Di Berardino M, Dijkstra A, Stüber D, Keck W, Gubler M
Pharma Research Department, F. Hoffman-La Roche Ltd., Basel, Switzerland.
FEBS Lett. 1996 Aug 26;392(2):184-8. doi: 10.1016/0014-5793(96)00809-5.
Using conserved fingerprints in the glycosyltransferase (GTase) domain of high-molecular-weight penicillin-binding proteins (PBP), a gene (mgt) encoding a putative monofunctional glycosyltransferase has been identified in Haemophilus influenzae and in other bacteria] species. Here we report the cloning of the homologous Escherichia coli gene and show that the solubilised membrane fraction of E. coli cells overexpressing the mgt gene contain a significantly increased peptidoglycan synthesis activity. In contrast to the high-molecular-weight PBPs, this activity is not inhibited by Flavomycin.
利用高分子量青霉素结合蛋白（PBP）糖基转移酶（GTase）结构域中的保守指纹图谱，在流感嗜血杆菌和其他细菌物种中鉴定出一个编码推定单功能糖基转移酶的基因（mgt）。在此，我们报告了同源大肠杆菌基因的克隆，并表明过表达mgt基因的大肠杆菌细胞的可溶性膜部分含有显著增加的肽聚糖合成活性。与高分子量PBP不同，这种活性不受黄霉素抑制。
