Felici A, Amicosante G, Oratore A, Strom R, Ledent P, Joris B, Fanuel L, Frère J M
Università degli Studi dell'Aquila, Dipartimento di Scienze e Tecnologie Biomediche e di Biometria, Italy.
Biochem J. 1993 Apr 1;291 ( Pt 1)(Pt 1):151-5. doi: 10.1042/bj2910151.
The catalytic properties of three class B beta-lactamases (from Pseudomonas maltophilia, Aeromonas hydrophila and Bacillus cereus) were studied and compared with those of the Bacteroides fragilis enzyme. The A. hydrophila beta-lactamase exhibited a unique specificity profile and could be considered as a rather specific 'carbapenemase'. No relationships were found between sequence similarities and catalytic properties. The problem of the repartition of class B beta-lactamases into sub-classes is discussed. Improved purification methods were devised for the P. maltophilia and A. hydrophila beta-lactamases including, for the latter enzyme, a very efficient affinity chromatography step on a Zn(2+)-chelate column.
研究了三种B类β-内酰胺酶（来自嗜麦芽窄食单胞菌、嗜水气单胞菌和蜡样芽孢杆菌）的催化特性，并与脆弱拟杆菌的酶进行了比较。嗜水气单胞菌β-内酰胺酶表现出独特的特异性谱，可被视为一种相当特异的“碳青霉烯酶”。未发现序列相似性与催化特性之间的关系。讨论了将B类β-内酰胺酶分为亚类的问题。设计了改进的嗜麦芽窄食单胞菌和嗜水气单胞菌β-内酰胺酶纯化方法，对于后者的酶，包括在Zn(2+)-螯合柱上进行非常有效的亲和层析步骤。
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