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Information on EC 6.3.4.21 - nicotinate phosphoribosyltransferase and Organism(s) Escherichia coli and UniProt Accession P18133
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6.3.4.21 nicotinate phosphoribosyltransferaseIUBMB Comments
The enzyme, which is involved in pyridine nucleotide recycling, can form beta-nicotinate D-ribonucleotide and diphosphate from nicotinate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) in the absence of ATP. However, when ATP is available the enzyme is phosphorylated resulting in a much lower Km for nicotinate. The phospho-enzyme is hydrolysed during the transferase reaction, regenerating the low affinity form. The presence of ATP shifts the products/substrates equilibrium from 0.67 to 1100 .
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Word Map
- 6.3.4.21
-
salvage
- nampt
-
2.4.2.11
- quinolinate
- nicotinamidase
- deamidase
-
preiss-handler
- nmnat
- medicine
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
nicotinic acid phosphoribosyltransferase, nicotinate phosphoribosyltransferase, naprtase, naprt1, na phosphoribosyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
niacin ribonucleotidase
-
-
-
-
nicotinate-nucleotide:pyrophosphate phospho-alpha-D-ribosyltransferase
-
-
-
-
nicotinic acid mononucleotide glycohydrolase
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
5-phospho-alpha-D-ribose 1-diphosphate:nicotinate ligase (ADP, diphosphate-forming)
The enzyme, which is involved in pyridine nucleotide recycling, can form beta-nicotinate D-ribonucleotide and diphosphate from nicotinate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) in the absence of ATP. However, when ATP is available the enzyme is phosphorylated resulting in a much lower Km for nicotinate. The phospho-enzyme is hydrolysed during the transferase reaction, regenerating the low affinity form. The presence of ATP shifts the products/substrates equilibrium from 0.67 to 1100 [4].
CAS REGISTRY NUMBER
COMMENTARY
9030-26-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
-
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
-
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.7
recombinant enzyme from Escherichia coli strain BA002, pH and temperature not specified in the publication
1.01
recombinant enzyme from Escherichia coli strain BA015, pH and temperature not specified in the publication
10.54
recombinant enzyme from Escherichia coli strain BA014, pH and temperature not specified in the publication
18.74
recombinant enzyme from Escherichia coli strain BA016, pH and temperature not specified in the publication
0.08
-
recombinant enzyme from Escherichia coli strain BA203, pH and temperature not specified in the publication
0.7
-
recombinant enzyme from Escherichia coli strain BA002, pH and temperature not specified in the publication
0.74
-
recombinant enzyme from Escherichia coli strain BA204, pH and temperature not specified in the publication
1.01
-
recombinant enzyme from Escherichia coli strain BA206, pH and temperature not specified in the publication
10.54
-
recombinant enzyme from Escherichia coli strain BA014, pH and temperature not specified in the publication
12.24
-
recombinant enzyme from Escherichia coli strain BA207, pH and temperature not specified in the publication
17.31
-
recombinant enzyme from Escherichia coli strain BA206, pH and temperature not specified in the publication
23.72
-
recombinant enzyme from Escherichia coli strain BA207, pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
bacteria disruption by alumina grinding, protamine sulfate precipitation and chromatography on DEAE-cellulose
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Imsande, J.
Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia coli
J. Biol. Chem.
236
1494-1497
1961
Escherichia coli
Liang, L.; Liu, R.; Wang, G.; Gou, D.; Ma, J.; Chen, K.; Jiang, M.; Wei, P.; Ouyang, P.
Regulation of NAD(H) pool and NADH/NAD(+) ratio by overexpression of nicotinic acid phosphoribosyltransferase for succinic acid production in Escherichia coli NZN111
Enzyme Microb. Technol.
51
286-293
2012
Escherichia coli (P18133), Escherichia coli
Ma, J.; Gou, D.; Liang, L.; Liu, R.; Chen, X.; Zhang, C.; Zhang, J.; Chen, K.; Jiang, M.
Enhancement of succinate production by metabolically engineered Escherichia coli with co-expression of nicotinic acid phosphoribosyltransferase and pyruvate carboxylase
Appl. Microbiol. Biotechnol.
97
6739-6747
2013
Escherichia coli (P18133), Escherichia coli
Liu, R.; Liang, L.; Wu, M.; Chen, K.; Jiang, M.; Ma, J.; Wei, P.; Ouyang, P.
CO2 fixation for succinic acid production by engineered Escherichia coli co-expressing pyruvate carboxylase and nicotinic acid phosphoribosyltransferase
Biochem. Eng. J.
79
77-83
2013
Escherichia coli
-
Jiang, M.; Chen, X.; Liang, L.; Liu, R.; Wan, Q.; Wu, M.; Zhang, H.; Ma, J.; Chen, K.; Ouyang, P.
Co-expression of phosphoenolpyruvate carboxykinase and nicotinic acid phosphoribosyltransferase for succinate production in engineered Escherichia coli
Enzyme Microb. Technol.
56
8-14
2013
Escherichia coli
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