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2.7.7.1: nicotinamide-nucleotide adenylyltransferase

This is an abbreviated version!
For detailed information about nicotinamide-nucleotide adenylyltransferase, go to the full flat file.

Word Map on EC 2.7.7.1

Reaction

ATP
+
nicotinamide ribonucleotide
=
diphosphate
 +
NAD+

Synonyms

adenosine triphosphate-nicotinamide mononucleotide transadenylase, adenylyltransferase, nicotinamide mononucleotide, Arabidopsis thaliana nicotinate/nicotinamide mononucleotide adenyltransferase, AtNMNAT, ATP:NMN adenylyltransferase, diphosphopyridine nucleotide pyrophosphorylase, Drosophila NMNAT, GlNMNAT, hNMNAT, hNMNAT-1, hNMNAT-2, human nicotinamide mononucleotide adenylyl-transferase, m-nonN-Nmnat1, mononucleotide adenylyltransferase, More, NAD synthase, NAD+ pyrophosphorylase, nadD, NadM-Nudix, NadR, NaMNAT, nicotinamide 5'-mononucleotide adenylyltransferase, nicotinamide 5'-mononucleotide adenylyltransferase-2, nicotinamide 5-mononucleotide adenylyltransferase-2, nicotinamide adenine dinucleotide pyrophosphorylase, nicotinamide mononucleotide adenylyl-transferase, nicotinamide mononucleotide adenylyltransferase, nicotinamide mononucleotide adenylyltransferase 1, nicotinamide mononucleotide adenylyltransferase 2, nicotinamide mononucleotide adenylyltransferase type 1, nicotinamide mononucleotide adenylyltransferase1, nicotinamide mononucleotide adenylyltransferase2, nicotinamide/nicotinate mononucleotide adenylyltransferase, nicotinamide/nicotinic acid mononucleotide adenylyltransferase, nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, nicotinate/nicotinamide mononucleotide adenyltransferase, NMN adenylyl transferase 1, NMN adenylyltransferase, NMN adenylyltransferase/ADP-ribose pyrophosphatase, NMN AT, NMN-adenylyltransferase, NMN/NaMN adenylyltransferase, NMN/NaMN adenylyltransferase 2, NMN/NaMN adenylyltransferase 3, NMNAT, NMNAT-2, NMNAT1, NMNAT2, NMNAT3, NMNATase, non-nuclear-localized-Nmnat1, PF3D7_1327600, PNAT, Pof1, pyridine nucleotide adenylyltransferase, Tc00.1047053507047.170, TK0067, TTHA1780, yNMNAT-1, yNMNAT-2

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.1 nicotinamide-nucleotide adenylyltransferase

Crystallization

Crystallization on EC 2.7.7.1 - nicotinamide-nucleotide adenylyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method, co-crystallization of ftNadM-Nudix complexed with the product AMP and Mn2+ ions in the Nudix active site
hanging drop vapor diffusion method, 20 mg/ml protein mixed with an equal volume of reservoir solution containing 1.8 M ammonium sulfate, 0.1 M Tris, pH 8 and 4% v/v isopropyl alcohol, 4-5 days at 20°C, monoclinic space group P21 if 20% glycerol is used, hexagonal space group P6322 if light paraffin oil is used
hanging drop vapor diffusion method, 20 mg/ml protein mixed with an equal volume of reservoir solution containing 100 mM sodium cacodylate, pH 6-7, 200 mM Li2SO4 and 20-25% polyethylene glycol 400
-
hanging drop vapor diffusion method, 25 mg/ml protein in 100 mM HEPES, pH 7.2, 0.5 M NaCl, 2 mM dithiothreitol, 1 mM EDTA and 0.03% Brij-35 was incubated with 10 mM NAD+ and then mixed with an equal volume of reservoir solution containing 0.1 mM sodium acetate, pH 4.2-6.4 and 1.6-1.8 mM sodium formate at 20°C for 1-2 weeks, monoclinic space group P21
homology modeling of structure, based on structures of isoform NMNAT1 and NMNAT3 and molecular docking of potential inhibitors
crystals of the enzyme in complex with ATP are grown using the hanging-drop vapor-diffusion method. The structure in complex with ATP has been solved by X-ray crystallography at 2.0 A resolution, using a combination of single isomorphous replacement and density modification techniques. The structure reveals a hexamer with 32 point group symmetry composed of alpha/beta topology subunits
hanging drop vapor diffusion method, in 100 mM HEPES, pH 7.5 at 20°C, crystals of native enzyme were grown in 1.5 M Li2SO4, crystals of H19A enzyme were grown in 1.6 M Li2SO4, space group: P6322
-
purified detagged recombinant wild-type and mutant enzymes, hanging drop vapour diffusion, method screening, mixing of 0.002 ml of 10 mg/ml protein in 10 mM HEPES, pH 7.5, 0.5 M NaCl, and 5 mM ligand NAD+ or NADP+, with 0.002 ml of reservoir solution containing 1.5-1.6 M ammonium sulfate, 5% glycerol, 100 mM Tris, pH 8.0, and equilibration against 0.5 ml of reservoir solution, 20°C, 48-72 h, X-ray diffraction structure determination and analysis at 1.9-2.3 A resolution, molecular replacement
structure of NMNAT3 to 2 A resolution
structures of NaMNAT in the product-bound state with nicotinic acid adenine dinucleotide and complexed with an alpha,beta-non-hydrolizable ATP analog to a resolution of 2.2 A and 2.5 A, respectively. NaMNAT possesses two cysteine residues within the active site likely to be involved in redox regulation of NaMNAT activity. NaMNAT is capable of utilizing nicotinic acid adenine dinucleotide and nicotinamide mononucleotide, reactions of EC 2.7.7.18 and EC 2.7.7.1, resectively, with a slight preference for nicotinic acid adenine dinucleotide
the enzyme is complexed with the co-purified NAD and pyrophosphate in the NadM-domain active site, and with ADPR substrate in the Nudix-domain, X-ray diffraction structure determination and analysis at 2.6 A resolution