Literature summary for 2.7.7.18 extracted from

Lu, S.; Smith, C.D.; Yang, Z.; Pruett, P.S.; Nagy, L.; McCombs, D.; Delucas, L.J.; Brouillette, W.J.; Brouillette, C.G.
Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis (2008), Acta Crystallogr. Sect. F, 64, 893-898.

Application

Application	Comment	Organism
drug development	the enzyme is a target for inhibitor development	Bacillus anthracis

Cloned(Commentary)

Cloned (Comment)	Organism
gene nadD, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)	Bacillus anthracis

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting drop and hanging drop vapour diffusion method, mixing 0.001 ml of 4 mg/ml protein in 50 mM Tris, pH 7.0, 100 mM NaCl, 100 mM Arg, 100 mM Glu, 1% glycerol, 1 mM DTT, and containing 200 mM trehalose, with 0.001 ml of reservoir solution containing 2.1 M ammonium sulfate, 100 mM HEPES pH 7.0, 2% PEG 400 and 10 mM MgCl2, cryoprotection by 25% glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution, usage molecular replacement and of self-interaction chromatography for process optimization	Bacillus anthracis

Crystallization (Comment)

Organism

sitting drop and hanging drop vapour diffusion method, mixing 0.001 ml of 4 mg/ml protein in 50 mM Tris, pH 7.0, 100 mM NaCl, 100 mM Arg, 100 mM Glu, 1% glycerol, 1 mM DTT, and containing 200 mM trehalose, with 0.001 ml of reservoir solution containing 2.1 M ammonium sulfate, 100 mM HEPES pH 7.0, 2% PEG 400 and 10 mM MgCl2, cryoprotection by 25% glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution, usage molecular replacement and of self-interaction chromatography for process optimization

Bacillus anthracis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.025	-	nicotinate ribonucleotide	pH 7.5, recombinant enzyme	Bacillus anthracis
0.044	-	ATP	pH 7.5, recombinant enzyme	Bacillus anthracis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Bacillus anthracis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
23347	-	x * 23347, sequence calculation	Bacillus anthracis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + nicotinate ribonucleotide	Bacillus anthracis	NaMNAT is the penultimate enzyme in the biosynthesis of NAD+ and catalyzes the adenylation of nicotinic acid mononucleotide by ATP to form nicotinic acid adenine dinucleotide	diphosphate + deamido-NAD+	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus anthracis	A0A6L7H177	gene nadD	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration to homogeneity	Bacillus anthracis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + nicotinate ribonucleotide	-	Bacillus anthracis	diphosphate + deamido-NAD+	-	?
ATP + nicotinate ribonucleotide	NaMNAT is the penultimate enzyme in the biosynthesis of NAD+ and catalyzes the adenylation of nicotinic acid mononucleotide by ATP to form nicotinic acid adenine dinucleotide	Bacillus anthracis	diphosphate + deamido-NAD+	-	?

Subunits

Subunits	Comment	Organism
?	x * 23347, sequence calculation	Bacillus anthracis
More	presence of considerable conformational heterogeneity and flexibility in three loops surrounding the substrate-binding area, analysis of protein aggregation during purification by self-interaction chromatography	Bacillus anthracis

Synonyms

Synonyms	Comment	Organism
NaMNAT	-	Bacillus anthracis
nicotinic acid mononucleotide adenylyltransferase	-	Bacillus anthracis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Bacillus anthracis

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Bacillus anthracis