Steady-state kinetic studies reveal that the anti-cancer target Ubiquitin-Specific Protease 17 (USP17) is a highly efficient deubiquitinating enzyme
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- 作者：Nicole M. Hjortlanda ; Andrew D. Mesecara ; b ; c ; d ; amesecar@purdue.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：Ubiquitin Specific Protease 17 ; DUB3 ; Ubiquitin ; Protein refolding ; USP17 ; Deubiquitinating
- 刊名：Archives of Biochemistry and Biophysics
- 出版年：2016
- 出版时间：15 December 2016
- 年：2016
- 卷：612
- 期：Complete
- 页码：35-45
- 全文大小：1499 K
文摘
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USP17 is highly upregulated in cancer and is a viable anti-cancer drug target.
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USP17 was purified from E. coli inclusion bodies and is highly active.
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USP17 appears to function as a monomer in solution.
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USP17 can recognize and cleave Lys11, Lys33, Lys48 and Lys63 ubiquitin linkages.
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Purified USP17 can be used for high-throughput screening to identify inhibitors.