Nicotinate phosphoribosyltransferase

In enzymology, a nicotinate phosphoribosyltransferase (EC 6.3.4.21) is an enzyme that catalyzes the chemical reaction

nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
nicotinate phosphoribosyltransferase
Nicotinate phosphoribosyltransferase dimer, Human
Identifiers
EC number6.3.4.21
CAS number9030-26-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the four substrates of this enzyme are nicotinate, 5-phospho-alpha-D-ribose 1-diphosphate, ATP, and H2O, whereas its four products are nicotinate D-ribonucleotide, diphosphate, ADP, and phosphate.

This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is 5-phospho-alpha-D-ribose 1-diphosphate:nicotinate ligase (ADP, diphosphate-forming) . 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.

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.

References

    • 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 (10): 3277–83. PMID 4324895.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.