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Article

Kinetic properties and metal content of the metallo-beta-lactamase CcrA harboring selective amino acid substitutions.

The Journal of biological chemistry - 28 May 1999

Yang Y, Keeney D, Tang X, Canfield N, Rasmussen B A

Abstract excerpt

The crystal structure of the metallo-beta-lactamase CcrA3 indicates that the active site of this enzyme contains a binuclear zinc center. To aid in assessing the involvement of specific residues in beta-lactam hydrolysis and susceptibility to inhibitors, individual substitutions of selected amino acids were generated. Substitution of the zinc-ligating residue Cys181 with Ser (C181S) resulted in a significant...

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PMID: 10336469
DOI: 10.1074/jbc.274.22.15706

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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