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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Application

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

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.18 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.18 0.025
-
 nicotinate ribonucleotide pH 7.5, recombinant enzyme Bacillus anthracis
2.7.7.18 0.044
-
 ATP pH 7.5, recombinant enzyme Bacillus anthracis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.18 Mg2+
-
 Bacillus anthracis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.7.18 23347
-
 x * 23347, sequence calculation Bacillus anthracis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.18 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

EC Number Organism UniProt Comment Textmining
2.7.7.18 Bacillus anthracis A0A6L7H177 gene nadD
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.18 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.18 ATP + nicotinate ribonucleotide
-
 Bacillus anthracis diphosphate + deamido-NAD+
-
 ?
2.7.7.18 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

EC Number Subunits Comment Organism
2.7.7.18 ? x * 23347, sequence calculation Bacillus anthracis
2.7.7.18 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

EC Number Synonyms Comment Organism
2.7.7.18 NaMNAT
-
 Bacillus anthracis
2.7.7.18 nicotinic acid mononucleotide adenylyltransferase
-
 Bacillus anthracis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.18 7.5
-
 assay at Bacillus anthracis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.7.18 ATP
-
 Bacillus anthracis