EC 2.4.2.19 - Nicotinate-nucleotide diphosphorylase (carboxylating)

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IntEnz Enzyme Nomenclature
EC 2.4.2.19

Names

Accepted name:
nicotinate-nucleotide diphosphorylase (carboxylating)
Other names:
NAD pyrophosphorylase
QAPRTase
nicotinate mononucleotide pyrophosphorylase (carboxylating)
quinolinate phosphoribosyltransferase (decarboxylating)
quinolinic acid phosphoribosyltransferase
quinolinic phosphoribosyltransferase
nicotinate-nucleotide pyrophosphorylase (carboxylating)
nicotinate-nucleotide:diphosphate phospho-α-D-ribosyltransferase (carboxylating)
Systematic name:
β-nicotinate-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase (carboxylating)

Reaction

Comments:

The reaction is catalysed in the opposite direction. Since quinolinate is synthesized from L-tryptophan in eukaryotes, but from L-aspartate in some prokaryotes, this is the first NAD+ biosynthesis enzyme shared by both eukaryotes and prokaryotes [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004514
CAS Registry Number: 37277-74-0
UniProtKB/Swiss-Prot: (24) [show] [UniProt]

References

  1. Gholson, R.K., Ueda, I., Ogasawara, N. and Henderson, L.M.
    The enzymatic conversion of quinolinate to nicotinic acid mononucleotide in mammalian liver.
    J. Biol. Chem. 239 : 1208-1214 (1964).
  2. Packman, P.M. and Jakoby, W.B.
    Crystalline quinolinate phosphoribosyltransferase.
    J. Biol. Chem. 240 : 4107-4108 (1965). [PMID: 5320648]
  3. Katoh, A., Uenohara, K., Akita, M., Hashimoto, T.
    Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid.
    Plant Physiol. 141 : 851-857 (2006). [PMID: 16698895]

[EC 2.4.2.19 created 1972]