| EC |
2.4.2.19 |
| Accepted name: |
nicotinate-nucleotide diphosphorylase (carboxylating) |
| Reaction: |
β-nicotinate D-ribonucleotide + diphosphate + CO2 = pyridine-2,3-dicarboxylate + 5-phospho-α-D-ribose 1-diphosphate |
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For diagram of NAD+ biosynthesis, click here |
| Glossary: |
quinolinate = pyridine-2,3-dicarboxylate |
| Other name(s): |
quinolinate phosphoribosyltransferase (decarboxylating); quinolinic acid phosphoribosyltransferase; QAPRTase; NAD+ pyrophosphorylase; nicotinate mononucleotide pyrophosphorylase (carboxylating); quinolinic phosphoribosyltransferase |
| Systematic name: |
β-nicotinate-D-ribonucleotide:diphosphate phospho-α-D-ribosyltransferase (carboxylating) |
| 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: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37277-74-0 |
| 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 (1964) 1208–1214. [PMID: 14165928] |
| 2. |
Packman, P.M. and Jakoby, W.B. Crystalline quinolinate phosphoribosyltransferase. J. Biol. Chem. 240 (1965) 4107–4108. [PMID: 5320648] |
| 3. |
Katoh, A., Uenohara, K., Akita, M. and Hashimoto, T. Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid. Plant Physiol. 141 (2006) 851–857. [DOI] [PMID: 16698895] |
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| [EC 2.4.2.19 created 1972] |
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