Hayashi T, Murray B W, Wang R, Wong C H
Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037, USA.
Bioorg Med Chem. 1997 Mar;5(3):497-500. doi: 10.1016/s0968-0896(96)00263-5.
Uridine 5'-diphospho-(2-deoxy-2-fluoro)galactose (UDP-2FGal), prepared and characterized for the first time by a chemoenzymatic method, was found to be a competitive inhibitor of beta-1,4-galactosyltransferase with a Ki value of 149 microM. This study supports that the glycosyltransferase reaction mechanism proceeds through a glycosidic cleavage transition state with sp2 character developed at the anomeric center.
首次通过化学酶法制备并表征的尿苷5'-二磷酸-(2-脱氧-2-氟)半乳糖（UDP-2FGal）被发现是β-1,4-半乳糖基转移酶的竞争性抑制剂，其Ki值为149微摩尔。该研究支持糖基转移酶反应机制通过在异头中心形成具有sp2特征的糖苷键裂解过渡态进行。
