Abstract
A novel class A beta-lactamase (SCO-1) encoded by an 80-kb self-transferable plasmid from Escherichia coli is described. The interaction of SCO-1 with beta-lactams was similar to that of the CARB-type enzymes. Also, SCO-1 exhibited a 51% amino acid sequence identity with the RTG subgroup of chromosomal carbenicillinases (RTG-1, CARB-5, and CARB-8).
MeSH terms
-
Amino Acid Sequence
-
Anti-Bacterial Agents / metabolism
-
Anti-Bacterial Agents / pharmacology*
-
Escherichia coli / drug effects*
-
Escherichia coli / enzymology*
-
Escherichia coli / genetics
-
Humans
-
Microbial Sensitivity Tests
-
Molecular Sequence Data
-
Penicillinase / chemistry
-
Penicillinase / genetics
-
Penicillinase / metabolism*
-
Plasmids*
-
Sequence Analysis, DNA
-
beta-Lactam Resistance
-
beta-Lactamases / chemistry
-
beta-Lactamases / genetics
-
beta-Lactamases / metabolism*
-
beta-Lactams / metabolism
-
beta-Lactams / pharmacology*
Substances
-
Anti-Bacterial Agents
-
beta-Lactams
-
Penicillinase
-
beta-Lactamases