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Information on EC 2.4.2.19 - nicotinate-nucleotide diphosphorylase (carboxylating) and Organism(s) Saccharomyces cerevisiae and UniProt Accession P43619

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EC Tree
IUBMB 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 .
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P43619
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
quinolinate phosphoribosyltransferase, quinolinic acid phosphoribosyltransferase, qaprtase, nad pyrophosphorylase, qprtase, quinolinate phosphoribosyl transferase, hqprtase, spnadc, quinolate phosphoribosyltransferase, quinolinate phosphoribosyltransferase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
quinolinate phosphoribosyl transferase
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general stress protein 70
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-
-
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GSP70
-
-
-
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NAD pyrophosphorylase
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-
-
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NadC
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-
-
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nicotinate mononucleotide pyrophosphorylase (carboxylating) (EC 2.4.2.19)
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-
-
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nicotinate-nucleotide pyrophosphorylase (carboxylating)
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-
-
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nicotinate-nucleotide:pyrophosphate phospho-alpha-D-ribosyltransferase (decarboxylating)
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-
-
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pyrophosphorylase, nicotinate mononucleotide (carboxylating)
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-
-
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QAPRTase
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-
-
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QPRTase
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-
-
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quinolinate phosphoribosyltransferase
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-
-
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quinolinate phosphoribosyltransferase (decarboxylating)
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-
-
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quinolinate phosphoribosyltransferase [decarboxylating]
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-
-
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quinolinic acid phosphoribosyltransferase
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-
-
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quinolinic phosphoribosyltransferase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
nicotinate-D-ribonucleotide:diphosphate phospho-alpha-D-ribosyltransferase (carboxylating)
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].
CAS REGISTRY NUMBER
COMMENTARY hide
37277-74-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
quinolinic acid + 5-phospho-alpha-D-ribose 1-diphosphate
nicotinic acid mononucleotide + diphosphate + CO2
show the reaction diagram
-
-
-
?
pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate
nicotinate D-ribonucleotide + diphosphate + CO2
show the reaction diagram
-
-
-
?
additional information
?
-
-
enzyme of the kynurenine pathway
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme of the kynurenine pathway
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
191000
6 * 191000, dynamic light scattering analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
6 * 191000, dynamic light scattering analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo, quinolinate-bound, 5-phospho-alpha-D-ribose 1-diphosphate-bound, and phthalate-bound forms. Crystallized at room temperature by the hanging drop vapor diffusion method. Both apo and holo crystals belong to space group R32 (alpha = 90°, beta = 90°, and gamma = 120°). One molecule per asymmetric unit except in QAPRTase holophthalate crystals where two molecules are found. The unit cell dimensions are: a = b = 154.9 A and c = 68.9 A (apo), a = b = 154.8 A and c = 68.6 A (holoquinolinate), a = b = 154.9 A and c = 70.6 A (holo-5-phospho-alpha-D-ribose 1-diphosphate), a = b = 155.5 A and c = 121.1 A (holophthalate), a = b = 154.7 A and c = 69.3 A (holophthalate-5-phospho-alpha-D-ribose 1-diphosphate)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into plasmid pTYB12 and expressed in Escherichia coli BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Panozzo, C.; Nawara, M.; Suski, C.; Kucharczyka, R.; Skoneczny, M.; Becam, A.M.; Rytka, J.; Herbert, C.J.
Aerobic and anaerobic NAD+ metabolism in Saccharomyces cerevisiae
FEBS Lett.
517
97-102
2002
Saccharomyces cerevisiae
Manually annotated by BRENDA team
di Luccio, E.; Wilson, D.K.
Comprehensive X-ray structural studies of the quinolinate phosphoribosyl transferase (BNA6) from Saccharomyces cerevisiae
Biochemistry
47
4039-4050
2008
Saccharomyces cerevisiae (P43619), Saccharomyces cerevisiae
Manually annotated by BRENDA team