Wang Z, Fast W, Valentine A M, Benkovic S J
The Pennsylvania State University, Department of Chemistry, 152 Davey Laboratory, University Park, PA 16802, USA.
Curr Opin Chem Biol. 1999 Oct;3(5):614-22. doi: 10.1016/s1367-5931(99)00017-4.
This past year has produced determinations of X-ray crystal structures for three metallo-beta-lactamases and the elucidation of the catalytic mechanisms for a monozinc and a dizinc enzyme. These advances shed light on how such a diverse group of enzymes are evolving to inactivate so efficiently a broad spectrum of beta-lactam antibiotics.
在过去的一年里，已确定了三种金属β-内酰胺酶的X射线晶体结构，并阐明了一种单锌酶和一种双锌酶的催化机制。这些进展揭示了如此多样的一组酶是如何进化以如此有效地使广谱β-内酰胺抗生素失活的。
