New insight into the binding modes of TNP-AMP to human liver fructose-1,6-bisphosphatase
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- 作者：Xinya Hana ; 1 ; Yunyuan Huanga ; 1 ; Rui Zhangb ; 1 ; San Xiaoa ; Shuaihuan Zhua ; Nian Qina ; Zongqin Honga ; Lin Weia ; Jiangtao Fenga ; Yanliang Rena ; Lingling Fenga ; fll708@mail.ccnu.edu.cn" class="auth_mail" title="E-mail the corresponding author ; Jian Wana ; jianwan@mail.ccnu.edu.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：FBPase ; fructose-1 ; 6-bisphosphatase ; TNP-AMP ; 2&prime ; 3&prime ; -O-(2 ; 4 ; 6-trinitrophenyl)adenosine 5&prime ; -monophosphate ; FBP ; fructose 1 ; 6-bisphosphate ; AMP ; adenosine monophosphate ; FDP ; fructose-2 ; 6-bisphosphate ; F6P ; fructose 6-phosphate
- 刊名：Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
- 出版年：2016
- 出版时间：5 August 2016
- 年：2016
- 卷：165
- 期：Complete
- 页码：155-160
- 全文大小：676 K
文摘
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The binding modes of TNP-AMP into the human liver FBPase has been re-examined.
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Not only AMP but also FBP can competitively inhibit the binding of TNP-AMP to FBPase.
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TNP-AMP can bind to both the active site and the allosteric site.
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K274 is important for TNP-AMP binding to the active site of FBPase.
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K274L is good candidate for exploring the allosteric site with TNP-AMP as fluorescent probe.