Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia.
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Walsh TR, Hall L, Assinder SJ, Nichols WW, Cartwright SJ, MacGowan AP, Bennett PM
Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia.
Biochim Biophys Acta. 1994 Jun 21;1218(2):199-201.
- PubMed ID
- 8018721 [ View in PubMed]
- 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.