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

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This record set is specific for:
Escherichia coli
UNIPROT: P30011


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria


The taxonomic range for the selected organisms is: Escherichia coli

EC NUMBER
COMMENTARY hide
2.4.2.19
-
RECOMMENDED NAME
GeneOntology No.
nicotinate-nucleotide diphosphorylase (carboxylating)
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
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NAD biosynthesis from 2-amino-3-carboxymuconate semialdehyde
-
-
NAD biosynthesis I (from aspartate)
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-
nicotine biosynthesis
-
-
superpathway of nicotine biosynthesis
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NAD metabolism
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Nicotinate and nicotinamide metabolism
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Metabolic 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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
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
INHIBITORS
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
-
0.0064
quinolinate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
2 * 36000, SDS-PAGE
70000
gel filtration
SUBUNITS
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