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PMID: 9593158 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Molecular heterogeneity of the L-1 metallo-beta-lactamase family from Stenotrophomonas maltophilia.

Antimicrobial agents and chemotherapy ·Vol. 42 ·No. 5 ·1998-05-00 ·Pages 1245-8

Sanschagrin F, Dufresne J, Levesque RC

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.

MeSH Terms
Amino Acid Sequence Base Sequence Genes, Bacterial/genetics Genetic Variation Molecular Sequence Data Sequence Alignment Sequence Homology, Amino Acid Xanthomonas/enzymology,genetics beta-Lactam Resistance/genetics beta-Lactamases/genetics
Chemicals
beta-lactamase L1 beta-Lactamases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Sanschagrin F
Microbiologie Moléculaire et Génie des Protéines, Sciences de la Vie et de la Santé, Faculté de Médecine, Université Laval, Ste-Foy, Québec, Canada.
Dufresne J
Levesque R C
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Article Info
Journal
Antimicrobial agents and chemotherapy
Abbr.
Antimicrob Agents Chemother
ISSN
0066-4804
DOI
10.1128/AAC.42.5.1245
Published
1998-05-00
Pages
1245-8
Language
English
Region
United States
NLM ID
0315061
PMCID
PMC105789
Subset
IM
Databases
GENBANK
AF010282
External Links
PubMed source DOI: 10.1128/AAC.42.5.1245 PMC Full Text View journal details
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