Structural and Functional Characterization of Plasmodium falciparum Nicotinic Acid Mononucleotide Adenylyltransferase

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• 作者：Jochen Bathke¹ ; Karin Fritz-Wolf¹ ; ² ; Christina Brandstä ; dter¹ ; Anja Burkhardt³ ; Esther Jortzik¹ ; Stefan Rahlfs¹ ; Katja Becker¹ ; ^{katja.becker@uni-giessen.de}
• 关键词：AMP ; adenine mononucleotide ; APC ; adenosine-5&prime ; -[(α ; β)-methyleno]diphosphate ; BaNaMNAT ; B. anthracis NaMNAT ; EcNaMNAT ; E. coli NaMNAT ; NaAD ; nicotinic acid adenine dinucleotide ; NAD ; nicotinamide adenine dinucleotide ; NaMN ; nicotinic acid mononucleotide ; NaMNAT ; nicotinic acid mononucleotide adenylyltransferase ; Ni-NTA ; nickel nitrilotriacetic acid ; NMN ; nicotinamide mononucleotide ; NMNAT ; nicotinamide mononucleotide adenylyltransferase ; PDB ; Protein Data Bank ; PEG ; polyethylene glycol ; PfN
• 刊名：Journal of Molecular Biology
• 出版年：2016
• 出版时间：4 December 2016
• 年：2016
• 卷：428
• 期：24
• 页码：4946-4961
• 全文大小：2234 K
• 卷排序：428

文摘

P. falciparum nicotinic acid mononucleotide adenylyltransferase was characterized. Two X-ray structures—in complex with NaAD and with an ATP analog—were obtained. Two active site cysteines are likely to be involved in redox regulation of PfNaMNAT. PfNaMNAT utilizes NaMN and nicotinamide mononucleotide, emphasizing its potential as a drug target.