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.

引用

页码：137 / 140

页数：4

共 12 条

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