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• W2022126145 abstract "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 Zn2 enzyme with a remarkable 15-fold increased activity with cefoxitin as substrate." @default.
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• W2022126145 date "1998-10-30" @default.
• W2022126145 modified "2023-09-25" @default.
• W2022126145 title "Mono- and binuclear Zn-β-lactamase from <i>Bacteroides fragilis</i> : catalytic and structural roles of the zinc ions" @default.
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• W2022126145 doi "https://doi.org/10.1016/s0014-5793(98)01289-7" @default.
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