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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The catalytic mechanism of β-lactamases: NMR titration of an active-site lysine residue of the TEM-1 enzyme
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The catalytic mechanism of β-lactamases: NMR titration of an active-site lysine residue of the TEM-1 enzyme

机译:β-内酰胺酶的催化机理:TEM-1酶活性位点赖氨酸残基的NMR滴定

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摘要

β-Lactamases are widespread in the bacte- rial world, where they are responsible for resistance to pen- icillins, cephalosporins, and related compounds, currently the most widely used antibacterial agents. Detailed structural and mechanistic understanding of these enzymes can be expected to guide the design of new antibacterial compounds resistant to their action. A number of high-resolution structures are available for class A β-lactamases, whose catalytic mechanism involves the acylation of a serine residue at the active site.
机译:β-内酰胺酶在细菌界很普遍,它们对青霉素,头孢菌素和相关化合物(目前使用最广泛的抗菌剂)产生抗性。可以预期对这些酶的详细结构和机理的理解将指导对它们的作用具有抗性的新抗菌化合物的设计。 A类β-内酰胺酶具有许多高分辨率结构,其催化机制包括在活性位点丝氨酸残基的酰化。

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