title: Molecular heterogeneity of the L-1 metallo-beta-lactamase family from Stenotrophomonas maltophilia.
abstract: We have determined the nucleotide sequence of the blaS gene encoding the carbapenem-hydrolyzing L-1 beta-lactamase from Stenotrophomonas maltophilia GN12873. Analysis of the DNA and deduced amino acid sequences identified a product of 290 amino acids. Comparisons of the L-1 amino acid sequence with those of other zinc beta-lactamases showed 88.6% identity with the L-1 enzyme from S. maltophilia IID1275 and less than 20% identity with other class B metalloenzymes.
authors.affiliation: Microbiologie Moléculaire et Génie des Protéines, Sciences de la Vie et de la Santé, Faculté de Médecine, Université Laval, Ste-Foy, Québec, Canada.
authors.forename: F
authors.initials: F
authors.lastname: Sanschagrin
authors.forename: J
authors.initials: J
authors.lastname: Dufresne
authors.forename: R C
authors.initials: RC
authors.lastname: Levesque
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D005798:Genes, Bacterial / Q000235:genetics*; D014644:Genetic Variation; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014974:Xanthomonas / Q000201:enzymology / Q000235:genetics*; D018440:beta-Lactam Resistance / Q000235:genetics*; D001618:beta-Lactamases / Q000235:genetics*
chemical_list: C088032:beta-lactamase L1; D001618:beta-Lactamases