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. 1992 May;36(5):1155–1157. doi: 10.1128/aac.36.5.1155

Biochemical characterization of the metallo-beta-lactamase CcrA from Bacteroides fragilis TAL3636.

Y Yang 1, B A Rasmussen 1, K Bush 1
PMCID: PMC188856  PMID: 1510410

Abstract

The CcrA beta-lactamase from Bacteroides fragilis TAL3636 was cloned into Escherichia coli and purified from inclusion bodies. This group 3 metalloenzyme hydrolyzed most beta-lactam antibiotics, including cephamycins and carbapenems. Following inhibition by chelators, enzyme activity was recovered with the cations Zn2+ and Co2+. Clavulanate and sulbactam were activators; tazobactam at 10 microM inactivated the enzyme.

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Selected References

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