Tözsér J, Bláha I, Copeland T D, Wondrak E M, Oroszlan S
Laboratory of Molecular Virology and Carcinogenesis, ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, MD 21702.
FEBS Lett. 1991 Apr 9;281(1-2):77-80. doi: 10.1016/0014-5793(91)80362-7.
The substrate specificity of the human immunodeficiency virus type 1 (HIV-1) and type 2 (HIV-2) proteinases was compared using oligopeptides corresponding to cleavage sites in the Gag and Gag-Pol polyproteins of both viruses. All peptides mimicking cleavage sites at the junction of major functional protein domains were correctly cleaved by both enzymes. However, some other peptides thought to represent secondary cleavage sites remained intact. The kinetic parameters (Km and kcat) obtained for the different substrates showed several hundred-fold variation but were similar for the same substrate.
使用与两种病毒的Gag和Gag-Pol多聚蛋白中切割位点相对应的寡肽，比较了1型人类免疫缺陷病毒（HIV-1）和2型人类免疫缺陷病毒（HIV-2）蛋白酶的底物特异性。所有模拟主要功能蛋白结构域交界处切割位点的肽都能被这两种酶正确切割。然而，一些被认为代表二级切割位点的其他肽仍然完整。针对不同底物获得的动力学参数（Km和kcat）显示出数百倍的差异，但相同底物的参数相似。
