β-nicotinamide mononucleotide (NMN) production in Escherichia coli
نویسندگان
چکیده
منابع مشابه
The Escherichia coli NadR regulator is endowed with nicotinamide mononucleotide adenylyltransferase activity.
The first identification and characterization of a catalytic activity associated with NadR protein is reported. A computer-aided search for sequence similarity revealed the presence in NadR of a 29-residue region highly conserved among known nicotinamide mononucleotide adenylyltransferases. The Escherichia coli nadR gene was cloned into a T7-based vector and overexpressed. In addition to functi...
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An enzyme which catalyzes the formation of nicotinamide mononucleotide in the presence of nicotinamide, S-phosphoribosylpyrophosphate, adenosine triphosphate, and Mgff has been purified from rat liver. The reaction is highly specific for ATP and is not substituted for by a variety of nucleotides. Enzymic activity has been found in all of the tissues studied, and in the crude homogenate it is ap...
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The gene (ybeN) coding for nicotinate mononucleotide adenylyltransferase, an NAD(P) biosynthetic enzyme, has been identified and overexpressed in Escherichia coli. This enzyme catalyzes the reversible adenylation of nicotinate mononucleotide and shows product inhibition. The rate of adenylation of nicotinate mononucleotide is at least 20 times faster than the rate of adenylation of nicotinamide...
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Nicotinamide mononucleoside 5'-diphosphate in its reduced form is an excellent substrate for polynucleotide phosphorylase from Micrococcus luteus both in de novo polymerization reactions and in primer extension reactions. The oxidized form of the diphosphate is a much less efficient substrate; it can be used to extend primers but does not oligomerize in the absence of a primer. The cyanide addu...
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ژورنال
عنوان ژورنال: Scientific Reports
سال: 2018
ISSN: 2045-2322
DOI: 10.1038/s41598-018-30792-0