as suicide substrates of essential d,d-transpeptidases. Bypass of these enzymes by unrelated l,d-transpeptidases results in β-lactam resistance, although carbapenems remain unexpectedly active. To gain insight into carbapenem specificity of l,d-transpeptidases (Ldts), we solved the nuclear magnetic resonance (NMR) structures of apo and imipenem-acylated Bacillus subtilis Ldt and show that the cysteine nucleophile is present as a neutral imidazole-sulfhydryl pair in the substrate-free enzyme. NMR relaxation dispersion does not reveal any preexisting conformational exchange in the apoenzyme, and change in flexibility is not observed upon noncovalent binding of β-lactams (KD > 37.5 mM). In contrast, covalent modification of active cysteine by both carbapenems and 2-nitro-5-thiobenzoate induces backbone flexibility that does not result from disruption of the imidazole-sulfhydryl proton interaction or steric hindrance. The chemical step of the reaction determines enzyme specificity since no differences in drug affinity were observed." @default.
- W2002668704 created "2016-06-24" @default.
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- W2002668704 date "2012-05-01" @default.
- W2002668704 modified "2023-10-14" @default.
- W2002668704 title "Dynamics Induced by β-Lactam Antibiotics in the Active Site of Bacillus subtilis l,d-Transpeptidase" @default.
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- W2002668704 doi "https://doi.org/10.1016/j.str.2012.03.015" @default.
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