Nicotinamide-nucleotide adenylyltransferase

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nicotinamide-nucleotide adenylyltransferase
1kku.jpg
Nicotinamide-nucleotide adenylyltransferase (nuclear) hexamer, Human
Identifiers
EC number 2.7.7.1
CAS number 9032-70-6
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO

In enzymology, a nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1) is an enzyme that catalyzes the chemical reaction

ATP + nicotinamide ribonucleotide diphosphate + NAD+

Thus, the two substrates of this enzyme are ATP and nicotinamide ribonucleotide, whereas its two products are diphosphate and NAD+.

This enzyme participates in nicotinate and nicotinamide metabolism.

The human version of this protein is NMNAT1.

Belongs to[edit]

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:nicotinamide-nucleotide adenylyltransferase. Other names in common use include NAD+ pyrophosphorylase, adenosine triphosphate-nicotinamide mononucleotide transadenylase, ATP:NMN adenylyltransferase, diphosphopyridine nucleotide pyrophosphorylase, nicotinamide adenine dinucleotide pyrophosphorylase, nicotinamide mononucleotide adenylyltransferase, and NMN adenylyltransferase.

Structural studies[edit]

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1EJ2, 1GZU, 1HYB, 1KKU, 1KQN, 1KQO, 1KR2, 1M8F, 1M8G, 1M8J, and 1M8K.

References[edit]

  • ATKINSON MR, JACKSON JF, MORTON RK (1961). "Nicotinamide mononucleotide adenylyltransferase of pig-liver nuclei. The effects of nicotinamide mononucleotide concentration and pH on dinucleotide synthesis". Biochem. J. 80 (2): 318&ndash, 23. PMC 1244001. PMID 13684981.
  • Dahmen W, Webb B, Preiss J (1967). "The deamido-diphosphopyridine nucleotide and diphosphopyridine nucleotide pyrophosphorylases of Escherichia coli and yeast". Arch. Biochem. Biophys. 120 (2): 440&ndash, 50. doi:10.1016/0003-9861(67)90262-7. PMID 4291828.
  • Kornberg A; Pricer WE (1951). "Enzymatic cleavage of diphosphopyridine nucleotide with radioactive pyrophosphate". J. Biol. Chem. 191 (2): 535&ndash, 541. PMID 14861199.