acylation mechanism; ab initio study; beta-lactamases
Abstract :
[en] The acylation reaction of beta-lactamases by beta-lactam compounds is modeled as a one-step process. Twenty seven transition-state models are investigated at the restricted Hartree-Fock (RHF) level within the minimal MINI-1' basis set. These transition states differ by the nature of both the substrate and the amino acids constituting the reactive nucleophile. The intrinsic reactivity of the class-A and class-C beta-lactamases are under concern. Eight transition-state models were docked in a class-A beta-lactamase, TEM1, as optimized with the benzylpenicillin at the molecular mechanics level. In the proposed one-step acylation process, only two amino acids are directly involved, the usual nucleophilic serine, S70 in TEM1, and a close serine or tyrosine, S130 in TEM1, Y150 in P99. The lysine close to these two residues, K73 in TEM1, plays only an indirect role in the process. (C) 1999 John Wiley & Sons, Inc. Int J Quant Chem 73: 161-174, 1999.
Disciplines :
Mathematics
Author, co-author :
Dive, Georges ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Dehareng, Dominique ; Université de Liège - ULiège > Centre d'ingénierie des protéines
scite shows how a scientific paper has been cited by providing the context of the citation, a classification describing whether it supports, mentions, or contrasts the cited claim, and a label indicating in which section the citation was made.
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