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Literature summary extracted from

  • Rizzi, M.; Bolognesi, M.; Coda, A.
    A novel deamido-NAD+-binding site revealed by the trapped NAD-adenylate intermediate in the NAD+ synthetase structure (1998), Structure, 6, 1129-1140.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.1.5 enzyme in complex with ATP, ATP-Tl+, ATP-Mn2+, or NAD-adenylate, hanging-drop vapour diffusion method, 15 mg/ml protein, 5 mM ATP, 20 mM NAD+ in 0.1 M sodium acetate, pH 5.2, 22% PEG 400, and 50 mM MgCl2, thallium acetate, or MnCl2 20°C, 24 h before data collection the crystale are soaked in a cryoprotectant buffer, X-ray diffraction structure determination at 1.3 A resolution, structure analysis and modeling Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.1.5 K+ required, 2 binding sites near the bound diphosphate at the ATP-binding site, can be substituted by Tl+ Bacillus subtilis
6.3.1.5 Mg2+ 2 Mg2+ ligands per molecule of enzyme Bacillus subtilis
6.3.1.5 Tl+ can substitute for K+ Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.1.5 ATP + deamido-NAD+ + NH3 Bacillus subtilis NAD-adenylate intermediate, key two step reaction in NAD+ biosynthesis AMP + diphosphate + NAD+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.1.5 Bacillus subtilis P08164
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.3.1.5 ATP + deamido-NAD+ + NH3 = AMP + diphosphate + NAD+ reaction mechanism, determination of deamido-NAD+-binding site, Asp173 is the key residue in both deprotonation of the primarily bound ammonium ion, and stabilization of the tetrahedral transition-state intermediate Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.1.5 ATP + deamido-NAD+ + NH3 NAD-adenylate intermediate, two step reaction Bacillus subtilis AMP + diphosphate + NAD+
-
 ?
6.3.1.5 ATP + deamido-NAD+ + NH3 NAD-adenylate intermediate, key two step reaction in NAD+ biosynthesis Bacillus subtilis AMP + diphosphate + NAD+
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.1.5 dimer homodimer, crystal structure determination Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
6.3.1.5 NAD synthase
-
 Bacillus subtilis
6.3.1.5 NAD synthetase
-
 Bacillus subtilis
6.3.1.5 Nicotinamide adenine dinucleotide synthetase
-
 Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.1.5 ATP binuclear magnesium cluster Bacillus subtilis