Lim H M, Pène J J, Shaw R W
School of Life and Health Sciences, University of Delaware, Newark 19716.
J Bacteriol. 1988 Jun;170(6):2873-8. doi: 10.1128/jb.170.6.2873-2878.1988.
Two forms of heat-stable, zinc-containing beta-lactamase II have been described for strains of Bacillus cereus and have been shown to differ in substrate specificity (R. B. Davies, E. P. Abraham, J. Fleming, and M. R. Pollock, Biochem. J. 145: 409-411, 1975). We report here the nucleotide sequence, inferred amino acid sequence, and expression of beta-lactamase II from B. cereus 5/B/6 and compare our results with those for its homolog characterized in B. cereus 569/H (M. Hussain, C. Anthony, M. J. Madonna, and J. O. Lampen, J. Bacteriol. 164: 223-229, 1985) to document amino acid differences contributing to the specific properties of these enzymes.
已针对蜡状芽孢杆菌菌株描述了两种形式的热稳定含锌β-内酰胺酶II,且已证明它们在底物特异性方面存在差异(R. B. 戴维斯、E. P. 亚伯拉罕、J. 弗莱明和M. R. 波洛克,《生物化学杂志》145: 409 - 411, 1975)。我们在此报告蜡状芽孢杆菌5/B/6中β-内酰胺酶II的核苷酸序列、推导的氨基酸序列及表达情况,并将我们的结果与蜡状芽孢杆菌569/H中其同源物的相关结果进行比较(M. 侯赛因、C. 安东尼、M. J. 麦当娜和J. O. 兰彭,《细菌学杂志》164: 223 - 229, 1985),以记录导致这些酶具有特定特性的氨基酸差异。