Your browser doesn't support javascript.
loading
Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia.
Walsh, T R; Hall, L; Assinder, S J; Nichols, W W; Cartwright, S J; MacGowan, A P; Bennett, P M.
Affiliation
  • Walsh TR; Department of Microbiology and Pathology, University of Bristol, UK.
Biochim Biophys Acta ; 1218(2): 199-201, 1994 Jun 21.
Article in En | MEDLINE | ID: mdl-8018721
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.
Subject(s)
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Xanthomonas / Beta-Lactamases Language: En Journal: Biochim Biophys Acta Year: 1994 Type: Article Affiliation country: United kingdom
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Xanthomonas / Beta-Lactamases Language: En Journal: Biochim Biophys Acta Year: 1994 Type: Article Affiliation country: United kingdom