Nicotinate-nucleotide diphosphorylase (carboxylating)

Nicotinate-nucleotide diphosphorylase (carboxylating)
nicotinate-nucleotide diphosphorylase (carboxylating)
Identifiers
EC number 2.4.2.19
CAS number 37277-74-0
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 / EGO

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

nicotinate D-ribonucleotide + diphosphate + CO2 \rightleftharpoons 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

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

  • 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: 1208–14. PMID 14165928. 
  • Packman PM, Jakoby WB (1965). "Crystalline quinolinate phosphoribosyltransferase". J. Biol. Chem. 240 (10): 4107–8. PMID 5320648. 
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