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Biochim Biophys Acta. 1994 Jun 21;1218(2):199-201.

Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia.

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  • 1Department of Microbiology and Pathology, University of Bristol, UK.

Abstract

The amino acid sequence deduced from the L1 beta-lactamase gene of Xanthomonas maltophilia shows a significant variation from that of the CphA and Blm metallo-beta-lactamases of Aeromonas hydrophila and Bacillus cereus, respectively. Whilst the N-terminus of the L1 protein shows some similarity, particularly at the histidine residues previously suggested as a zinc-binding motif, the C-terminus of the protein demonstrates very little similarity. Such differences amongst this group of enzymes would argue for at least three subclasses within the Group 3 beta-lactamases. However, in order to predict their phylogenetic ancestry more sequence data are required from other possible metallo-beta-lactamases.

PMID:
8018721
[PubMed - indexed for MEDLINE]
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