Walsh T R, Gamblin S, Emery D C, MacGowan A P, Bennett P M
Department of Microbiology and Pathology, School of Medical Sciences, University of Bristol, UK.
J Antimicrob Chemother. 1996 Mar;37(3):423-31. doi: 10.1093/jac/37.3.423.
The metallo-beta-lactamase from Aeromonas sobria 163a, ImiS, was isolated in a two stage purification procedure using protein affinity columns. Enzyme kinetics show that ImiS hydrolyses the carbapenems but displays poor activity against other beta-lactams. ImiS possesses the narrowest spectrum of activity of the Group 3 enzymes that have been analysed. Sequencing of the 40 N-terminal amino acids show this region to be identical to that of the CphA metallo-beta-lactamase from Aeromonas hydrophila (Massidda, Rossolini & Satta, 1991). Light scattering analysis indicates that ImiS is functionally active as a monomer.
嗜水气单胞菌163a的金属β-内酰胺酶ImiS是通过使用蛋白质亲和柱的两步纯化程序分离得到的。酶动力学表明，ImiS可水解碳青霉烯类，但对其他β-内酰胺类的活性较差。ImiS在已分析的3类酶中具有最窄的活性谱。对40个N端氨基酸的测序表明，该区域与嗜水气单胞菌的CphA金属β-内酰胺酶的相应区域相同（马西达、罗索利尼和萨塔，1991年）。光散射分析表明，ImiS作为单体具有功能活性。
