Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia.
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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Xanthomonas
/
Beta-Lactamases
Language:
En
Journal:
Biochim Biophys Acta
Year:
1994
Type:
Article
Affiliation country:
United kingdom