Cleavage efficiency by adenovirus protease is site-dependent
Cleavage efficiency by adenovirus protease is site-dependent
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DOI：
10.1074/jbc.271.51.32511
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发表时间：
1996-12-20
影响因子：
4.8
通讯作者：
Weber, JM
中科院分区：
文献类型：
--
作者：
Diouri, M;KeyvaniAmineh, H;Weber, JM
腺病毒蛋白酶切割共有序列（M/I/L）XGX-G和（M/I/L）XGG-X。利用纯化的重组蛋白酶，我们发现带有GX-G位点的肽比带有GG-X位点的肽水解得更快，GX-G位点也优先被带有两个切割位点的病毒蛋白pVI切割。提出的证据表明，这一差异裂解效率的生物学作用。
The adenovirus protease cleaves consensus sequences (M/I/L)XGX-G and (M/I/L)XGG-X. Using purified recombinant protease, we showed that a peptide bearing the GX-G site was hydrolyzed more rapidly than a peptide bearing the GG-X site, The GX-G site was also preferentially cleaved on viral protein pVI which bears both sites of cleavage. Evidence is presented that suggests a biological role for this differential cleavage efficiency.