Abstract
Two species of beta-lactamase determined by plasmids in enteric bacteria that show some resemblance to TEM enzymes are described. Both are distinct from all other plasmid-mediated beta-lactamases and differ from the TEM beta-lactamases in ability to hydrolyze some substrates, in isoelectric point, in immunological specificity, and in susceptibility to inhibition. One of the enzyme species, mediated by plasmid p453, has been briefly described previously. We have discovered that this beta-lactamase, designated SHV-1, is unique in its response to inhibition by the sulfhydryl group reagent p-chloromercuribenzoate, because the hydrolysis of cephaloridine but not that of benzylpenicillin is affected. This enzyme is found in a variety of plasmid types which were transferred from several bacterial species collected from a wide geographic range. The other enzyme species is novel; only a single plasmid determining this kind of beta-lactamase (designated HMS-1) has been detected.