Crystal structure of human nicotinic acid phosphoribosyltransferase
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- 作者：Ada Serena Marlettaa ; Alberto Massarottia ; Giuseppe Orsomandob ; Giulio Magnib ; Menico Rizzia ; menico.rizzi@uniupo.it" class="auth_mail" title="E-mail the corresponding author ; Silvia Garavagliaa ; silvia.garavaglia@uniupo.it" class="auth_mail" title="E-mail the corresponding author
- 关键词：Na ; nicotinic acid ; NaAD ; nicotinic acid dinucleotide ; NAD ; nicotinamide adenine dinucleotide ; NaMN ; nicotinic acid mononucleotide ; NamR ; nicotinamide riboside ; NaPRTase ; nicotinic acid phosphoribosyltransferase ; NMN ; nicotinamide mononucleotide ; NMNAT ; nicotinamide mononucleotide adenylyltransferase ; PRPP ; 5-phosphoribosyl-1-pyrophosphate ; QA ; quinolinic acid
- 刊名：FEBS Open Bio
- 出版年：2015
- 出版时间：2015
- 年：2015
- 卷：5
- 期：Complete
- 页码：419-428
- 全文大小：3734 K
文摘
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Human NaPRTase is a functional dimer.
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The structural bases for FK866 lack of inhibition of human NaPRTas were identified.
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Na, Nam and QA phosphoribosyltransferases share a conserved fold.
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Na, Nam and QA phosphoribosyltransferases show distinctive traits in the active site.
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Human and Enterococcus faecalis NaPRTase are highly structurally conserved.