Callens M, Van Roy J, Zeelen J P, Borchert T V, Nalis D, Wierenga R K, Opperdoes F R
Research Unit for Tropical Diseases, International Institute of Cellular and Molecular Pathology, Brussels, Belgium.
Biochem Biophys Res Commun. 1993 Sep 15;195(2):667-72. doi: 10.1006/bbrc.1993.2097.
Hydrophobic cyclic hexapeptides have been reported to selectively inhibit glycosomal triosephosphate isomerase from Trypanosoma brucei (Kuntz et al, 1992, Eur. J. Biochem., 207, 441-447). Here it is shown that this inhibition is not due to a specific interaction between the enzyme and soluble hydrophobic cyclic hexapeptides, but that it is the result of a coprecipitation of trypanosome triosephosphate isomerase with cyclic hexapeptides when the solubilities of the latter are exceeded. A study of the interaction of these hexapeptides with other glycosomal enzymes revealed that several of them, such as phosphoglycerate kinase and hexokinase, also coprecipitated with these peptides, whereas most of the homologous enzymes from other organisms did not coprecipitate, nor were they inactivated.
据报道，疏水环六肽可选择性抑制布氏锥虫的糖体磷酸丙糖异构酶（Kuntz等人，1992年，《欧洲生物化学杂志》，207卷，441 - 447页）。本文表明，这种抑制并非由于酶与可溶性疏水环六肽之间的特异性相互作用，而是当后者的溶解度超过限度时，锥虫磷酸丙糖异构酶与环六肽共沉淀的结果。对这些环六肽与其他糖体酶相互作用的研究表明，其中几种酶，如磷酸甘油酸激酶和己糖激酶，也与这些肽共沉淀，而来自其他生物体的大多数同源酶既不共沉淀，也未失活。
