Studies on substrate specificity at PR/p3 cleavage site of HTLV-1 protease
Studies on substrate specificity at PR/p3 cleavage site of HTLV-1 protease
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DOI：
10.1007/s10989-006-9062-z
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发表时间：
2007-06-01
影响因子：
2.5
通讯作者：
Akaji, Kenichi
中科院分区：
文献类型：
--
作者：
Bang, Jeong Kyu;Teruya, Kenta;Akaji, Kenichi
使用底物肽的小文库阐明了在HTLV-1蛋白酶的PR/p3位点识别的底物特异性。通过平行合成/消化覆盖PR/p3位点的合成肽（KGPPVILPIQA）来检查P-1和P-1 '位置处的特异性。通过含有底物序列（PPVILPIQ）的烯烃-肽文库的拆分和混合合成，检查P-2至P-4位置的特异性。固相Horner-Emmons反应成功地应用于多组分文库制备底物的合成。通过化学合成的HTLV-1蛋白酶突变体（C2 A HTLV-1 PR）对底物肽的消化，首次发现该酶在P-1 ′位置对Pro的偏好和在P-2位置对Ile的偏好是独特的。
Substrate specificities for recognition at the PR/p3 site of HTLV-1 protease were clarified using small libraries of substrate peptides. Specificities at P-1 and P-1 ' positions were examined by parallel synthesis/digestion of synthetic peptides covering the PR/p3 site (KGPPVILPIQA). Specificities at P-2 to P-4 positions were examined by split and mix syntheses of olefin-peptide libraries containing the substrate sequence (PPVILPIQ). The solid-phase Horner-Emmons reaction was successfully applied to syntheses of multi-component substrates for library preparation. From the digestion of substrate peptides by a chemically synthesized mutant of HTLV-1 protease (C2A HTLV-1 PR), it was found for the first time that the preference for Pro at the P-1 ' position and for Ile at the P-2 position is unique for this enzyme.