β-内酰胺化合物的负电荷在与活性位点丝氨酸DD-肽酶和β-内酰胺酶相互作用中的重要性。
The importance of the negative charge of beta-lactam compounds in the interactions with active-site serine DD-peptidases and beta-lactamases.
作者信息
Varetto L, De Meester F, Monnaie D, Marchand-Brynaert J, Dive G, Jacob F, Frère J M
机构信息
Centre for Protein Engineering, Université de Liège, Belgium.
出版信息
Biochem J. 1991 Sep 15;278 ( Pt 3)(Pt 3):801-7. doi: 10.1042/bj2780801.
Abstract
The interaction between various penicillins and cephalosporins the carboxylate group of which at C-3 or C-4 had been esterified or amidated and different penicillin-recognizing enzymes was studied. In general, our findings reinforced the common assumption that an anionic group at that position is necessary for the effective acylation of these enzymes. However, the relative activities of the modified beta-lactams as inactivators of the Streptomyces R61 DD-peptidase or as substrates of the Bacillus licheniformis, Streptomyces albus G and Enterobacter cloacae beta-lactamases did not fit a general scheme in which the intrinsic electronic and geometric properties of the beta-lactam compounds would be sufficient to explain their substrate or inactivator properties towards the various types of enzymes investigated.
摘要
研究了各种青霉素和头孢菌素（其C-3或C-4位的羧基已被酯化或酰胺化）与不同青霉素识别酶之间的相互作用。总体而言，我们的研究结果强化了一个普遍的假设，即该位置的阴离子基团对于这些酶的有效酰化是必要的。然而，修饰后的β-内酰胺作为链霉菌R61 DD-肽酶的失活剂或作为地衣芽孢杆菌、白色链霉菌G和阴沟肠杆菌β-内酰胺酶的底物的相对活性并不符合一个通用的模式，即β-内酰胺化合物的内在电子和几何性质足以解释它们对所研究的各种类型酶的底物或失活剂性质。
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本文引用的文献
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Delta 2- and delta 3-cephalosporins, penicillinate and 6-unsubstituted penems. Intrinsic reactivity and interaction with beta-lactamases and D-alanyl-D-alanine-cleaving serine peptidases.δ2-和δ3-头孢菌素、青霉素酸盐及6-未取代青霉烯。内在反应活性以及与β-内酰胺酶和D-丙氨酰-D-丙氨酸裂解丝氨酸肽酶的相互作用。
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