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

Biochim Biophys Acta. 1994 Jun 21;1218(2):199-201. doi: 10.1016/0167-4781(94)90011-6.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Molecular Sequence Data
  • Sequence Alignment
  • Xanthomonas / genetics*
  • beta-Lactamases / genetics*

Substances

  • beta-lactamase L1
  • beta-Lactamases

Associated data

  • GENBANK/X75074