Matthew M, Hedges R W, Smith J T
J Bacteriol. 1979 Jun;138(3):657-62. doi: 10.1128/jb.138.3.657-662.1979.
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.
本文描述了在肠道细菌中由质粒决定的两种β-内酰胺酶,它们与TEM酶有一些相似之处。这两种酶均不同于所有其他质粒介导的β-内酰胺酶,在水解某些底物的能力、等电点、免疫特异性以及对抑制作用的敏感性方面与TEMβ-内酰胺酶有所不同。其中一种由质粒p453介导的酶,此前曾有过简要描述。我们发现,这种被命名为SHV-1的β-内酰胺酶,对巯基试剂对氯汞苯甲酸的抑制反应独特,因为它影响头孢菌素的水解而不影响苄青霉素的水解。这种酶存在于多种质粒类型中,这些质粒是从广泛地理区域收集的几种细菌物种中转移而来的。另一种酶是新发现的;仅检测到一种决定这种β-内酰胺酶(命名为HMS-1)的质粒。