Nicotinate phosphoribosyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a nicotinate phosphoribosyltransferase (EC 2.4.2.11) is an enzyme that catalyzes the chemical reaction

nicotinate D-ribonucleotide + diphosphate $\rightleftharpoons$ nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate

Thus, the two substrates of this enzyme are nicotinate D-ribonucleotide and diphosphate, whereas its two products are nicotinate 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. Other names in common use include niacin ribonucleotidase, nicotinic acid mononucleotide glycohydrolase, nicotinic acid mononucleotide pyrophosphorylase, and nicotinic acid phosphoribosyltransferase. This enzyme participates in nicotinate and nicotinamide metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1VLP, 1YBE, 1YIR, 1YTD, 1YTE, 1YTK, and 2F7F.

[edit] References

IUBMB entry for 2.4.2.11
BRENDA references for 2.4.2.11 (Recommended.)
PubMed references for 2.4.2.11
PubMed Central references for 2.4.2.11
Google Scholar references for 2.4.2.11
IMSANDE J (1961). "Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia coli". J. Biol. Chem. 236: 1494–7. PMID 13717628.
IMSANDE J, HANDLER P (1961). "Biosynthesis of diphosphopyridine nucleotide. III. Nicotinic acid mononucleotide pyrophos-phorylase". J. Biol. Chem. 236: 525–30. PMID 13717627.
Kosaka A, Spivey HO, Gholson RK (1971). "Nicotinate phosphoribosyltransferase of yeast. Purification and properties". J. Biol. Chem. 246: 3277–83. PMID 4324895.