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Information on EC 2.4.2.19 - nicotinate-nucleotide diphosphorylase (carboxylating) and Organism(s) Helicobacter pylori and UniProt Accession O25909

for references in articles please use BRENDA:EC2.4.2.19
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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:
Helicobacter pylori
UNIPROT: O25909
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Word Map
The taxonomic range for the selected organisms is: Helicobacter pylori
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
type II quinolinic acid phosphoribosyltransferase
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general stress protein 70
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GSP70
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NAD pyrophosphorylase
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-
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NadC
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nicotinate mononucleotide pyrophosphorylase (carboxylating) (EC 2.4.2.19)
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nicotinate-nucleotide pyrophosphorylase (carboxylating)
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nicotinate-nucleotide:pyrophosphate phospho-alpha-D-ribosyltransferase (decarboxylating)
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pyrophosphorylase, nicotinate mononucleotide (carboxylating)
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QAPRTase
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-
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QPRTase
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quinolinate phosphoribosyltransferase
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quinolinate phosphoribosyltransferase (decarboxylating)
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quinolinate phosphoribosyltransferase [decarboxylating]
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quinolinic acid phosphoribosyltransferase
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quinolinic phosphoribosyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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-
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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
pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate
nicotinate D-ribonucleotide + diphosphate + CO2
show the reaction diagram
essential enzyme in the NAD+ biosynthetic pathway
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-
?
pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate
nicotinate D-ribonucleotide + diphosphate + CO2
show the reaction diagram
-
-
-
?
additional information
?
-
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key enzyme of NAD+ biosynthesis
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-
?
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
pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate
nicotinate D-ribonucleotide + diphosphate + CO2
show the reaction diagram
essential enzyme in the NAD+ biosynthetic pathway
-
-
?
additional information
?
-
-
key enzyme of NAD+ biosynthesis
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
Hp-QAPRTase forms a hexamer with a - trimer of dimers - configuration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of Hp-QAPRTase with bound quinolinic acid, nicotinic acid mononucleotide, and phthalic acid. Hp-QAPRTase crystals are grown at 20°C using the hanging drop vapor diffusion method
hanging-drop vapor-diffusion method
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, M.K.; Kim, Y.S.; Rho, S.H.; Im, Y.J.; Lee, J.H.; Kang, G.B.; Eom, S.H.
Crystallization and preliminary X-ray crystallographic analysis of quinolinate phosphoribosyltransferase of Helicobacter pylori
Acta Crystallogr. Sect. D
59
1265-1266
2003
Helicobacter pylori
Manually annotated by BRENDA team
Kim, M.; Im, Y.J.; Lee, J.H.; Eom, S.H.
Crystal structure of quinolinic acid phosphoribosyltransferase from Helicobacter pylori
Proteins
63
252-255
2006
Helicobacter pylori (O25909), Helicobacter pylori
Manually annotated by BRENDA team