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Literature summary for 2.7.7.1 extracted from

  • Lowe, G.; Tansley, G.
    The stereochemical course of nucleotidyl transfer catalysed by NAD pyrophosphorylase (1983), Eur. J. Biochem., 132, 117-120.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Sus scrofa
Mg2+ MgATP2- is the reactive substrate Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + nicotinamide ribonucleotide Sus scrofa
-
diphosphate + NAD+
-
r

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + nicotinamide ribonucleotide = diphosphate + NAD+ mechanism Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + nicotinamide ribonucleotide
-
Sus scrofa diphosphate + NAD+
-
r
ATP + nicotinamide ribonucleotide i.e. NMN or nicotinamide mononucleotide Sus scrofa diphosphate + NAD+
-
r
ATP + nicotinamide ribonucleotide stereochemistry: catalyses nucleotidyl transfer from adenosine (R)-5'-triphosphate to nicotinamide mononucleotide with inversion of configuration at the alpha-phosphate giving (S)-NAD+ Sus scrofa diphosphate + NAD+
-
r