Nicotinate phosphoribosyltransferase: Difference between revisions
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| IUBMB_EC_number = 6/3/4/21 |
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| GO_code = 0004516 |
| GO_code = 0004516 |
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| caption = Nicotinate phosphoribosyltransferase dimer, Human |
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In [[enzymology]], a '''nicotinate phosphoribosyltransferase''' ({{EC number|6.3.4.21}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] |
In [[enzymology]], a '''nicotinate phosphoribosyltransferase''' ({{EC number|6.3.4.21}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]] |
Revision as of 07:18, 2 November 2017
nicotinate phosphoribosyltransferase | |||||||||
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![]() Nicotinate phosphoribosyltransferase dimer, Human | |||||||||
Identifiers | |||||||||
EC no. | 6.3.4.21 | ||||||||
CAS no. | 9030-26-6 | ||||||||
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 / QuickGO | ||||||||
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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
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.