Structural and functional insight of New Delhi Metallo β-lactamase-1 variants

被引:19
作者
Khan, Sidra [1 ]
Ali, Abid [1 ]
Khan, Asad U. [1 ]
机构
[1] Aligarh Muslim Univ, Med Microbiol & Mol Biol Lab, Interdisciplinary Biotechnol Unit, Aligarh 202002, Uttar Pradesh, India
关键词
beta-lactam; antibiotics; hydrolysis; loops; mechanism; mutations; NDM-1; New Delhi Metallo-beta-lactamase-1; resistance; variants; BETA-LACTAMASE VARIANT; COLI CLINICAL ISOLATE; ANTIBIOTIC-RESISTANCE; KLEBSIELLA-PNEUMONIAE; CRYSTAL-STRUCTURE; SUBSTRATE RECOGNITION; NDM-1; CARBAPENEMASE; HYDROLYSIS; REVEALS;
D O I
10.4155/fmc-2017-0143
中图分类号
R914 [药物化学];
学科分类号
100701 ;
摘要
New Delhi Metallo beta-lactamase-1 (NDM-1) is a member of the Metallo-beta-lactamase family, capable of catalyzing the hydrolysis of all beta-lactam antibiotics. The rapid dissemination of NDM producers, 'superbugs', has become a worldwide concern to health workers. Seventeen different variants of NDM have been reported so far, across the world. These variants varied in their sequences either by single or multiple amino acid substitutions. This review summarizes the crystal structure of NDM and provides a comparative analysis of all variants. Moreover, we have for the first time highlighted the role of a-helix, beta-sheet and loop structures of NDM enzyme, having different mutations occurred in these regions. The effect of these substitutions on its structure and functional aspect has to be thoroughly understood to design effective inhibitors in future.
引用
收藏
页码:221 / 229
页数:9
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