Kellam P, Dallas W S, Ballantine S P, Delves C J
Structural Biology Group, GlaxoWellcome Research Laboratories, Beckenham, Kent, UK.
FEMS Microbiol Lett. 1995 Dec 15;134(2-3):165-9. doi: 10.1111/j.1574-6968.1995.tb07932.x.
A 1,7-kilobase fragment of the Staphylococcus haemolyticus chromosome containing the dihydropteroate synthase gene has been cloned by complementation in a temperature-sensitive mutant of Escherichia coli. The gene, designated folP, predicts a gene product of 29613 Da which shares significant amino acid sequence identity with other known bacterial dihydropteroate synthases. Analysis of the DNA sequence upstream and downstream of folP identified two further, incomplete open reading frames, one of which shows predicted amino acid sequence similarity to a second bacterial folic acid synthesis enzyme, dihydroneopterin aldolase.
通过在大肠杆菌的温度敏感突变体中进行互补,克隆出了包含溶血性葡萄球菌染色体二氢蝶酸合酶基因的一个1.7千碱基片段。该基因命名为folP,预测其基因产物为29613道尔顿,与其他已知细菌二氢蝶酸合酶具有显著的氨基酸序列同一性。对folP上下游DNA序列的分析确定了另外两个不完整的开放阅读框,其中一个显示出预测的氨基酸序列与第二种细菌叶酸合成酶二氢新蝶呤醛缩酶相似。