Information on EC 2.4.2.12 - nicotinamide phosphoribosyltransferase

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

EC NUMBER
COMMENTARY hide
2.4.2.12
-
RECOMMENDED NAME
GeneOntology No.
nicotinamide phosphoribosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
nicotinamide D-ribonucleotide + diphosphate = nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
NAD biosynthesis III
-
-
Nicotinate and nicotinamide metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
nicotinamide-D-ribonucleotide:diphosphate phospho-alpha-D-ribosyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9030-27-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Picea glauca
suspension cultured cells
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
implicated in the pathogenesis of a number of human diseases or conditions such as acute lung injury, aging, atherosclerosis, cancer, diabetes, rheumatoid arthritis and sepsis
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + ATP
ATP + ADP
show the reaction diagram
-
isotope exchange reaction (in presence of radiolabeled ADP and ATP but in absence of other reactants, meaning without NMN synthesis) requires high-energy phosphorylated NAMPT
-
-
r
ATP + H2O
ADP + phosphate
show the reaction diagram
-
DELTAG = -7.3, in presence of NAMPT slow steady-state reaction after initial burst, ATPase activity in absence of other substrates, but can be modulated by addition of single substrates and mixtures
-
-
?
ATP + NAMPT
ADP + phospho-NAMPT
show the reaction diagram
-
autophosphorylation (DELTAG = 1.9 kcal/mol, Keq = 0.047) is unfavourable and appears as initial burst of ADP generation
at 2.5 mM ATP and 46 microM NAMPT 77% of NAMPT is phosphorylated (proposed: His247 phospho-NAMPT), hydrolysis of phospho-NAMPT at 0.8/min, active phosphorylated NAMPT species neither isolated nor characterized yet
-
r
nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate
nicotinamide D-ribonucleotide + diphosphate
show the reaction diagram
nicotinamide + 5-phosphoribosyl 1-diphosphate
nicotinamide mononucleotide + diphosphate
show the reaction diagram
nicotinamide + alpha-D-5-phosphoribosyl 1-diphosphate
nicotinamide mononucleotide + diphosphate
show the reaction diagram
nicotinamide + alpha-D-5-phosphoribosyl 1-diphosphate + ATP + H2O
nicotinamide mononucleotide + diphosphate + ADP + phosphate
show the reaction diagram
-
DELTAG = -1.0 kcal/mol, Keq = 5.0, reversion of the preestablished equilibrium in a non-ATP-coupled reaction, thermodynamic switch of the product-to-substrate ratio towards NMN production compared to the non-ATP-coupled reaction with an energy difference of -2.1 kcal/mol (meaning only 2.1 kcal/mol of 7.3 kcal/mol of the energy from ATP hydrolysis coupled to NMN formation), formation or hydrolysis of high-energy phosphorylated NAMPT may be rate limiting for overall ATP-coupled NMN synthesis
in presence of 2-2.5 mM ATP: 1 mol ADP per NMN formed (stoichiometric coupling ratio, R = 1), under optimal conditions (2 microM nicotinamide, 100 microM PRPP, 2.5 mM ATP, 5 mM Mg2+): R increases linearly with increasing diphosphate concentration
-
r
nicotinamide + alpha-D-5-phosphoribosyl-1-diphosphate
nicotinamide mononucleotide + diphosphate
show the reaction diagram
-
-
-
-
r
nicotinamide + alpha-D-5-phosphoribosyl-1-diphosphate
nicotinamide mononucleotide + inorganic diphosphate
show the reaction diagram
-
-
-
r
nictoinamide + alpha-D-5-phosphoribosyl 1-diphosphate
nicotinamide mononucleotide + diphosphate
show the reaction diagram
-
whole cell lysates incubated with 5 microM [carbonyl-14C]nicotinamide + 0.5 mM alpha-D-5-phosphoribosyl-1-diphosphate at pH 8.8
produced NMN quantified by scintillation counting
-
r
phospho-NAMPT + H2O
NAMPT + phosphate
show the reaction diagram
-
DELTAG = -9.2 kcal/mol
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nicotinamide + 5-phospho-alpha-D-ribose 1-diphosphate
nicotinamide D-ribonucleotide + diphosphate
show the reaction diagram
nicotinamide + alpha-D-5-phosphoribosyl 1-diphosphate
nicotinamide mononucleotide + diphosphate
show the reaction diagram
nicotinamide + alpha-D-5-phosphoribosyl-1-diphosphate
nicotinamide mononucleotide + diphosphate
show the reaction diagram
-
-
-
-
r
nicotinamide + alpha-D-5-phosphoribosyl-1-diphosphate
nicotinamide mononucleotide + inorganic diphosphate
show the reaction diagram
Q80Z29
-
-
-
r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(4',5,7-trihydroxyflavone)-(3'->8)-(4',5,7-trihydroxyflavone)
-
-
(4',7-dimethoxy-5-hydroxyflavone)-(3'->8)-(4',7-dimethoxy-5-hydroxyflavone)
-
-
3-acetylpyridine
-
weak, kinetics
3-acetylpyridine adenine dinucleotide
-
kinetics
5-Fluoronicotinamide
-
weak, kinetics
5P-DADMe-NMN
-
poor, competitive inhibitor of non-ATP and ATP coupled NMN synthesis with respect to PRPP and nicotinamide, 3-fold increased binding in presence of ATP
6-aminonicotinamide
-
weak, kinetics
alpha-D-5-phosphoribosyl 1-diphosphate
-
inhibits ATPase activity at 1 mM concentration, nearly complete inhibition of ADP-ATP exchange at 100 microM
Alpha-NAD+
-
weak
APO866
CHS-828
-
competitive inhibitor
FK-866
gallotanine
-
i.e. (2R,3S,5R,6S)-tetrahydro-2H-pyran-2,3,4,5,6-pentaylpentakis(oxycarbonyl-5,6-dihydroxybenzene-3,1-diyl) pentakis(3,4,5-trihydroxybenzoate)
GMX1777
hypoxanthine
-
phosphorolysis
N-biphenyl-2-yl-8-(4-pyridin-3-yl-1H-1,2,3-triazol-1-yl)octanamide
-
displays an IC50 for cytotoxicity in vitro of 3.8 nM and an IC50 for NAD depletion of 3.0 nM. Compound induces autophagic cell death
-
NADPH
-
weak
nicotinamide
-
substrate inhibition
nicotinamide hypoxanthine dinucleotide
-
-
nicotinamide mononucleotide
-
kinetics
nicotinamide mononucleotide-H2
-
strong, kinetics
nicotinamide riboside
-
kinetics
nicotinate adenine dinucleotide
Thionicotinamide
-
weak, kinetics
Thionicotinamide adenine dinucleotide
-
-
TP201565
-
competitive inhibitor
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphosphate
-
enhanced ATPase activity
EDTA
-
50% activation, 1 mM
nicotinamide
-
enhanced ATPase activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0038 - 0.00537
5-phospho-alpha-D-ribose 1-diphosphate
0.00051 - 0.0232
5-phosphoribosyl 1-diphosphate
0.44
ADP
-
+/-0.05 mM, ADP-ATP radiolabel exchange in absence of other reactants
0.00063 - 0.0117
alpha-D-5-phosphoribosyl 1-diphosphate
2.2 - 7.4
ATP
0.000005 - 100
nicotinamide
0.18
phosphate
-
+/-0.02 mM, pH 7.5, 88 nM NAMPT, HPLC-based quantification
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003 - 0.0433
ATP
0.00137 - 0.02
nicotinamide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00016 - 0.0071
5P-DADMe-NMN
0.0003 - 0.0004
FK866
0.00014 - 0.0021
NAD+
0.00022 - 0.0032
NADH
0.00025 - 0.003
nicotinamide
additional information
ATP
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0066
(4',5,7-trihydroxyflavone)-(3'->8)-(4',5,7-trihydroxyflavone)
Mus musculus
-
pH 7.5, 37C
0.0175
(4',7-dimethoxy-5-hydroxyflavone)-(3'->8)-(4',7-dimethoxy-5-hydroxyflavone)
Mus musculus
-
pH 7.5, 37C
0.0000009 - 0.008585
FK-866
0.0013
gallotanine
Mus musculus
-
i.e. (2R,3S,5R,6S)-tetrahydro-2H-pyran-2,3,4,5,6-pentaylpentakis(oxycarbonyl-5,6-dihydroxybenzene-3,1-diyl) pentakis(3,4,5-trihydroxybenzoate), pH 7.5, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000225
-
-
0.00213
-
at 0.001 mM 5-phosphoribosyl 1-diphosphate, without ATP, pH 7.5, 37C
0.0259
-
at 0.050 mM 5-phosphoribosyl 1-diphosphate, without ATP, pH 7.5, 37C; substrate 5-phosphoribosyl 1-diphosphate, without ATP, pH 7.5, 37C
0.0393
-
substrate nicotinamide, without ATP, pH 7.5, 37C
0.0397
-
substrate nicotinamide, with 1 mM ATP, pH 7.5, 37C
0.0481
-
at 0.050 mM 5-phosphoribosyl 1-diphosphate, with 1 mM ATP, pH 7.5, 37C
0.0704
-
at 0.001 mM 5-phosphoribosyl 1-diphosphate, with 1 mM ATP, pH 7.5, 37C
0.0741
-
substrate 5-phosphoribosyl 1-diphosphate, with 1 mM ATP, pH 7.5, 37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7.6
-
-
7.4
-
assay at
7.5
-
for both, NMN synthesis and ATP hydrolysis activity
8.5 - 9
-
assay at pH 8.8. where NAD glycohydrolase is not active
8.8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1 - 8.5
-
about half-maximal activity at pH 6.1 and pH 8.5
6.5 - 8.5
-
preincubation of NAMPT for 1 h at 25 C and various pH values in presence of 1 microM nicotinamide, 1 mM ATP, 30 nM NAMPT (NAMPT reaction started with 200 microM alpha-D-5-phosphoribosyl 1-diphosphate) or 2 mM ATP, 0.75 microM NAMPT (ATP hydrolysis)
7.8 - 9.2
-
about half-maximal activity at pH 7.8 and about 80% of maximal activity at pH 9.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.69
-
theoretic value
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
primary SMC culture, Nampt expression declines as SMC approach senescence as detected by immunoblotting using rabbit-polyclonal anti-human Nampt/Pre-B-cell colony-enhancing factor antibody; primary SMC culture stably expressing Nampt, 2.1 +/-0.3 additional population doublings constituting 34 +/-4% lifespan prolongation
Manually annotated by BRENDA team
similar mRNA expression levels in (fa/fa) Zucker rats (obese) compared to lean Zucker rats (control) as well as in cafeteria diet-fed Wistar rats (diet-induced obesity) compared to standard chow diet-fed Wistar rats (control)
Manually annotated by BRENDA team
positive staining in blood vessels from arthritic joints as revealed by immunohistochemistry using rat monoclonal anti-murine NAMPT antibody
Manually annotated by BRENDA team
inguinal white adipose tissue
Manually annotated by BRENDA team
-
release of NAMPT enzyme into the cell culture supernatant occurs constitutively. In primary hepatocytes, secretion within 24 h is far higher than the cellular content, but is neither influenced by inhibitors of secretion nor by glucose, insulin or TNFalpha. In primary human hepatocytes, secreted NAMPT is less active than intracellular enzyme
Manually annotated by BRENDA team
-
SMC clonal line, Nampt expression declines as SMC approach senescence as detected by immunoblotting using rabbit-polyclonal anti-human Nampt/Pre-B-cell colony-enhancing factor antibody, 14 +/-3% of basal Nampt activity in presenescent SMC, direct relationship between Nampt activity and number of replication cycles preceeding senescence; SMC clonal line stably expressing Nampt, 7.1 +/-3.1 fold higher Nampt activity, 6.3 +/-0.3 additional population doublings constituting 71 +/-7% lifespan prolongation, 19 +/-2% reduction in number of senescent cells at passage 37 compared to control HITC6 cells is dependent on SIRT1 activity and associated with increased p53 degradation and protection against oxidative cell damage as response to 150 microM hydrogen peroxide
Manually annotated by BRENDA team
massive expression in synoviocytes of the synovial lining layer, sub-intimal synovium and pannus in joints from mice with type II collagen induced arthritis (CIA) compared to non-arthritic naive DBA/1 mice as revealed by immunohistochemistry using rat monoclonal anti-murine NAMPT antibody, some positive staining in chondrocytes from normal and arthritic joints and in blood vessels and inflammatory cells from arthritic joints
Manually annotated by BRENDA team
-
leukemia cell line
Manually annotated by BRENDA team
-
isolated from total PBMCs from blood from healthy individuals
Manually annotated by BRENDA team
-
from blood from healthy individuals
Manually annotated by BRENDA team
elevated levels in mice with type II collagen induced arthritis (CIA) compared to non-arthritic naive DBA/1 mice as revealed by ELISA using a mouse visfatin/PBEF ELISA kit
Manually annotated by BRENDA team
-
PBMC from blood from healthy individuals
Manually annotated by BRENDA team
(PEC) isolated from naive C57BL/6 mice of from lipopolysaccharide-treated mice
Manually annotated by BRENDA team
-
from individual with Hutchison-Gilford progeria syndrome associated with premature atherosclerosis, cell lifespan extension upon Nampt overexpression
Manually annotated by BRENDA team
similar mRNA expression levels in mesenteric, retroperitoneal and epididymal WAT depots of (fa/fa) Zucker rats (obese) compared to lean Zucker rats (control)
Manually annotated by BRENDA team
lean Wistar rats: mRNA expression levels are maximal in mesenteric WAT (2.01 +/-0.08) followed by inguinal (1.23 +/-0.15), epididymal (0.88 +/-0.13), and retroperitoneal (0.79 +/-0.07) WAT; lean Zucker rats: mRNA expression levels are similar in subcutaneous (inguinal, 1.18 +/-0.33) and visceral (mesenteric (0.99 +/-0.15), retroperitoneal (0.56 +/-0.10), epididymal (1.17 +/-0.14)) WAT; mesenteric, significantly decreased mRNA expression level in cafeteria diet-fed Wistar rats (diet-induced obesity) compared to standard chow diet-fed Wistar rats (control); significantly reduced mRNA expression level in (fa/fa) Zucker rats (obese) compared to lean Zucker rats (control) and in cafeteria diet-fed Wistar rats (diet-induced obesity) compared to standard chow diet-fed Wistar rats (control)
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
-
gel filtration, part of the enzyme in supernatant of HepG2 cells
120000
-
gel filtration, most of the enzyme in supernatant of HepG2 cells
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
-
1 * 55000, SDS-PAGE, plus some dimer, supernatant of HepG2 cells
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo enzyme, diffraction of third crystals at 2 A resolution at -174C, crystals belong to space group P2(1) with unit-cell parameters a = 60.56 A, b = 106.40 A, c =82.78 A, beta = 96.50, technique: 1 microlitre of 10 mg/ml protein solution to 1 microlitre reservoir solution (38% pentaerytritol propoxylate (5/4 PO/OH) and 200 mM KCl pH 9) one week at 4C, generation of first crystals by hanging-drop vapour diffusion (Index HT screening kit), generation of second crystals by microseeding: reservoir solution contained crushed first crystals, generation of third crystals by Repeated Seeding Technique: reservoir solution contained crushed second crystals
-
crystal structures at up to 2.1 A resolution of NMPRTase, alone and in complex with the reaction product nicotinamide mononucleotide or the inhibitor FK866. Crystals of the selenomethionyl free enzyme of human NMPRTase (F132M I151M double mutant) are grown with the sitting drop vapor diffusion method at 22C. Crystals of wild-type human NMPRTase in complex with NMN are obtained at 22C by sitting drop vapor diffusion
-
crystal structures of the enzyme in the free form and bound to nicotinamide and 5-phospho-alpha-D-ribose 1-diphosphate at the resolution of 2.0 A to 2.2 A are essentially identical to that of the complex with nicotinamide mononucleotide, except for some variations that can facilitate the substitution reaction by fixing the nucleophile and the leaving group for the requisite inversion of configuration at the C1-carbon of the ribose ring. In the active site near the C1-atom of the bound 5-phospho-alpha-D-ribose 1-diphosphate or nicotinamide mononucleotide, there is neither negatively charged group nor waterproof environment necessary to support the feasibility of a ribo-oxocarbocation intermediate inherent in the SN1 mechanism
-
crystallization of recombinant human NMPRTase in the free form, sitting-drop vapour-diffusion method, hanging-drop vapour-diffusion method, crystal quality is improved by successive use of the microseeding technique. The resultant crystals diffract to 2.0 A resolution. These crystals belongs to space group P2(1), with unit-cell parameters a = 60.56, b = 106.40, c = 82.78 A
-
crystal structures at up to 2.1 A resolution of NMPRTase, alone and in complex with the reaction product nicotinamide mononucleotide or the inhibitor FK866. Crystals of wild-type murine NMPRTase free enzyme are obtained by sitting drop vapor diffusion at 4C
-
hanging drop vapor diffusion method, crystallization of apoenzyme and complex with either nicotinamide mononucleotide or the NAmPRTase inhibitor FK-866
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
preincubation of 30 nM NAMPT for 1 h at 25 C and various pH values, NMN synthesis: reaction started with 200 microM alpha-D-5-phosphoribosyl 1-diphosphate in presence of 1 microM nicotinamide, 1 mM ATP
690900
7 - 10
-
stable
489738
8.8
-
rapid inactivation below
489738
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
10 min, stable, heat treatment during purification
70
-
5 min, stable, heat treatment during purification
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin, glutathione, cysteine, DTT, EDTA, cystine or H2O2 does not stabilize during storage
-
freeze-thawing inactivates
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C to +20C, about 70% loss of activity overnight
-
-70C, in crude erythrocyte lysates, at least 30 days
-
-80C, crude, 4-6 months
-
4C, crude, inactivation overnight
-
storage at room temperature, 4C, or frozen, unstable upon
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography
-
immobilized metal ion affinity chromatography (Ni2+)
-
lysis of bacteria by French press, elution from Ni-NTA column by 100 and 200 mM imidazole, concentration and desalting, elution from HiLoad Superdex 200GP 26/60 column with 100 mM HEPES pH 7.5, 100 mM NaCl, 10 mM beta-mercaptoethanol, concentrated to 50-75 mg/ml, kept frozen
-
lysis of bacteria by ultrasonification in presence of 1 mM phenylmethylsulfonylfluorid (PMSF) and 1 mM dithiothreitol (DTT), ultracentrifugation, supernatant applied to glutathione Sepharose 4B beads and washed, cleavage of glutathione S-transferase (GST) tag by PreScission Protease, purification by gel-filtration chromatography in Tris-HCl pH 8.5, 150 mM NaCl, 1 mM DTT, concentration to 10 mg/ml by ultrafiltration on Microcon YM-10, stored at 4C
-
partial
partially frim K-562 leukemic cells
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a retroviral gene delivery system is used to generate human cells stably overexpressing Nampt. Introducing the Nampt gene into aging human SMCs delays senescence and substantially lengthened cell lifespan, together with enhanced resistance to oxidative stress; in pQCXIP-IHRES-PURO for retroviral delivery and stable overexpression in Phoenix-amphotropic retrovirus packaging cell line
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cDNA into pGEX6p1 for expression in Escherichia coli BL21 (DE) as glutathione S-transferase (GST) tagged fusion protein
-
chemically synthesised DNA (DNA 2.0) in pBAD DEST 49 for expression in Escherichia coli BL21 (DE3)-pLys
-
DNA sequence determination and analysis, phylogenetic analysis, expression of His-tagged enzyme and of enzyme fused to Sir2 in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIL
-
expressed in Escherichia coli Rosetta 2 (DE3)
-
expression in Escherichia coli
expression in Escherichia coli BL21
-
pre-B-cell colony enhancing factor
-
significant homology to human pre-B-cell colony enhancing factor
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of Nampt in the heart is significantly decreased by ischemia, ischemia/reperfusion and pressure overload. Downregulation of Nampt increases caspase 3 cleavage, cytochrome c release, and TUNEL-positive cells, which are inhibited in the presence of Bcl-xL, but do not increase hairpin 2positive cells, suggesting that endogenous Nampt negatively regulates apoptosis but not necrosis. Downregulation of Nampt also impairs autophagic flux
-
increased during macrophage differentiation
-
upon aging: enzyme level increases in serum but decreases in brain, decreases in cortex and hippocampus but remains unchanged in cerebellum and striatum in brain, and increases in microglia but likely decreases in neuron
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA D93
-
naturally occuring mutation in CHS-828 or APO866 resistant cell lines, about 20% of wild type aczivity
H191R
-
activity reduced by about 50%
H191R/K342R
-
naturally occuring mutation in APO866 resistant cell line
H191R/K342R/Q388R
-
naturally occuring mutation in TP201565 resistant cell line
H247A
-
active site residue, no detectable activity
H247E
-
active site residue, low activity
K342R
-
naturally occuring mutation, activity reduced by about 50%
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
inhibitor-soaking experiments
medicine
pharmacology
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