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Updated reaction and EC number (transferred by IUBMB in 2013: http://www.enzyme-database.org/query.php?ec=2.4.2.11)
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{{enzyme
{{enzyme
| Name = nicotinate phosphoribosyltransferase
| Name = nicotinate phosphoribosyltransferase
| EC_number = 2.4.2.11
| EC_number = 6.3.4.21
| CAS_number = 9030-26-6
| CAS_number = 9030-26-6
| IUBMB_EC_number = 2/4/2/11
| IUBMB_EC_number = 6/3/4/21
| GO_code = 0004516
| GO_code = 0004516
| image =
| image =
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| caption =
| caption =
}}
}}
In [[enzymology]], a '''nicotinate phosphoribosyltransferase''' ({{EC number|2.4.2.11}}) 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]]


:nicotinate D-ribonucleotide + diphosphate <math>\rightleftharpoons</math> nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate
:nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H<sub>2</sub>O <math>\rightleftharpoons</math> nicotinate D-ribonucleotide + diphosphate + ADP + phosphate


Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[nicotinate D-ribonucleotide]] and [[diphosphate]], whereas its two [[product (chemistry)|products]] are [[nicotinate]] and [[5-phospho-alpha-D-ribose 1-diphosphate]].
Thus, the four [[substrate (biochemistry)|substrates]] of this enzyme are [[nicotinate]], [[Phosphoribosyl pyrophosphate|5-phospho-alpha-D-ribose 1-diphosphate]], [[Adenosine triphosphate|ATP]], and [[Water|H<sub>2</sub>O]], whereas its four [[product (chemistry)|products]] are [[nicotinate D-ribonucleotide]], [[diphosphate]], [[Adenosine diphosphate|ADP]], and [[phosphate]].


This enzyme belongs to the family of [[glycosyltransferase]]s, 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]].
This enzyme belongs to the family of [[ligase]]s, 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==
==Structural studies==

Revision as of 12:20, 3 July 2015

nicotinate phosphoribosyltransferase
Identifiers
EC no.6.3.4.21
CAS no.9030-26-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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.{{cite journal}}: CS1 maint: multiple names: authors list (link)