The promiscuous ectonucleotidase NPP1: molecular insights into substrate binding and hydrolysis

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• 作者：Vigneshwaran Namasivayam¹ ; Sang-Yong Lee¹ ; Christa E. Mü ; ller ; ^{christa.mueller@uni-bonn.de}
• 关键词：AP4A ; diadenosine tetraphosphate ; CE ; capillary electrophoresis ; 2&prime ; 3&Prime ; -cGAMP ; cyclic guanosine-(2&prime ; 5&prime ; )-monophosphate-adenosine-(3&Prime ; 5&Prime ; )-monophosphate ; 3&prime ; 3&Prime ; -cGAMP ; cyclic guanosine-(3&prime ; 5&prime ; )-monophosphate-adenosine-(3&Prime ; 5&Prime ; )-monophosphate ; 3&prime ; 3&Prime ; -cdiGMP ; cyclic guanosine-(3&prime ; 5&prime ; )-monophosphate-guanosine-(3&Prime ; 5&Prime ; )-monophosphate ; 3&prime ; 3&Prime ; -cdiIMP ; cyclic inosine-(3&prime ; 5&prime ; )-monophosph
• 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：1861
• 期：3
• 页码：603-614
• 全文大小：2336 K
• 卷排序：1861

文摘

Substrate preferences of NPP1 were analyzed by combining biochemical experiments, homology modeling and docking studies. All nucleotides are hydrolyzed to nucleoside 5’-monophosphates. The mechanism of 2’,3’’-cGAMP hydrolyis by NPP1 was elucidated. The cyclic dinucleotide 2’,3’’-cGAMP yields 5’-AMP and 5’-GMP, while 3’,3’’-bridged cyclic dinucleotides are not hydrolyzed.