McKinnon R D, Wosnick M A, White B N
Nucleic Acids Res. 1978 Dec;5(12):4865-76. doi: 10.1093/nar/5.12.4865.
Drosophila tRNA can be guanylated by a crude enzyme from rabbit reticulocytes. Guanylating activity is also present in crude extracts of adult Drosophila. A major product of this reaction as well as several minor ones were resolved by RPC-5 chromatography. The main substrate of both the Drosophila and rabbit reticulocyte enzymes was the non-Q-containing aspartic acid tRNA, tRNA2gammaAsp. The QU-lacking (gamma) forms of asparagine, histidine and tyrosine tRNAs were also substrates and gave rise to the minor products of the reaction. In contrast, the Q- or Q*-containing (delta) forms of these tRNAs appear not to be substrates. The evidence strongly suggests that the guanyating enzyme is involved in Q biosynthesis and would be better termed a guanine replacement or pre-Q insertion enzyme.
果蝇的tRNA可被来自兔网织红细胞的粗酶进行鸟苷酸化。鸟苷酸化活性也存在于成年果蝇的粗提物中。该反应的一种主要产物以及几种次要产物通过RPC - 5色谱法得以分离。果蝇和兔网织红细胞酶的主要底物都是不含Q的天冬氨酸tRNA,即tRNA2γAsp。缺乏QU的(γ)形式的天冬酰胺、组氨酸和酪氨酸tRNA也是底物,并产生该反应的次要产物。相比之下,这些tRNA的含Q或Q*的(δ)形式似乎不是底物。有力的证据表明,鸟苷酸化酶参与Q的生物合成,更宜称为鸟嘌呤置换酶或前Q插入酶。