School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, 152-160 Pearse Street, Dublin 2, Ireland.
Chem Commun (Camb). 2020 Apr 7;56(27):3915-3918. doi: 10.1039/c9cc09887a. Epub 2020 Mar 9.
Eukaryotic tRNA-guanine transglycosylase (TGT) - an enzyme recently recognised to be of potential therapeutic importance - catalyses base-exchange of guanine for queuine at the wobble position of tRNAs associated with 4 amino acids via a distinct mechanism to that reported for its eubacterial homologue. The presence of queuine is unequivocally required as a trigger for reaction between the enzyme and tRNA and exhibits cooperativity not seen using guanine as a substrate.
真核 tRNA-鸟嘌呤转糖基酶（TGT）-一种最近被认为具有潜在治疗重要性的酶-通过与报道的其细菌同源物不同的机制，催化 tRNA 上与 4 个氨基酸相关的摆动位置的鸟嘌呤与 queuine 发生碱基交换。queuine 的存在是酶与 tRNA 之间反应的必要触发因素，并且表现出协同作用，而使用鸟嘌呤作为底物则没有观察到这种作用。
