他唑巴坦(青霉酸磺胺衍生物)与活性位点丝氨酸β -内酰胺酶相互作用的动力学研究。

Journal of enzyme inhibition Pub Date : 2000-01-01
M Perilli, N Franceschini, G Bonfiglio, B Segatore, S Stefani, G Nicoletti, M M Perez, C Bianchi, A Zollo, G Amicosante
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引用次数: 0

摘要

用分光光度法研究了他唑巴坦与几种染色体和质粒编码(TEM、SHV、PSE型)A类和C类β -内酰胺酶的相互作用。他唑巴坦表现为竞争性抑制剂或失活剂,在一些情况下能够恢复哌拉西林作为伙伴β -内酰胺的效率。详细的动力学分析允许测量一些头孢菌素酶和广谱β -内酰胺酶的酰化效率;还评估了酰基-酶络合物翻转的存在。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
A kinetic study on the interaction between tazobactam (a penicillanic acid sulphone derivative) and active-site serine beta-lactamases.

The interaction between tazobactam and several chromosome- and plasmid-encoded (TEM, SHV, PSE types) class A and C beta-lactamases was studied by spectrophotometry. Tazobactam behaved as a competitive inhibitor or inactivator able to restore in several cases the efficiency of piperacillin as a partner beta-lactam. A detailed kinetic analysis permitted measurement of the acylation efficiency for some cephalosporinases and broad-spectrum beta-lactamases; the presence of a turn-over of acyl-enzyme complex was also evaluated.

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