Analysis of <Emphasis Type="Italic">Escherichia coli</Emphasis> nicotinate mononucleotide adenylyltransferase mutants <Emphasis Type="Italic">in vivo</Emphasis> and <Emphasis Type="Italic">in vitro</Emphasis>期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

Analysis of Escherichia coli nicotinate mononucleotide adenylyltransferase mutants in vivo and in vitro

Authors:	Martin?Stancek,Robert?Schnell,Monica?Rydén-Aulin author-information" > author-information__contact u-icon-before" > mailto:monica@gmt.su.se" title=" monica@gmt.su.se" itemprop=" email" data-track=" click" data-track-action=" Email author" data-track-label=" " >Email author

Affiliation:	(1) Department of Genetics, Microbiology and Toxicology, Stockholm University, S-106 91 Stockholm, Sweden;(2) In vitro Sweden AB, Box 21160, S-100 31 Stockholm, Sweden;(3) Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden

Abstract:	Background Adenylation of nicotinate mononucleotide to nicotinate adenine dinucleotide is the penultimate step in NAD⁺ synthesis. In Escherichia coli, the enzyme nicotinate mononucleotide adenylyltransferase is encoded by the nadD gene. We have earlier made an initial characterization in vivo of two mutant enzymes, NadD72 and NadD74. Strains with either mutation have decreased intracellular levels of NAD⁺, especially for one of the alleles, nadD72.

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