Pingoud A, Block W, Urbanke C, Wolf H
Eur J Biochem. 1982 Apr 1;123(2):261-5. doi: 10.1111/j.1432-1033.1982.tb19762.x.
Pulvomycin and kirromycin, two antibiotics which inhibit protein biosynthesis in Escherichia coli by complex formation with the elongation factor Tu (EF-Tu), bind to different sites on the protein. While only one molecule of kirromycin can be bound to one molecule of EF-Tu, more than one molecule of pulvomycin interacts with a molecule of EF-Tu. This has been deduced from experiments in which the aminoacyl-tRNA binding and the GTPase activity of EF-Tu were measured in the presence of varying amounts of both antibiotics. These experiments are interpreted to mean that pulvomycin but not kirromycin can replace the other antibiotic in its respective site. Our conclusions are supported by circular dichroism spectroscopy.
普尔沃霉素和奇霉素是两种通过与延伸因子Tu（EF-Tu）形成复合物来抑制大肠杆菌中蛋白质生物合成的抗生素，它们与该蛋白质上的不同位点结合。虽然奇霉素的一个分子只能与EF-Tu的一个分子结合，但普尔沃霉素的一个以上分子会与EF-Tu的一个分子相互作用。这是从在不同量的两种抗生素存在下测量EF-Tu的氨酰tRNA结合和GTP酶活性的实验中推断出来的。这些实验被解释为意味着普尔沃霉素而非奇霉素可以在其各自的位点取代另一种抗生素。我们的结论得到了圆二色光谱的支持。
