Mono- and binuclear Zn-β-lactamase from Bacteroides fragilis:: catalytic and structural roles of the zinc ions

被引：64
|
作者：
Paul-Soto, R
Hernandez-Valladares, M
Galleni, M
Bauer, R
Zeppezauer, M
Frère, JM
Adolph, HW [1 ]
机构：
[1] Univ Saarland, Fachrichtung Biochem 124, D-66041 Saarbrucken, Germany
[2] Univ Liege, Inst Chim B6, Ctr Ingn Prot, B-4000 Liege, Belgium
[3] Royal Vet & Agr Univ, Dept Phys, DK-1871 Frederiksberg, Denmark
来源：
FEBS LETTERS | 1998年 / 438卷 / 1-2期
关键词：
Bacteroides fragilis; zinc beta-lactamase; zinc removal; metal exchange; thermal denaturation;
D O I：
10.1016/S0014-5793(98)01289-7
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The Bacteroides fragilis Zn-beta-lactamase is active with a mono- and a binuclear zinc site, The apoenzyme produced by removal of both Zn ions does not recover full activity upon readdition of Zn2+ in contrast to an active mono-Zn form prepared at pH 6.0. Differences in k(cat) values observed are substrate-dependent implying distinct mechanisms for the mono- and binuclear species. The substrate profile of a Zn,Cd hybrid obtained by selective exchange of one zinc ion is different from that of the Zn-2 enzyme with a remarkable 15-fold increased activity with cefoxitin as substrate. (C) 1998 Federation of European Biochemical Societies.
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收藏
页码：137 / 140
页数：4
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