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本文引用的文献

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beta-Lactamase-catalyzed hydrolysis of acyclic depsipeptides and acyl transfer to specific amino acid acceptors.β-内酰胺酶催化的无环缩肽水解及酰基转移至特定氨基酸受体。
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A spectrophotometric assay of beta-lactamase action on penicillins.一种关于β-内酰胺酶对青霉素作用的分光光度测定法。
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The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution.白色链霉菌G的β-内酰胺酶在0.3纳米分辨率下的晶体结构。
Biochem J. 1987 Aug 1;245(3):911-3. doi: 10.1042/bj2450911.
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Kinetics and mechanism of the serine beta-lactamase catalyzed hydrolysis of depsipeptides.丝氨酸β-内酰胺酶催化缩肽水解的动力学与机制
Biochemistry. 1987 Jun 16;26(12):3385-95. doi: 10.1021/bi00386a021.
6
Bacterial resistance to beta-lactam antibiotics: crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.5 A resolution.细菌对β-内酰胺抗生素的耐药性：金黄色葡萄球菌PC1的β-内酰胺酶在2.5埃分辨率下的晶体结构。
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Recent developments in beta-lactamase research and their implications for the future.β-内酰胺酶研究的最新进展及其对未来的影响。
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A类β-内酰胺酶的膦酸单酯抑制剂

Phosphonate monoester inhibitors of class A beta-lactamases.

作者信息

Rahil J, Pratt R F

机构信息

Department of Chemistry, Wesleyan University, Middletown, CT 06457.

出版信息

Biochem J. 1991 May 1;275 ( Pt 3)(Pt 3):793-5. doi: 10.1042/bj2750793.

DOI:10.1042/bj2750793
PMID:1903928
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1150124/
Abstract

Phosphonate monoesters with the general structure: [formula: see text] are inhibitors of representative class A and class C beta-lactamases. This result extends the range of this type of inhibitor to the class A enzymes. Compounds where X is an electron-withdrawing substituent are better inhibitors than the unsubstituted analogue (X = H), and enzyme inhibition is concerted with stoichiometric release of the substituted phenol. Slow turnover of the phosphonates also occurs. These observations support the proposition that the mechanism of action of these inhibitors involves phosphorylation of the beta-lactamase active site. The inhibitory ability of these phosphonates suggests that the beta-lactamase active site is very effective at stabilizing negatively charged transition states. One of the compounds described also inactivated the Streptomyces R61 D-alanyl-D-alanine carboxypeptidase/transpeptidase.

摘要

具有以下通式结构的膦酸单酯

[化学式：见原文]是典型的A类和C类β-内酰胺酶抑制剂。这一结果将此类抑制剂的范围扩展至A类酶。X为吸电子取代基的化合物比未取代类似物（X = H）是更好的抑制剂，并且酶抑制作用与取代酚的化学计量释放协同发生。膦酸酯也会出现缓慢周转。这些观察结果支持了这些抑制剂的作用机制涉及β-内酰胺酶活性位点磷酸化的观点。这些膦酸酯的抑制能力表明β-内酰胺酶活性位点在稳定带负电荷的过渡态方面非常有效。所描述的化合物之一还使链霉菌R61 D-丙氨酰-D-丙氨酸羧肽酶/转肽酶失活。