Sakurai Y, Tsukamoto K, Sawai T
Division of Microbial Chemistry, Faculty of Pharmaceutical Sciences, Chiba University, Japan.
J Bacteriol. 1991 Nov;173(21):7038-41. doi: 10.1128/jb.173.21.7038-7041.1991.
The structural gene of a carbenicillinase was cloned from the chromosomal DNA of Proteus mirabilis GN79. This gene codes for a protein of 270 amino acids. Alignment of the amino acid sequence with those of known beta-lactamases revealed that the enzyme is a novel class A beta-lactamase with a unique conserved triad, RTG. By using a DNA fragment of the structural gene, a lack of cross hybridization was confirmed between the DNA probe and total DNAs from natural isolates of P. mirabilis, suggesting that the carbenicillinase may not be a species-specific beta-lactamase of P. mirabilis.
从奇异变形杆菌GN79的染色体DNA中克隆出羧苄青霉素酶的结构基因。该基因编码一种由270个氨基酸组成的蛋白质。将该氨基酸序列与已知β-内酰胺酶的序列进行比对，结果显示该酶是一种新型的A类β-内酰胺酶，具有独特的保守三联体RTG。通过使用结构基因的DNA片段，证实了DNA探针与奇异变形杆菌天然分离株的总DNA之间不存在交叉杂交，这表明羧苄青霉素酶可能不是奇异变形杆菌的种特异性β-内酰胺酶。
