β-内酰胺酶中底物诱导构象变化的直接核磁共振证据。
Direct n.m.r. evidence for substrate-induced conformational changes in a beta-lactamase.
作者信息
Jamin M, Damblon C, Bauduin-Misselyn A M, Durant F, Roberts G C, Charlier P, Llabres G, Frère J M
机构信息
Laboratoire d'Enzymologie, Université de Liège, Belgium.
出版信息
Biochem J. 1994 Jul 1;301 ( Pt 1)(Pt 1):199-203. doi: 10.1042/bj3010199.
Abstract
Cefoxitin and other beta-lactam antibiotics with a methoxy group on the alpha-face behave as very poor substrates of the Bacillus licheniformis beta-lactamase. The kinetic properties of the enzyme-cefoxitin system made it theoretically suitable for a detailed structural study of the acyl-enzyme. Unfortunately, soaking the crystals in cefoxitin solution did not allow detection of a crystalline acyl-enzyme complex. In contrast, direct observation by n.m.r. of the stable acyl-enzyme formed with cefoxitin and moxalactam indicated clear modifications of the enzyme structure, which were reflected in the aromatic and high-field methyl regions of the spectrum. The return to the initial free enzyme spectrum was concomitant with the hydrolysis of the acyl-enzyme, the process being slow enough to allow multidimensional n.m.r. experiments.
摘要
头孢西丁和其他在α面带有甲氧基的β-内酰胺抗生素是地衣芽孢杆菌β-内酰胺酶的极差底物。酶-头孢西丁系统的动力学特性使其在理论上适合对酰基酶进行详细的结构研究。不幸的是，将晶体浸泡在头孢西丁溶液中无法检测到结晶酰基酶复合物。相比之下，通过核磁共振直接观察由头孢西丁和莫拉卡坦形成的稳定酰基酶，结果表明酶结构发生了明显改变，这在光谱的芳香族和高场甲基区域有所体现。酰基酶水解时会恢复到初始的游离酶光谱，该过程足够缓慢，从而能够进行多维核磁共振实验。
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