Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia.
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.
Walsh
T R
TR
Department of Microbiology and Pathology, University of Bristol, UK.
Hall
L
L
Assinder
S J
SJ
Nichols
W W
WW
Cartwright
S J
SJ
MacGowan
A P
AP
Bennett
P M
PM
D000595:Amino Acid Sequence; D001483:Base Sequence; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D014974:Xanthomonas / Q000235:genetics*; D001618:beta-Lactamases / Q000235:genetics*
C088032:beta-lactamase L1; D001618:beta-Lactamases