Maveyraud Laurent, Golemi-Kotra Dasantila, Ishiwata Akihiro, Meroueh Oussama, Mobashery Shahriar, Samama Jean-Pierre
Groupe de Cristallographie Biologique, Institut de Pharmacologie et de Biologie Structurale du CNRS, 205 route de Narbonne, 31077-Toulouse Cedex, France.
J Am Chem Soc. 2002 Mar 20;124(11):2461-5. doi: 10.1021/ja016736t.
Beta-lactamases are resistance enzymes for beta-lactam antibiotics. These enzymes hydrolyze the beta-lactam moieties of these antibiotics, rendering them inactive. Of the four classes of known beta-lactamases, the enzymes of class D are the least understood. We report herein the high-resolution (1.9 A) crystal structure of the class D OXA-10 beta-lactamase inhibited by a penicillanate derivative. The structure provides evidence that the carboxylated Lys-70 (a carbamate) is intimately involved in the mechanism of the enzyme.
β-内酰胺酶是β-内酰胺类抗生素的耐药酶。这些酶水解这些抗生素的β-内酰胺部分，使其失去活性。在已知的四类β-内酰胺酶中，D类酶是了解最少的。我们在此报告了被青霉素酸衍生物抑制的D类OXA-10β-内酰胺酶的高分辨率（1.9 Å）晶体结构。该结构提供了证据，表明羧化的赖氨酸-70（一种氨基甲酸酯）密切参与了该酶的作用机制。
