的分子表征enterobacterial beta-lactamase发现在临床分离的金属粘质沙雷氏菌显示imipenem阻力。
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研究员合作Osano E,荒川Y, Wacharotayankun R, M, Horii T, Ito H, Yoshimura F,加藤N
的分子表征enterobacterial beta-lactamase发现在临床分离的金属粘质沙雷氏菌显示imipenem阻力。
Antimicrob代理Chemother。1994年1月,38 (1):71 - 8。
- PubMed ID
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8141584 (在PubMed]
- 文摘
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临床分离的粘质沙雷氏菌(TN9106)产生一个beta-lactamase金属(IMP-1)授予imipenem阻力和广谱beta-lactams。blaIMP基因提供imipenem阻力在大肠杆菌HB101克隆和表达。从大肠杆菌HB101 IMP-1被净化,港口pSMBNU24 blaIMP,及其明显的分子质量计算大约30 kDa的钠十二烷基sulfate-polyacrylamide凝胶电泳。beplayapp对各种动力学研究IMP-1 beta-lactams透露,这种酶水解不仅各种广谱beta-lactams而且碳青霉烯。然而,对IMP-1 aztreonam是相对稳定的。虽然clavulanate或邻氯青霉素未能抑制IMP-1, Hg2 +价或Cu2 +封锁了酶的活动。此外,EDTA在反应中缓冲区的存在导致减少酶的活动。碳青霉烯耐药并没有从美国转移marcescens TN9106大肠杆菌CSH2接合。杂交的一项研究证实,blaIMP编码的染色体是美国marcescens TN9106。通过核苷酸序列分析,发现blaIMP编码246个氨基酸残基的蛋白质,并证明有相当大的金属beta-lactamase基因的同源性蜡样芽胞杆菌、脆弱拟杆菌,气单胞菌属hydrophila。 The G+C content of blaIMP was 39.4%. Four consensus amino acid residues, His-95, His-97, Cys-176, and His-215, which form putative zinc ligands, were conserved in the deduced amino acid sequence of IMP-1. By determination of the amino acid sequence at the N terminus of purified mature IMP-1, 18 amino acid residues were found to be processed from the N terminus of the premature enzyme as a signal peptide. These results clearly show that IMP-1 is an enterobacterial metallo beta-lactamase, of which the primary structure has been completely determined, that confers resistance to carbapenems and other broad-spectrum beta-lactams.