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Information on EC 6.3.4.21 - nicotinate phosphoribosyltransferase
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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 enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
EC 2.4.2.11, LOC_Os03g62110, More, NA phosphoribosyltransferase, NAPRT, NaPRT1, NAPRTase, niacin ribonucleotidase, nicotinate phosphoribosyltransferase, nicotinate phosphoribosyltransferases, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.4.2.11
NA phosphoribosyltransferase
NAPRT
NAPRTase
niacin ribonucleotidase
-
-
-
-
nicotinate phosphoribosyltransferase
nicotinate phosphoribosyltransferases
nicotinate-nucleotide:pyrophosphate phospho-alpha-D-ribosyltransferase
-
-
-
-
nicotinic acid mononucleotide glycohydrolase
-
-
-
-
nicotinic acid mononucleotide pyrophosphorylase
nicotinic acid phosphoribosyltransferase
pncB
additional information
enzyme is a member of the phosphoribosyltransferase superfamily or PRTase superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
sequential steady state mechanism
-
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O = beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
ordered ping pong kinetic mechanism
-
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O = beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
active site structure
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O = beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
active site structure
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O = beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
pentosyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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].
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CAS REGISTRY NUMBER
COMMENTARY
9030-26-6
-
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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 + GTP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + GDP + phosphate
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ITP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + IDP + phosphate
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
favoured reaction
-
r
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
favoured reaction
-
r
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
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
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
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
the pyridine N and carboxyl groups are important for interaction with the enzyme
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
in the presence of Mg2+ and inorganic phosphate
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
lack of the de novo pathway for NAD+ synthesis from tryptophan, utilizes both nicotinic acid and nicotinamide as NAD+ precursors
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
first step in NAD+-(salvage) biosynthesis
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
NAPRT is essential for nicotinic acid to increase cellular NAD levels and thus to prevent oxidative stress of the cells
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
+ whole cell lysates, pH 7.5, 37°C, 10 mM MgCl2, 2.5 mM dithiothreitol, 1 mM ATP, 25 microgram bovine serum albumin, with or without NAD+
termination by boiling for 60 seconds, analysis by thin layer chromatography (radiolabeled nicotinic acid) or ESI-MS, no NaMN detectable in Hep-G2 cells
-
r
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
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
-
-
r
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
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
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
first step in NAD+-(salvage) biosynthesis
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
essential for the NAD salvage pathway
-
-
r
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
the enzyme is a facultative ATPase that uses ATP hydrolysis to drive the synthesis of nicotinate mononucleotide and diphosphate from nicotinic acid and phosphoribosyl diphosphate in a steady-state reaction, the enzyme undergoes phosphorylation in His-219 by bound ATP, phosphorylated enzyme has higher affinity for substrates than does nonphosphorylated enzyme
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
the enzyme is a facultative ATPase that uses ATP hydrolysis to drive the synthesis of nicotinate mononucleotide and diphosphate from nicotinic acid and phosphoribosyl diphosphate in a steady-state reaction, the enzyme undergoes phosphorylation in His-219 by bound ATP, phosphorylated enzyme has higher affinity for substrates than does nonphosphorylated enzyme
-
-
r
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
mutants in the His-219 residue do catalyze the slow formation of nicotinic acid mononucleotide in the absence of ATP similarly to the wild type enzymes
-
-
?
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
-
no phosphoribosylation of nicotinamide, quinolic acid, adenine or hypoxanthine
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + GTP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + GDP + phosphate
-
-
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + GTP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + GDP + phosphate
-
-
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ITP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + IDP + phosphate
-
-
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ITP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + IDP + phosphate
-
5-phospho-alpha-D-ribose 1-diphosphate in complex with Mg
-
-
?
additional information
?
-
-
one mol ATP is cleaved per mol product formed
-
-
?
additional information
?
-
-
one mol ATP is cleaved per mol product formed
-
-
?
additional information
?
-
-
one mol ATP is cleaved per mol product formed
-
-
?
additional information
?
-
-
one mol ATP is cleaved per mol product formed
-
-
?
additional information
?
-
-
no ATPase activity in the absence of substrates
-
-
?
additional information
?
-
-
no ATPase activity in the absence of substrates
-
-
?
additional information
?
-
-
enzyme is able to generate adenosine 5'-tetraphosphate using substrate ATP and product phosphate, reaction of EC 3.6.1.14. Accompanying a typically irreversible hydrolysis of ATP to ADP and phosphate, is a fully reversible phosphate transfer reaction between ATP and adenosine 5'-tetraphosphate
-
-
?
additional information
?
-
-
ATP and phosphoribose diphosphate compete for ATP-binding site
-
-
?
additional information
?
-
-
ATPase activity in the presence of either product and in the absence of phosphoribose diphosphate
-
-
?
additional information
?
-
molecular evolution mechanism
-
-
?
additional information
?
-
-
negligible ATPase activity in the absence of nicotinic acid
-
-
?
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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
-
-
-
-
?
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
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
lack of the de novo pathway for NAD+ synthesis from tryptophan, utilizes both nicotinic acid and nicotinamide as NAD+ precursors
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
first step in NAD+-(salvage) biosynthesis
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
NAPRT is essential for nicotinic acid to increase cellular NAD levels and thus to prevent oxidative stress of the cells
-
-
?
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
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
-
-
-
r
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
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
-
first step in NAD+-(salvage) biosynthesis
-
-
?
nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O
beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate
essential for the NAD salvage pathway
-
-
r
additional information
?
-
molecular evolution mechanism
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
60-70% stimulation with different enzyme preparations, the largest effects are observed with aged preparations of the enzyme
ATP
-
1 mol ATP is hydrolyzed to ADP plus phosphate per mol product formed
ATP
-
1 mol ATP is hydrolyzed to ADP plus phosphate per mol product formed
ATP
-
1 mol ATP is hydrolyzed to ADP plus phosphate per mol product formed
ATP
1 mol ATP is hydrolyzed to ADP plus phosphate per mol product formed
ATP
-
2000fold increase in the Kcat/KM
ATP
-
the Vmax of nicotinic acid mononucleotide synthesis activity is stimulated 10fold
ATP
1640fold increase in the product/substrate ratio
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
requirement, slight synergism with ATP, more effective than Mg2+ with or without ATP
Mg2+
MgATP2-
Mn2+
-
requirement, 7.5 mM, no synergism with ATP, more effective than Mg2+ with or without ATP
phosphate
additional information
Mg2+
omission of Mg2+ from the reaction mixture results in a complete loss of activity
MgATP2-
-
maximal activation at equimolar levels of Mg2+ and ATP, presumably enzyme structure stabilizing
additional information
-
absolute requirement of divalent cation, no activation with Ba2+, Ca2+, Cu2+, Cd2+, Al3+, Fe3+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
at 1 mM 40% inhibition of activity (concentrations of substrates 1 mM)
CoA
at 1 mM 70% inhibition of activity (concentrations of substrates 1 mM)
D-fructose 1,6-bisphosphate
at 1 mM 36% inhibition of activity (concentrations of substrates 1 mM)
glutaryl-CoA
at 1 mM 42% inhibition of activity (concentrations of substrates 1 mM)
glyceraldehyde 3-phosphate
at 1 mM 27% inhibition of activity (concentrations of substrates 1 mM)
phosphoenolpyruvate
at 1 mM 33% inhibition of activity (concentrations of substrates 1 mM)
succinyl-CoA
at 1 mM 53% inhibition of activity (concentrations of substrates 1 mM)
5-phospho-alpha-D-ribose 1-diphosphate
-
at high concentrations, when Mg2+ below 0.03 mM
ATP
-
3 mM, competitive inhibition of nicotinic acid mononucleotide formation in mutants enzymes
nicotinate mononucleotide
-
competitive to MgATP2-; non-competitive to nicotinate
nicotinate mononucleotide
-
competitive to nicotinate and noncompetitive to phosphoribobose diphosphate
additional information
-
no inhibition by nicotinamide; no inhibition by quinolinic acid, AMP, GMP
-
additional information
-
no inhibition by nicotinamide; no inhibition by nicotinate, up to 10 mM
-
additional information
not inhibited by up to 1 mM NAD+, lack of feedback inhibition by NAD+
-
additional information
-
not inhibited by up to 1 mM NAD+, lack of feedback inhibition by NAD+
-
additional information
not inhibitory: FK866. NaPRTase acks a tunnel that, in nicotinamide phosphoribosiltransferase EC 2.4.2.12, represents the binding site of inhibitor FK866
-
additional information
-
not inhibitory: FK866. NaPRTase acks a tunnel that, in nicotinamide phosphoribosiltransferase EC 2.4.2.12, represents the binding site of inhibitor FK866
-
additional information
-
no inhibition by antibodies against pig kidney quinolinate phosphoribosyltransferase; no inhibition by nicotinamide mononucleotide, deamino-NAD+
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
functional modulation by ATP via autophosphorylation of His232, activation by ATP hydrolysis, determination of the binding site
additional information
-
3,5-cycloadenosine, borate and sulfate do not affect the reaction rate
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Bone Marrow Failure Disorders
The complex genetic landscape of familial MDS and AML reveals pathogenic germline variants.
Carcinoma
Dependence of tumor cell lines and patient-derived tumors on the NAD salvage pathway renders them sensitive to NAMPT inhibition with GNE-618.
Carcinoma, Non-Small-Cell Lung
Dependence of tumor cell lines and patient-derived tumors on the NAD salvage pathway renders them sensitive to NAMPT inhibition with GNE-618.
Glioblastoma
Inhibition of nicotinamide phosphoribosyltransferase (NAMPT) activity by small molecule GMX1778 regulates reactive oxygen species (ROS)-mediated cytotoxicity in a p53- and nicotinic acid phosphoribosyltransferase1 (NAPRT1)-dependent manner.
Glioblastoma
The small molecule GMX1778 is a potent inhibitor of NAD+ biosynthesis: strategy for enhanced therapy in nicotinic acid phosphoribosyltransferase 1-deficient tumors.
Glioma
NAD+ depletion radiosensitizes 2-DG-treated glioma cells by abolishing metabolic adaptation.
Glucose Intolerance
Tissue-specific regulation of sirtuin and nicotinamide adenine dinucleotide biosynthetic pathways identified in C57Bl/6 mice in response to high-fat feeding.
Lymphoma
Expression patterns of nicotinamide phosphoribosyltransferase and nicotinic acid phosphoribosyltransferase in human malignant lymphomas.
Neoplasms
A preclinical study on the rescue of normal tissue by nicotinic acid in high-dose treatment with APO866, a specific nicotinamide phosphoribosyltransferase inhibitor.
Neoplasms
Anti-tumor NAMPT inhibitor, KPT-9274, mediates gender-dependent murine anemia and nephrotoxicity by regulating SIRT3-mediated SOD deacetylation.
Neoplasms
Dependence of tumor cell lines and patient-derived tumors on the NAD salvage pathway renders them sensitive to NAMPT inhibition with GNE-618.
Neoplasms
Dual and Specific Inhibition of NAMPT and PAK4 By KPT-9274 Decreases Kidney Cancer Growth.
Neoplasms
Extensive regulation of nicotinate phosphoribosyltransferase (NAPRT) expression in human tissues and tumors.
Neoplasms
Inhibition of nicotinamide phosphoribosyltransferase (NAMPT) activity by small molecule GMX1778 regulates reactive oxygen species (ROS)-mediated cytotoxicity in a p53- and nicotinic acid phosphoribosyltransferase1 (NAPRT1)-dependent manner.
Neoplasms
NAMPT and NAPRT1: novel polymorphisms and distribution of variants between normal tissues and tumor samples.
Neoplasms
Nicotinic Acid Phosphoribosyltransferase Regulates Cancer Cell Metabolism, Susceptibility to NAMPT Inhibitors, and DNA Repair.
Neoplasms
Supplementation of nicotinic acid with NAMPT inhibitors results in loss of in vivo efficacy in NAPRT1-deficient tumor models.
Neoplasms
Targeting the NAD Salvage Synthesis Pathway as a Novel Therapeutic Strategy for Osteosarcomas with Low NAPRT Expression.
Neoplasms
The complex genetic landscape of familial MDS and AML reveals pathogenic germline variants.
Neoplasms
The small molecule GMX1778 is a potent inhibitor of NAD+ biosynthesis: strategy for enhanced therapy in nicotinic acid phosphoribosyltransferase 1-deficient tumors.
Neuroblastoma
Inhibition of nicotinamide phosphoribosyltransferase (NAMPT) activity by small molecule GMX1778 regulates reactive oxygen species (ROS)-mediated cytotoxicity in a p53- and nicotinic acid phosphoribosyltransferase1 (NAPRT1)-dependent manner.
Neuroblastoma
The small molecule GMX1778 is a potent inhibitor of NAD+ biosynthesis: strategy for enhanced therapy in nicotinic acid phosphoribosyltransferase 1-deficient tumors.
nicotinate phosphoribosyltransferase deficiency
The small molecule GMX1778 is a potent inhibitor of NAD+ biosynthesis: strategy for enhanced therapy in nicotinic acid phosphoribosyltransferase 1-deficient tumors.
Ovarian Neoplasms
Nicotinic Acid Phosphoribosyltransferase Regulates Cancer Cell Metabolism, Susceptibility to NAMPT Inhibitors, and DNA Repair.
Sarcoma
Inhibition of nicotinamide phosphoribosyltransferase (NAMPT) activity by small molecule GMX1778 regulates reactive oxygen species (ROS)-mediated cytotoxicity in a p53- and nicotinic acid phosphoribosyltransferase1 (NAPRT1)-dependent manner.
Sarcoma
The small molecule GMX1778 is a potent inhibitor of NAD+ biosynthesis: strategy for enhanced therapy in nicotinic acid phosphoribosyltransferase 1-deficient tumors.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.16
ITP
-
good alternative substrate for ATP
0.00022
5-phospho-alpha-D-ribose 1-diphosphate
+/-0.07 microM, in presence of 1 mM NAD+, 20 ng enzyme, 40 microM nicotinamide, 0.14-1 microM PRPP, 15 min, 37°C, TLC-based quantification
0.00025
5-phospho-alpha-D-ribose 1-diphosphate
+/-0.06 microM, 20 ng enzyme, 40 microM nicotinamide, 0.14-1 microM PRPP, 15 min, 37°C, TLC-based quantification
0.013
5-phospho-alpha-D-ribose 1-diphosphate
-
reduced to 0.002 mM in the presence of ATP
0.013
5-phospho-alpha-D-ribose 1-diphosphate
-
reduced to 0.002 mM in the presence of ATP
0.02
5-phospho-alpha-D-ribose 1-diphosphate
-
in the coupled reaction, 200fold lower than in the uncoupled reaction
0.022
5-phospho-alpha-D-ribose 1-diphosphate
-
pncB gene, in the coupled reaction
0.0382
5-phospho-alpha-D-ribose 1-diphosphate
in the presence of phosphate, pH 7.5, 37°C
2.3 - 48
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant enzymes
4.5
5-phospho-alpha-D-ribose 1-diphosphate
-
-
4.5
5-phospho-alpha-D-ribose 1-diphosphate
-
pncB gene, in the uncoupled reaction
0.0015
nicotinate
-
pncB gene, in the coupled reaction
0.29
nicotinate
-
pncB gene, in the uncoupled reaction
0.33 - 0.4
nicotinate
-
mutant enzymes
0.0127
nicotinic acid
+/-3.6 microM, in presence of 1 mM NAD+, 80 ng enzyme, 10-70 microM nicotinamide, 0.3 mM PRPP, 30 min, 37°C, TLC-based quantification
0.0155
nicotinic acid
+/-3.4 microM, 80 ng enzyme, 10-70 microM nicotinamide, 0.3 mM PRPP, 30 min, 37°C, TLC-based quantification
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.36
5-phospho-alpha-D-ribose 1-diphosphate
in the presence of phosphate, pH 7.5, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.42
5-phospho-alpha-D-ribose 1-diphosphate
in the presence of phosphate, pH 7.5, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0169
+/-0.006 micromol/min/mg, with respect to nicotinic acid, in presence of 1 mM NAD+, 80 ng enzyme, 10-70 microM nicotinamide, 0.3 mM PRPP, 30 min, 37°C, TLC-based quantification
0.0186
+/-0.006 micromol/min/mg, with respect to nicotinic acid, 80 ng enzyme, 10-70 microM nicotinamide, 0.3 mM PRPP, 30 min, 37°C, TLC-based quantification
0.0226
+/-0.0016 micromol/min/mg, with respect to 5-phospho-alpha-D-ribose 1-diphosphate, in presence of 1 mM NAD+, 20 ng enzyme, 40 microM nicotinamide, 0.14-1 microM PRPP, 15 min, 37°C, TLC-based quantification
0.0236
+/-0.0015 micromol/min/mg, with respect to 5-phospho-alpha-D-ribose 1-diphosphate, 20 ng enzyme, 40 microM nicotinamide, 0.14-1 microM PRPP, 15 min, 37°C, TLC-based quantification
0.08
-
recombinant enzyme from Escherichia coli strain BA203, pH and temperature not specified in the publication
0.7
0.74
-
recombinant enzyme from Escherichia coli strain BA204, pH and temperature not specified in the publication
1.01
10.54
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
18.74
recombinant enzyme from Escherichia coli strain BA016, 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
0.7
-
recombinant enzyme from Escherichia coli strain BA002, 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
1.01
recombinant enzyme from Escherichia coli strain BA015, 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
10.54
recombinant enzyme from Escherichia coli strain BA014, pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8
-
about half-maximal activity at pH 5.5 and about 85% of maximal activity at pH 8
additional information
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene NPT1 at ocus YOR209C, eukaryotic type II enzyme
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
very low protein expression level (mouse polyclonal anti-human NAPRT antibody) and enzymatic activity (TLC)
brenda
additional information
1.9 kb mRNA detected by Northern blot analysis, moderate expression
brenda
-
1.9 kb mRNA detected by Northern blot analysis, moderate expression
-
brenda
exogenously added nicotinic acid (1-10 microM) leads to increase in basal total NAD++ level (revealed by ESI-MS) in a dose-dependent manner and to NaAD+ accumulation which are reduced by siRNA-based knock-down of endogenous NAPRT, knock-down does not affect basal NAD++ levels (503 +/-104 microM) in absence of exogenous nicotinic acid, exogenously added nicotinic acid decreases oxidative cytotoxicity (by 30-50 microM hydrogen peroxide) through elevated NAD+ levels mediated by NAPRT activity as revealed by siRNA-based knock-down of NAPRT
brenda
detected by Western blot using mouse polyclonal anti-human NAPRT antibody, robust endogenous activity
brenda
detected by Western blot using mouse polyclonal anti-human NAPRT antibody, robust endogenous activity
brenda
additional information
-
gene is ubiquitously expressed at the mRNA level in all normal human tissues tested. No expression MKN-28 cell
brenda
additional information
-
distribution in rat tissues: trace activities in brain, lung or stomach, not in thigh muscle, testis or serum
brenda
additional information
protein not detectable in small intestine
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
when overexpressed in Hep-G2 cells and detected by mouse polyclonal anti-human NAPRT antibody
brenda
subcellular fractionation, revealed by Western blot and activity measurements
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
both NAPRT and nicotinamide phosphoribosyltransferase NAMPT increase intracellular NAD+ levels. NAPRT silencing reduces energy status, protein synthesis, and cell size in ovarian and pancreatic cancer cells. NAPRT silencing sensitizes cells to NAMPT inhibitors both in vitro and in vivo
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
non-denaturing polyacrylamide gel electrophoresis of purified recombinant NAPRT in active state as controlled by applying gel slice to TLC-based activity assay with 50 microM nicotinic acid + 0.3 mM PRPP, 3 h, 37°C
43000
45000
45530
predicted from DNA sequence
51000
52000
overexpressed, His-tagged NAPRT in Hep-G2 cells detected in Western blot using mouse polyclonal anti-human NAPRT antibody
55000
2 * 55000, non-denaturing polyacrylamide gel electrophoresis of purified recombinant NAPRT in active state
43000
6 * 43000, (alphabeta)3, SDS-PAGE and crystal structure analysis
51000
endogenous NAPRT detected in Western blot using mouse polyclonal anti-human NAPRT antibody
51000
endogenous NAPRT detected in Western blot using mouse polyclonal anti-human NAPRT antibody
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
6 * 43000, (alphabeta)3, SDS-PAGE and crystal structure analysis
homodimer
2 * 55000, non-denaturing polyacrylamide gel electrophoresis of purified recombinant NAPRT in active state
monomer
additional information
additional information
enzyme monomer consists of 3 dimeric domains: an N-terminal alpha + beta domain, a central alpha/beta domain, and a C-terminal domain containing an unique zinc finger
additional information
-
enzyme monomer consists of 3 dimeric domains: an N-terminal alpha + beta domain, a central alpha/beta domain, and a C-terminal domain containing an unique zinc finger
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by molecular replacement at a resolution of 2.9 A, in its ligand-free form. The enzyme consists of two domains and functions as a dimer with the active site located at the interface of the monomers. NaPRTase acks a tunnel that, in nicotinamide phosphoribosyltransferase EC 2.4.2.12, represents the binding site of inhibitor FK866
recombinant selenomethionine-labeled enzyme, 10-30 mg/ml, in 10 mM Tris, pH 7.8, 150 mM NaCl, nanodroplet vapour diffusion method, 4°C, reservoir solution contains 6-16% PEG 5000 monomethyl ether, 0.06 M MES, and 0.04 M NaMES, pH 6.0, usage of 15-20% ethylene glycol as cryoprotectant, X-ray structure determination and analysis at 1.75 A resolution
recombinant detagged wild-type and selenomethionine-labeled enzymes, hanging drop vapour diffusion method, room temperature, 0.001 ml protein solution mixed with equal volume of well solution containing 0.2 M ammonium acetate, 0.1 M Tris-HCl, pH 8.5, 45% 2-methyl-2,4-pentanediol, 1 week, crystallization condition screening using sitting drop vapour diffusion at room temperature, iridium complexed, X-ray diffraction structure determination and analysis at 2.8 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H213A
P21L
mutation identified in a strain with early leaf sensescence, mutation causes the expression of the gene at the transcriptional level to decline by 40% in fully expanded leaves. Leaf nicotinate and nicotinamide contents are elevated, while NAD levels are reduced. Leaf tissue of P21L exhibits significant DNA fragmentation and H2O2 accumulation, along with up-regulation of genes associated with senescence. The mutant also shows reduced expression of SIR2-like genes SRT1 and SRT2 and increased acetylation of histone H3K9
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
5 min: 95% loss of activity, MgATP2-, Mg-phosphoribose diphosphate, ATP, GTP or nicotinic acid protect, with 27%, 37%, 52%, 54% or 61% loss of activity, respectively. 10 min: 97% loss of activity, MgATP2-, Mg-5-phospho-alpha-D-ribose 1-diphosphate, ATP, GTP or nicotinic acid protect, with 43%, 52%, 60%, 63% or 69% loss of activity, respectively
additional information
additional information
-
thermostability of the enzyme is increased by ATP and 5-phospho-alpha-D-ribose 1-diphosphate
additional information
thermostability of the enzyme is increased by ATP and 5-phospho-alpha-D-ribose 1-diphosphate
additional information
thermostability of the enzyme is increased by ATP and 5-phospho-alpha-D-ribose 1-diphosphate
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
50% activity recovered at salt concentrations of 50 mM, inactivation with salt concentrations below 20 mM, 20-35% glycerol partially protects
-
dialysis against 50 mM Tris-HCl buffer at pH 7.3 in the absence of potassium phosphate, significant loss of activity
first order activity loss in the presence of 1/200 trypsin/enzyme
-
glycerol, 20-35%, stabilizes during dialysis against low buffer concentrations, more highly purified preparations require higher glycerol concentrations
-
rapidly inactivates the ATPase and nicotinic acid mononucleotide synthesis activities with cleavages at Arg-384 and Lys-374, ATP and 5-phospho-alpha-D-ribose 1-diphosphate increase the t1/2 for inactivation 8fold and 4fold, respectively, and 32fold, together
-
sensitive to trypsin, partial proteolysis, 4fold increase in t1/2 for inactivation in the presence of 1 mM MgATP2-
-
dialysis against 50 mM Tris-HCl buffer at pH 7.3 in the absence of potassium phosphate, significant loss of activity
-
dialysis against 50 mM Tris-HCl buffer at pH 7.3 in the absence of potassium phosphate, significant loss of activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70ºC, no significantly decreased activity for up to 3 years, no significantly decreased after 8 years
-
4ºC, as 70% saturated ammonium sulfate suspensions in 200 mM phosphate buffer, pH 8, 10% glycerol and 5 mM DTT
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium hydroxide precipitation, chromatography on DEAE-Sephadex, Sephacryl and phenyl-Sepharose
-
ammonium sulfate fractionation, chromatography on DEAE-cellulose, chromatography on Sephadex, affinity column chromatography and hydroxylapatite column chromatography, 30000fold purified
-
bacteria disruption by alumina grinding, protamine sulfate precipitation and chromatography on DEAE-cellulose
-
bacterial suspension disruption and centrifugation, chromatography on Q-Sepharose and phenyl-Sepharose
-
bacterial suspension disruption and centrifugation, chromatography on Sephadex-G, DEAE-Toyopearl, Cibacron Blue and Sephacryl gel filtration
-
extraction, ammonium sulfate fractionation, chromatography on DEAE-cellulose and hydroxylapatite, 1000fold purified
-
extraction, fractionation chromatography on phosphocellulose, hydroxyapatite, blue Sephadex and DEAE-cellulose
-
partial, extraction, ammonium sulfate fractionation and chromatography on DEAE-cellulose, 60fold purified
-
recombinant N-terminally tagged selenomethionine-labeled enzyme variant from Escherichia coli strain DL41
recombinant tagged wild-type and selenomethionine-labeled fusion enzymes from Escherichia coli to homogeneity by high-trap chelating nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA fragment (as probe for Northern blot analysis) reverse transcribed from tissue total RNA using sense primer 5â-GTG AGG TGA ATG TCA TTG GC-3â and antisense primer 5â-ACA GTG CGA CCG GAT ACA CT-3â
expression of N-terminally tagged enzyme as selenomethionine-labeled variant in Escherichia coli strain DL41
expression of pncB gene on a multicopy pUC19 plasmid in Salmonella typhimurium
-
expression of the enzyme as His6-tagged-maltose-binding fusion protein containing a tobacco etch virus protease cleavage site in Escherichia coli strain BL21(DE3) for the wild-type, and in strain B834(DE3) for a selenomethionine-labeled variant
in pET22b and pET15b for expression in Escherichia coli BL21 (DE3) as fusion protein with C-terminal or N-terminal hexa-His-tag, respectively, in pcDNA3His(6) for expression in eukaryotic cell culture, specific siRNAs against nt829-1634 and nt445-935 for transfection into HEK-293 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
presence of more than one NAPRT transcript in most tissues, all with identical 3' end sequence. Some NAPRT transcripts appear to be tissuespecific. Brain shows the highest number of alternative transcripts. Several modulators of the NAPRT gene expression are involved, i.e. mutations in transcription factor binding sites, promoter methylation and alternative splicing
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
NAPRT is amplified and overexpressed in a subset of common types of cancer, including ovarian cancer, where NAPRT expression correlates with a BRCAness gene expression signature. Both NAPRT and nicotinamide phosphoribosyltransferase NAMPT increase intracellular NAD+ levels. NAPRT silencing reduces energy status, protein synthesis, and cell size in ovarian and pancreatic cancer cells. NAPRT silencing sensitizes cells to NAMPT inhibitors both in vitro and in vivo. Reducing NAPRT levels in a BRCA2-deficient cancer cell line exacerbates DNA damage in response to chemotherapeutics
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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
brenda
Imsande, J.; Handler, P.
Biosynthesis of diphosphopyridine nucleotide. III. Nicotinic acid mononucleotide pyrophosphorylase
J. Biol. Chem.
236
525-530
1961
Bos taurus
brenda
Kosaka, A.; Spivey, H.O.; Gholson, R.K.
Nicotinate phosphoribosyltransferase of yeast. Purification and properties
J. Biol. Chem.
246
3277-3283
1971
Saccharomyces cerevisiae
brenda
Gaut, Z.N.; Solomon, H.M.
Inhibition of nicotinate phosphoribosyltransferase in human platelet lysate by nicotinic acid analogs
Biochem. Pharmacol.
20
2903-2906
1971
Homo sapiens
brenda
Niedel, J.; Dietrich, L.S.
Nicotinate phosphoribosyltransferase of human erythrocytes. Purification and properties
J. Biol. Chem.
248
3500-3505
1973
Homo sapiens
brenda
Hanna, L.S.; Hess, S.L.; Sloan, D.L.
Kinetic analysis of nicotinate phosphoribosyltransferase from yeast using high pressure liquid chromatography
J. Biol. Chem.
258
9745-9754
1983
Saccharomyces cerevisiae
brenda
Hayakawa, T.; Shibata, K.; Iwai, K.
Purification and some properties of nicotinate phosphoribosyltransferase from hog liver
Agric. Biol. Chem.
48
445-453
1984
Rattus norvegicus, Sus scrofa, Rattus norvegicus male Wistar
-
brenda
Hayakawa, T.; Shibata, K.; Iwai, K.
Nicotinate phosphoribosyltransferase from hog liver: regulatory effect of ATP at a physiological concentrations of 5-phosphoribosyl-1-pyrophosphte
Agric. Biol. Chem.
48
455-460
1984
Rattus norvegicus, Sus scrofa
-
brenda
Kosaka, A.; Spivey, H.O.; Gholson, R.K.
Yeast nicotinic acid phosphoribosyltransferase. Studies of reaction paths, phosphoenzyme, and Mg2+ effects
Arch. Biochem. Biophys.
179
334-341
1977
Saccharomyces cerevisiae
brenda
Imsande, J.
A cross-linked control system. I. Properties of a triphosphate-dependent nicotinic acid mononucleotide pyrophosphorylase from Bacillus subtilis
Biochim. Biophys. Acta
85
255-264
1964
Bacillus subtilis, Bacillus subtilis SB19
brenda
Gross, J.W.; Rajavel, M.; Grubmeyer, C.
Kinetic mechanism of nicotinic acid phosphoribosyltransferase. Implications for energy coupling
Biochemistry
37
4189-4199
1998
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Rajavel, M.; Lalo, D.; Gross, J.W.; Grubmeyer, C.
Conversion of a cosubstrate to an inhibitor. Phosphorylation mutants of nicotinic acid phosphoribosyltransferase
Biochemistry
37
4181-4188
1998
Salmonella enterica subsp. enterica serovar Typhimurium, Saccharomyces cerevisiae (P39683), Saccharomyces cerevisiae
brenda
Rajavel, M.; Gross, J.W.; Segura, E.; Moore, W.T.; Grubmeyer, C.
Limited proteolysis of Salmonella typhimurium nicotinic acid phosphoribosyltransferase reveals ATP-linked conformational change
Biochemistry
35
3909-3916
1996
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Vinitsky, A.; Grubmeyer, C.
A new paradigm for biochemical energy coupling. Salmonella typhimurium nicotinate phosphoribosyltransferase
J. Biol. Chem.
268
26004-26010
1993
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Pescaglini, M.; Micheli, V.; Simmonds, H.A.; Rocchigiani, M.; Pompucci, G.
Nicotinic acid phosphoribosyltransferase activity in human erythtocytes: studies using a niw HPLC method
Clin. Chim. Acta
229
15-25
1994
Homo sapiens
brenda
Grubmeyer, C.T.; Gross, J.W.; Rajavel, M.
Energy coupling through molecular discrimination: nicotinate phosphoribosyltransferase
Methods Enzymol.
308
28-48
1999
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P39683), Salmonella enterica subsp. enterica serovar Typhimurium (P22253), Mycobacterium tuberculosis (P9WJW5), Mycobacterium tuberculosis H37Rv (P9WJW5)
brenda
Shin, D.H.; Oganesyan, N.; Jancarik, J.; Yokota, H.; Kim, R.; Kim, S.H.
Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum
J. Biol. Chem.
280
18326-18335
2005
Thermoplasma acidophilum (Q9HJ28), Thermoplasma acidophilum
brenda
Chappie, J.S.; Canaves, J.M.; Han, G.W.; Rife, C.L.; Xu, Q.; Stevens, R.C.
The structure of a eukaryotic nicotinic acid phosphoribosyltransferase reveals structural heterogeneity among type II PRTases
Structure
13
1385-1396
2005
Saccharomyces cerevisiae (P39683), Saccharomyces cerevisiae
brenda
Hara, N.; Yamada, K.; Shibata, T.; Osago, H.; Hashimoto, T.; Tsuchiya, M.
Elevation of cellular NAD levels by nicotinic acid and involvement of nicotinic acid phosphoribosyltransferase in human cells
J. Biol. Chem.
282
24574-24582
2007
Mus musculus, Mus musculus (Q8CC86), Rattus norvegicus (Q6XQN1), Homo sapiens (Q6XQN6), Homo sapiens, Mus musculus BALB/c (Q8CC86)
brenda
Ashihara, H.; Stasolla, C.; Yin, Y.; Loukanina, N.; Thorpe, T.A.
De novo and salvage biosynthetic pathways of pyridine nucleotides and nicotinic acid conjugates in cultured plant cells
Plant Sci.
169
107-114
2005
Catharanthus roseus, Picea glauca
brenda
Galassi, L.; Di Stefano, M.; Brunetti, L.; Orsomando, G.; Amici, A.; Ruggieri, S.; Magni, G.
Characterization of human nicotinate phosphoribosyltransferase: Kinetic studies, structure prediction and functional analysis by site-directed mutagenesis
Biochimie
94
300-309
2012
Homo sapiens (Q6XQN6), Homo sapiens
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.
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Escherichia coli (P18133), Escherichia coli
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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
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Escherichia coli
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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.
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Escherichia coli
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Piacente, F.; Caffa, I.; Ravera, S.; Sociali, G.; Passalacqua, M.; Vellone, V.G.; Becherini, P.; Reverberi, D.; Monacelli, F.; Ballestrero, A.; Odetti, P.; Cagnetta, A.; Cea, M.; Nahimana, A.; Duchosal, M.; Bruzzone, S.; Nencioni, A.
Nicotinic acid phosphoribosyltransferase regulates cancer cell metabolism, susceptibility to NAMPT inhibitors, and DNA repair
Cancer Res.
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Homo sapiens (Q6XQN6)
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Amici, A.; Grolla, A.A.; Del Grosso, E.; Bellini, R.; Bianchi, M.; Travelli, C.; Garavaglia, S.; Sorci, L.; Raffaelli, N.; Ruggieri, S.; Genazzani, A.A.; Orsomando, G.
Synthesis and degradation of adenosine 5-tetraphosphate by nicotinamide and nicotinate phosphoribosyltransferases
Cell Chem. Biol.
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Homo sapiens
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Marletta, A.S.; Massarotti, A.; Orsomando, G.; Magni, G.; Rizzi, M.; Garavaglia, S.
Crystal structure of human nicotinic acid phosphoribosyltransferase
FEBS open bio
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Homo sapiens (Q6XQN6), Homo sapiens
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Duarte-Pereira, S.; Pereira-Castro, I.; Silva, S.S.; Correia, M.G.; Neto, C.; da Costa, L.T.; Amorim, A.; Silva, R.M.
Extensive regulation of nicotinate phosphoribosyltransferase (NAPRT) expression in human tissues and tumors
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Homo sapiens
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Wu, L.; Ren, D.; Hu, S.; Li, G.; Dong, G.; Jiang, L.; Hu, X.; Ye, W.; Cui, Y.; Zhu, L.; Hu, J.; Zhang, G.; Gao, Z.; Zeng, D.; Qian, Q.; Guo, L.
Down-regulation of a nicotinate phosphoribosyltransferase gene, OsNaPRT1, leads to withered leaf tips
Plant Physiol.
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Oryza sativa Japonica Group (Q851M0)
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