ATP类似物作为大肠杆菌MRE 600亮氨酰-tRNA合成酶的底物
ATP-analogues as substrates for the leucyl-tRNA synthetase from Escherichia coli MRE 600.
作者信息
Marutzky R, Flossdorf J, Kula M R
出版信息
Nucleic Acids Res. 1976 Aug;3(8):2067-77. doi: 10.1093/nar/3.8.2067.
Abstract
No analogous nucleoside triphosphate was found which acts as well as ATP in binding to and supporting catalysis of leucyl-tRNA synthetase from Escherichia coli MRE 600. However, there are numerous nucleotides which are able to replace ATP, but with lower efficiency. The 6-amino group of the adenine ring and the 2'-hydroxyl group of the ribose ring are essential for binding and catalytic activity. Alterations in the triphosphate moiety of the molecule can cause drastic changes in Km and/or Vmax, whereas alterations of the imidazole ring and substitutions at the 8-position of the adenine ring cause only minor losses of catalytic activity.
摘要
未发现有类似的三磷酸核苷在结合和支持来自大肠杆菌MRE 600的亮氨酰-tRNA合成酶催化方面能像ATP那样发挥作用。然而，有许多核苷酸能够替代ATP，但效率较低。腺嘌呤环的6-氨基和核糖环的2'-羟基对于结合和催化活性至关重要。分子三磷酸部分的改变可导致Km和/或Vmax发生剧烈变化，而咪唑环的改变以及腺嘌呤环8位的取代仅导致催化活性的轻微损失。
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