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IUBMB 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 .
The taxonomic range for the selected organisms is: Escherichia coli The enzyme appears in selected viruses and cellular organisms
Synonyms
nicotinic acid phosphoribosyltransferase, nicotinate phosphoribosyltransferase, naprtase, naprt1, na phosphoribosyltransferase,
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nicotinic acid phosphoribosyltransferase
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niacin ribonucleotidase
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nicotinate-nucleotide:pyrophosphate phospho-alpha-D-ribosyltransferase
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nicotinic acid mononucleotide glycohydrolase
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nicotinic acid mononucleotide pyrophosphorylase
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nicotinic acid phosphoribosyltransferase
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pentosyl group transfer
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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].
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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
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nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
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nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
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nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
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r
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nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
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nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
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ATP
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Mg2+
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requirement
Mg2+
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maximal activity: 20 mM
Mg2+
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synergism with ATP
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0.03
5-phospho-alpha-D-ribose 1-diphosphate
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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
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recombinant enzyme from Escherichia coli strain BA203, pH and temperature not specified in the publication
0.7
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recombinant enzyme from Escherichia coli strain BA002, pH and temperature not specified in the publication
0.74
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recombinant enzyme from Escherichia coli strain BA204, pH and temperature not specified in the publication
1.01
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recombinant enzyme from Escherichia coli strain BA206, pH and temperature not specified in the publication
10.54
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recombinant enzyme from Escherichia coli strain BA014, pH and temperature not specified in the publication
12.24
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recombinant enzyme from Escherichia coli strain BA207, pH and temperature not specified in the publication
17.31
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recombinant enzyme from Escherichia coli strain BA206, pH and temperature not specified in the publication
23.72
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recombinant enzyme from Escherichia coli strain BA207, pH and temperature not specified in the publication
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additional information
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active over a wide range
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UniProt
brenda
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45000
x * 45000, SDS-PAGE
46000
x * 46000, SDS-PAGE
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?
x * 45000, SDS-PAGE
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bacteria disruption by alumina grinding, protamine sulfate precipitation and chromatography on DEAE-cellulose
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expressed in Escherichia coli NZN111
expressed in Escherichia coli strains BA002, BA014, BA015, and BA016
expressed in Escherichia coli strains BA002, BA014, BA026, and BA207
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expressed in Escherichia coli strains BA203, BA204, BA206, and BA209
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Imsande, J.
Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia coli
J. Biol. Chem.
236
1494-1497
1961
Escherichia coli
brenda
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
brenda
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
brenda
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
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brenda
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
brenda