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Information on EC 2.4.2.19 - nicotinate-nucleotide diphosphorylase (carboxylating) and Organism(s) Escherichia coli and UniProt Accession P30011

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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:
Escherichia coli
UNIPROT: P30011
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The taxonomic range for the selected organisms is: Escherichia coli
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
general stress protein 70
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GSP70
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-
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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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nicotinate-nucleotide pyrophosphorylase (carboxylating)
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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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QAPRTase
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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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-
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quinolinic acid phosphoribosyltransferase
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-
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quinolinic phosphoribosyltransferase
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-
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
beta-nicotinate D-ribonucleotide + diphosphate + CO2 = pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
ordered binding mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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-
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-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-fructose-1,6-diphosphate
competitive with respect to 5-phosphoribosyl-1-diphosphate and noncompetitive with respect to quinolinate
diphosphate
noncompetitive with respect to both 5-phosphoribosyl-1-diphosphate and quinolinate
nicotinate mononucleotide
competitive with respect to 5-phosphoribosyl-1-diphosphate
Phthalic acid
dead-end inhibitor, competitive with respect to quinolinate, uncompetitive with respect to 5-phosphoribosyl-1-diphosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0156
5-phospho-alpha-D-ribose 1-diphosphate
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0.0064
quinolinate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
2 * 36000, SDS-PAGE
70000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 36000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for 1 month
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bhatia, R.; calvo, K.C.
The sequencing, expression, purification, and steady-state kinetic analysis of quinolinate phosphoribosyl transferase from Escherichia coli
Arch. Biochem. Biophys.
325
270-278
1996
Escherichia coli (P30011), Escherichia coli
Manually annotated by BRENDA team