Bettinger G E, Lampen J O
J Bacteriol. 1970 Oct;104(1):283-8. doi: 10.1128/jb.104.1.283-288.1970.
Induction of penicillinase (beta-lactamase) in Bacillus licheniformis 749 by 2-(2'-carboxyphenyl)-benzoyl-6-aminopenicillanic acid (CBAP) was examined, since this compound was reported to be a gratuitous inducer of penicillinase in Staphylococcus aureus. The specific activity of enzyme optimally induced by CBAP is slightly more than that formed in response to cephalosporin C and threefold the level induced by benzylpenicillin. The optimal inducer concentration of CBAP was not inhibitory toward the growth of penicillinase-deficient mutants, unlike benzylpenicillin or cephalosporin C which showed marked toxicities. CBAP is hydrolyzed by the Bacillus penicillinase, but as indicated by its "physiological efficiency" (V(max)/K(m)), CBAP is a poor substrate at low concentrations. At very high concentrations, CBAP inhibited benzylpenicillin hydrolysis. The overall effectiveness of CBAP as an inducer can be attributed to its low "physiological efficiency" which enables the use of nontoxic levels of CBAP for induction without its rapid hydrolysis. Although CBAP is not a true gratuitous inducer, operationally it approaches gratuity for induction of B. licheniformis penicillinase better than other known inducers.
对2-(2'-羧基苯基)-苯甲酰基-6-氨基青霉烷酸（CBAP）诱导地衣芽孢杆菌749产生青霉素酶（β-内酰胺酶）进行了研究，因为据报道该化合物是金黄色葡萄球菌中青霉素酶的一种安慰诱导剂。由CBAP最佳诱导的酶的比活性略高于对头孢菌素C响应形成的酶，是苄青霉素诱导水平的三倍。与显示出明显毒性的苄青霉素或头孢菌素C不同，CBAP的最佳诱导剂浓度对青霉素酶缺陷型突变体的生长没有抑制作用。CBAP可被芽孢杆菌青霉素酶水解，但从其“生理效率”（V(max)/K(m)）来看，CBAP在低浓度下是一种较差的底物。在非常高的浓度下，CBAP抑制苄青霉素的水解。CBAP作为诱导剂的总体有效性可归因于其低“生理效率”，这使得能够使用无毒水平的CBAP进行诱导而无需其快速水解。虽然CBAP不是真正的安慰诱导剂，但在操作上它比其他已知诱导剂更接近地衣芽孢杆菌青霉素酶诱导的安慰性。
