Nicotinate-nucleotide diphosphorylase (carboxylating)

In enzymology, a nicotinate-nucleotide diphosphorylase (carboxylating) (EC 2.4.2.19) is an enzyme that catalyzes the chemical reaction

nicotinate-nucleotide diphosphorylase (carboxylating)
Nicotinate-nucleotide pyrophosphorylase (carboxylating) hexamer, Human
Identifiers
EC no.2.4.2.19
CAS no.37277-74-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
nicotinate D-ribonucleotide + diphosphate + CO2 pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate

The 3 substrates of this enzyme are nicotinate D-ribonucleotide, diphosphate, and CO2, whereas its two products are pyridine-2,3-dicarboxylate and 5-phospho-alpha-D-ribose 1-diphosphate.

This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is nicotinate-nucleotide:diphosphate phospho-alpha-D-ribosyltransferase (carboxylating). Other names in common use include quinolinate phosphoribosyltransferase (decarboxylating), quinolinic acid phosphoribosyltransferase, QAPRTase, NAD+ pyrophosphorylase, nicotinate mononucleotide pyrophosphorylase (carboxylating), and quinolinic phosphoribosyltransferase. This enzyme participates in nicotinate and nicotinamide metabolism.

Structural studies

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As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1QAP, 1QPN, 1QPO, 1QPQ, 1QPR, 1X1O, 2B7N, 2B7P, and 2B7Q.

References

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  • GHOLSON RK, UEDA I, OGASAWARA N, HENDERSON LM (1964). "The Enzymatic Conversion of Quinolinate to Nicotinic Acid Mononucleotide in Mammalian Liver". J. Biol. Chem. 239 (4): 1208–14. doi:10.1016/S0021-9258(18)91413-4. PMID 14165928.
  • Packman PM, Jakoby WB (1965). "Crystalline quinolinate phosphoribosyltransferase". J. Biol. Chem. 240 (10): 4107–8. doi:10.1016/S0021-9258(18)97157-7. PMID 5320648.