Denesyuk A I, Vihinen M, Lundell J, Zav'yalov V P, Korpela T
Institute of Immunology, Moscow Region, Russia.
Biochem Biophys Res Commun. 1993 Apr 30;192(2):912-7. doi: 10.1006/bbrc.1993.1502.
Two enzymes, cyclophilin A and FK506-binding protein, with similar cis-trans isomerization catalytic activities but no similarity on the amino acid sequence level were compared in their three-dimensional structure by computer modelling. Cyclophilin A and FK506-binding protein proved to have similar arrangements at nine of the amino acids at their active site pockets. Two inhibitory peptides, cyclosporin A and FK506, also have structural similarities at their contact regions to the active sites. The studied systems may be another example of convergent evolution of enzyme catalytic site.
通过计算机建模比较了两种具有相似顺反异构化催化活性但氨基酸序列水平上无相似性的酶，亲环蛋白A和FK506结合蛋白的三维结构。结果表明，亲环蛋白A和FK506结合蛋白在其活性位点口袋的九个氨基酸处具有相似的排列方式。两种抑制性肽，环孢菌素A和FK506，在其与活性位点的接触区域也具有结构相似性。所研究的系统可能是酶催化位点趋同进化的另一个例子。
