National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences , Beijing 100101, China.
J Am Chem Soc. 2014 Oct 22;136(42):14694-7. doi: 10.1021/ja508388e. Epub 2014 Oct 7.
Cephalosporins constitute a large class of β-lactam antibiotics clinically used as antimicrobial drugs. New Dehli metallo-β-lactamase (NDM-1) poses a global threat to human health as it confers on bacterial pathogen resistance to almost all β-lactams, including penicillins, cephalosporins, and carbapenems. Here we report the first crystal structures of NDM-1 in complex with cefuroxime and cephalexin, as well as NMR spectra monitoring cefuroxime and cefixime hydrolysis catalyzed by NDM-1. Surprisingly, cephalosporoate intermediates were captured in both crystal structures determined at 1.3 and 2.0 Å. These results provide detailed information concerning the mechanism and pathways of cephalosporin hydrolysis. We also present the crystal structure and enzyme assays of a D124N mutant, which reveals that D124 most likely plays a more structural than catalytic role.
头孢菌素类抗生素属于β-内酰胺类抗生素,临床上作为抗菌药物使用。新德里金属β-内酰胺酶(NDM-1)对人类健康构成了全球性威胁,因为它使细菌病原体对几乎所有β-内酰胺类抗生素(包括青霉素类、头孢菌素类和碳青霉烯类)产生耐药性。在这里,我们报告了 NDM-1 与头孢呋辛和头孢氨苄复合物的第一个晶体结构,以及监测 NDM-1 催化头孢呋辛和头孢克肟水解的 NMR 谱。令人惊讶的是,在两个分别以 1.3 和 2.0 Å分辨率测定的晶体结构中均捕获到了头孢菌素中间体。这些结果提供了有关头孢菌素水解机制和途径的详细信息。我们还展示了 D124N 突变体的晶体结构和酶测定结果,表明 D124 很可能主要起结构作用而不是催化作用。