Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 3-acetyl-pyridine-NAD+
?
ATP + 3-pyridinealdehyde-NAD+
?
ATP + beta-nicotinate D-ribonucleotide
diphosphate + deamido-NAD+
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
ATP + nicotinate beta-D-ribonucleotide
diphosphate + deamido-NAD+
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
ATP + nicotinic acid mononucleotide
nicotinic acid adenine dinucleotide + diphosphate
ATP + nicotinic acid ribonucleotide
diphosphate + deamido-NAD+
-
-
-
?
ATP + NMN
diphosphate + NAD+
-
-
-
-
r
ATP + reduced nicotinamide nucleotide
diphosphate + NADH + H+
-
-
-
?
deoxy-ATP + nicotinamide ribonucleotide
?
deoxy-ATP + nicotinate ribonucleotide
?
NAD+ + diphosphate
ATP + nicotinamide nucleotide
-
-
-
-
?
nicotinate mononucleotide + ATP
nicotinate adenine dinucleotide + diphosphate
-
PreissHandler-dependent pathway
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
nicotinic acid mononucleotide + ATP
nicotinic acid dinucleotide + diphosphate
additional information
?
-
ATP + 3-acetyl-pyridine-NAD+
?
-
poor substrate
-
-
?
ATP + 3-acetyl-pyridine-NAD+
?
-
reaction at 76% the rate of nicotinamide ribonucleotide
-
-
?
ATP + 3-pyridinealdehyde-NAD+
?
-
poor substrate
-
-
?
ATP + 3-pyridinealdehyde-NAD+
?
-
reaction at 28% the rate of nicotinamide ribonucleotide
-
-
?
ATP + beta-nicotinate D-ribonucleotide
diphosphate + deamido-NAD+
-
-
-
?
ATP + beta-nicotinate D-ribonucleotide
diphosphate + deamido-NAD+
-
-
-
?
ATP + beta-nicotinate D-ribonucleotide
diphosphate + deamido-NAD+
-
-
-
?
ATP + beta-nicotinate D-ribonucleotide
diphosphate + deamido-NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide, reverse reaction at 17% the rate of deamido-NAD+-synthesis
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinate beta-D-ribonucleotide
diphosphate + deamido-NAD+
-
-
-
?
ATP + nicotinate beta-D-ribonucleotide
diphosphate + deamido-NAD+
-
-
-
?
ATP + nicotinate beta-D-ribonucleotide
diphosphate + deamido-NAD+
-
-
-
?
ATP + nicotinate beta-D-ribonucleotide
diphosphate + deamido-NAD+
-
-
-
?
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
-
-
-
?
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
NaMNAT is the penultimate enzyme in the biosynthesis of NAD+ and catalyzes the adenylation of nicotinic acid mononucleotide by ATP to form nicotinic acid adenine dinucleotide
-
-
?
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
-
-
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
-
best substrate
i.e. nicotinic acid adenine dinucleotide
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
-
i.e. nicotinate mononucleotide
i.e. nicotinic acid adenine dinucleotide
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
-
i.e. nicotinate mononucleotide
i.e. nicotinic acid adenine dinucleotide
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
-
-
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
-
i.e. nicotinate mononucleotide
i.e. nicotinic acid adenine dinucleotide
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
-
-
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
-
i.e. nicotinate mononucleotide
i.e. nicotinic acid adenine dinucleotide
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
-
reaction at 77% the rate of nicotinamide ribonucleotide
i.e. nicotinic acid adenine dinucleotide
r
ATP + nicotinic acid mononucleotide
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
-
r
ATP + nicotinic acid mononucleotide
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
-
r
ATP + nicotinic acid mononucleotide
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
-
r
ATP + nicotinic acid mononucleotide
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
-
r
deoxy-ATP + nicotinamide ribonucleotide
?
-
-
-
-
?
deoxy-ATP + nicotinamide ribonucleotide
?
-
-
-
-
?
deoxy-ATP + nicotinate ribonucleotide
?
-
-
-
-
?
deoxy-ATP + nicotinate ribonucleotide
?
-
-
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
activity observed with GTP, ITP
-
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
activity observed with dATP, ITP
-
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid dinucleotide + diphosphate
-
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid dinucleotide + diphosphate
-
-
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid dinucleotide + diphosphate
-
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid dinucleotide + diphosphate
-
-
-
?
additional information
?
-
bifunctional enzyme, that also shows nicotinamide-nucleotide adenylyltransferase activity, EC 2.7.7.1
-
-
?
additional information
?
-
-
bifunctional enzyme, additionally catalyzes the reaction with nicotinamide ribonucleotide, reaction of EC 2.7.7.1
-
-
-
additional information
?
-
additionally cataylzes the reaction of EC 2.7.7.1. No donors: ADP, AMP, TMP, GMP, CMP, UMP and IMP
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-(2,4-dimethylphenyl)-N-(4-([(5-methyl-3-isoxazolyl)amino]sulfonyl)phenyl)-4-quinolinecarboxamide
MIC80 values of 0.02-0.1 mM and above. The compounds show no inhibition of the human enzyme
2-(2,4-dimethylphenyl)-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]quinoline-4-carboxamide
-
2-(2,4-dimethylphenyl)-N-[4-[(5-methyl-1,2-oxazol-3-yl)sulfamoyl]phenyl]quinoline-4-carboxamide
-
2-(2-chlorophenyl)-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]quinoline-4-carboxamide
-
2-(4-bromophenyl)-N-[4-[(4-methylpyrimidin-2-yl)sulfamoyl]phenyl]quinoline-4-carboxamide
-
2-(furan-2-yl)-N-[3-(3,4,5,6-tetrahydropyridin-2-ylsulfamoyl)phenyl]quinoline-4-carboxamide
-
2-(furan-2-yl)-N-[3-methoxy-4-(morpholin-4-ylsulfonyl)phenyl]quinoline-4-carboxamide
-
2-(furan-2-yl)-N-[3-methyl-4-(morpholin-4-ylsulfonyl)phenyl]quinoline-4-carboxamide
-
2-(pyridin-4-yl)-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]quinoline-4-carboxamide
-
2-phenyl-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]quinoline-4-carboxamide
-
3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]benzamide
-
4,4'-[cyclohexa-2,5-diene-1,4-diylidenebis[(E)methylylidene(E)diazene-2,1-diyl]]bis[N-(2-chlorophenyl)-4-oxobutanamide]
-
4-[2-(anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide
-
4-[ethyl(phenyl)sulfamoyl]-N-[5-(2-methoxyphenyl)-1,3,4-oxadiazol-2-yl]benzamide
-
5-(4-bromophenyl)-N'-[(E)-(1-methyl-1H-indol-3-yl)methylidene]-4-oxopentanehydrazide
-
5-(4-bromophenyl)-N'-[(E)-(2,3-dimethoxynaphthalen-1-yl)methylidene]-4-oxopentanehydrazide
-
5-(4-fluorophenyl)-N'-[(E)-(1-methyl-1H-indol-3-yl)methylidene]-4-oxopentanehydrazide
-
5-[(2E)-2-(anthracen-9-ylmethylidene)hydrazinyl]-N-(4-bromophenyl)-5-oxopentanamide
-
5-[(2E)-2-(anthracen-9-ylmethylidene)hydrazinyl]-N-(4-fluorophenyl)-5-oxopentanamide
-
5-[(2E)-2-(biphenyl-4-ylmethylidene)hydrazinyl]-N-(4-bromophenyl)-5-oxopentanamide
-
5-[(2E)-2-(biphenyl-4-ylmethylidene)hydrazinyl]-N-(4-fluorophenyl)-5-oxopentanamide
-
5-[(2E)-2-[(2,3-dimethoxynaphthalen-1-yl)methylidene]hydrazinyl]-N-(4-fluorophenyl)-5-oxopentanamide
-
5-[(4-bromophenyl)amino]-N'-[(E)-(1-methyl-1H-indol-3-yl)methylidene]hex-5-enehydrazide
-
N'-[(E)-(2,3-dimethoxynaphthalen-1-yl)methylidene]-5-(4-fluorophenyl)-4-oxopentanehydrazide
-
N'-[(E)-anthracen-9-ylmethylidene]-5-(2-bromophenyl)-4-oxopentanehydrazide
-
N'-[(E)-anthracen-9-ylmethylidene]-5-(2-hydroxyphenyl)-4-oxopentanehydrazide
-
N'-[(E)-anthracen-9-ylmethylidene]-5-(3-bromophenyl)-4-oxopentanehydrazide
-
N'-[(E)-anthracen-9-ylmethylidene]-5-(3-hydroxyphenyl)-4-oxopentanehydrazide
-
N'-[(E)-anthracen-9-ylmethylidene]-5-(4-bromophenyl)-4-oxopentanehydrazide
-
N'-[(E)-anthracen-9-ylmethylidene]-5-(4-fluorophenyl)-4-oxopentanehydrazide
-
N'-[(E)-anthracen-9-ylmethylidene]-5-(4-hydroxyphenyl)-4-oxopentanehydrazide
-
N'-[(E)-biphenyl-4-ylmethylidene]-5-(4-bromophenyl)-4-oxopentanehydrazide
-
N'-[(E)-biphenyl-4-ylmethylidene]-5-(4-fluorophenyl)-4-oxopentanehydrazide
-
N-(4-bromophenyl)-5-[(2E)-2-[(2,3-dimethoxynaphthalen-1-yl)methylidene]hydrazinyl]-5-oxopentanamide
-
N-[3-(3,4-dihydro-2H-pyrrol-5-ylsulfamoyl)phenyl]-2-(furan-2-yl)quinoline-4-carboxamide
-
N-[3-[1-(6-chloro-4-phenylquinazolin-2-yl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-3-yl]phenyl]methanesulfonamide
-
N-[4-(3,4-dihydro-2H-pyrrol-5-ylsulfamoyl)phenyl]-2-(furan-2-yl)quinoline-4-carboxamide
-
N-[4-(4-iodophenyl)-1,3-thiazol-2-yl]-3-[(phenylsulfonyl)amino]benzamide
-
N-[4-(4-methoxyphenyl)-1,3-thiazol-2-yl]-3-[(phenylsulfonyl)amino]benzamide
-
N-[4-[(3,4-dimethyl-1,2-oxazol-5-yl)sulfamoyl]-3-methylphenyl]-2-(4-methoxyphenyl)quinoline-4-carboxamide
-
N-[4-[(3,4-dimethyl-1,2-oxazol-5-yl)sulfamoyl]-3-methylphenyl]-2-(4-methylphenyl)quinoline-4-carboxamide
-
nicotinic acid adenine dinucleotide
product inhibition
S-(4-bromo-8-chloronaphthalen-1-yl) [4-(1,3-thiazol-2-ylsulfamoyl)phenyl]carbamothioate
-
Tithonia diversifolia oil
-
i.e Mexican sunflower, its essential oil is mostly active against Staphylococcus aureus with a halo of 14 mm. The essential oil selectively inhibits in vitro the pure NadD from S. aureus (IC50 of about 60 x02g/mL), with basically none or only minor effects on mammalian orthologue enzymes
-
[(2E)-1-[4-[(2-chlorophenyl)amino]-4-oxobutanoyl]-2-(naphthalen-1-ylmethylidene)hydrazino]acetic acid
-
NAD+
-
deamido-NAD+ as substrate
additional information
inhibitory profiling of partially active mutants and wild-type enzyme MtNadD using small molecule inhibitors, overview. Substrate inhibition in an ordered bi-reactant system
-
additional information
-
inhibitory profiling of partially active mutants and wild-type enzyme MtNadD using small molecule inhibitors, overview. Substrate inhibition in an ordered bi-reactant system
-
additional information
inhibitor synthesis and in vivo evaluation, MIC50 values determined using a standard SYBR green growth assay on synchronous ring stage parasites, overview
-
additional information
-
inhibitor synthesis and in vivo evaluation, MIC50 values determined using a standard SYBR green growth assay on synchronous ring stage parasites, overview
-
additional information
Tithonia diversifolia (Mexican sunflower, flowerheads harvested in Dschang, West Province of Cameroon, Campus of Dschang University) essential oil is mostly active against Staphylococcusaureus and inhibits in vitro the pure NAD biosyntheticenzyme NadD from Staphylococcus aureus with IC50of of about 0.06 mg/ml, with basically none or only minor effects on mammalian orthologue enzymes, GC and NMR spectroemtric analysis of the essential oil composition, detailed overview. The essential oil of Maxican sunflower shows antibacterialand antioxidant activity, and cytotoxicity on human tumor cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.27
3-acetylpyridine-NAD+
-
37°C, pH 7.5
0.74
3-pyridinealdehyde-NAD+
-
37°C, pH 7.5
0.07 - 1.7
beta-nicotinate D-ribonucleotide
0.0045 - 0.029
deamido-NAD+
0.021 - 0.7
nicotinamide mononucleotide
0.043 - 0.4
nicotinamide ribonucleotide
0.0358 - 2.8
nicotinate beta-D-ribonucleotide
0.025 - 1.3
nicotinate ribonucleotide
0.015
nicotinic acid mononucleotide
-
0.011 - 0.323
nicotinic acid ribonucleotide
0.0304
reduced nicotinamide nucleotide
-
-
additional information
additional information
-
0.0017
ATP
-
0.006
ATP
pH 7.5, 37°C, recombinant mutant K47A
0.011
ATP
pH 7.5, 37°C, recombinant mutant T86A
0.011
ATP
pH 7.5, 37°C, recombinant mutant W45A
0.017
ATP
pH 7.5, 37°C, recombinant mutant P44A
0.0199
ATP
recombinant His6-tagged enzyme, pH 7.5, 37°C
0.023
ATP
pH 7.5, 37°C, recombinant mutant W117F
0.033
ATP
pH 7.5, 37°C, recombinant mutant Q46A
0.041
ATP
pH 7.5, 37°C, recombinant wild-type enzyme
0.042
ATP
pH 7.5, 37°C, recombinant mutant T12A
0.044
ATP
pH 7.5, recombinant enzyme
0.06
ATP
-
37°C, pH 7.5, + nicotinate ribonucleotide
0.17
ATP
pH 7.5, 37°C, recombinant mutant L164A
0.19
ATP
pH 7.5, 37°C, recombinant mutant L164Q
0.456
ATP
mutant C41A/C43A, pH not specified in the publication, temperature not specified in the publication
0.525
ATP
wild-type, pH not specified in the publication, temperature not specified in the publication
0.624
ATP
mutant C43A, pH not specified in the publication, temperature not specified in the publication
1.186
ATP
mutant C41A, pH not specified in the publication, temperature not specified in the publication
0.07
beta-nicotinate D-ribonucleotide
mutant A86W/Y118N, pH 7.5, 30°C
0.11
beta-nicotinate D-ribonucleotide
wild-type, pH 7.5, 30°C
1.7
beta-nicotinate D-ribonucleotide
mutant Y84V/Y118D, pH 7.5, 30°C
0.0045
deamido-NAD+
-
37°C, pH 7.5
0.0068
deamido-NAD+
-
37°C, pH 7.4
0.029
deamido-NAD+
-
37°C, pH 7.5
0.083
diphosphate
-
0.65
diphosphate
-
37°C, pH 7.5
1.1
diphosphate
-
37°C, pH 7.5
4.2
diphosphate
-
37°C, pH 7.4
0.069
NAD+
-
37°C, pH 7.5
0.021
nicotinamide mononucleotide
range 0.021-0.032 mM
0.17
nicotinamide mononucleotide
-
0.7
nicotinamide mononucleotide
-
0.043
nicotinamide ribonucleotide
-
37°C, pH 7.4
0.2
nicotinamide ribonucleotide
-
37°C, pH 7.5
0.4
nicotinamide ribonucleotide
-
37°C, pH 7.5
0.0358
nicotinate beta-D-ribonucleotide
recombinant His6-tagged enzyme, pH 7.5, 37°C
0.33
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant Q46A
0.43
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant L164Q
0.48
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant wild-type enzyme
0.52
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant L164A
0.53
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant T12A
0.84
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant P44A
0.98
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant W45A
1.13
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant W117F
2.67
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant W117A
2.7
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant K47A
2.8
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant T86A
0.025
nicotinate ribonucleotide
pH 7.5, recombinant enzyme
0.03
nicotinate ribonucleotide
-
37°C, pH 7.5
0.08
nicotinate ribonucleotide
-
37°C, pH 7.5
0.13
nicotinate ribonucleotide
-
37°C, pH 7.5
1.3
nicotinate ribonucleotide
-
30°C, pH 7.5
0.011
nicotinic acid ribonucleotide
mutant C43A, pH not specified in the publication, temperature not specified in the publication
0.022
nicotinic acid ribonucleotide
wild-type, pH not specified in the publication, temperature not specified in the publication
0.194
nicotinic acid ribonucleotide
mutant C41A/C43A, pH not specified in the publication, temperature not specified in the publication
0.323
nicotinic acid ribonucleotide
mutant C41A, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
4.82 Vmax/KM NMN
-
additional information
additional information
-
7.16 Vmax/KM NaMN
-
additional information
additional information
Michaelis-Menten kinetics are observed for NMN and ATP, but saturation is not accomplished with NAMN, implying low affinity yet detectable activity with this substrate. Double-reciprocal plots show no cooperativity for this enzyme
-
additional information
additional information
steady-state kinetic analysis, sequential kinetic mechanism, bisubstrate enzyme kinetics, overview
-
additional information
additional information
-
steady-state kinetic analysis, sequential kinetic mechanism, bisubstrate enzyme kinetics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.5 - 25
beta-nicotinate D-ribonucleotide
0.002 - 5.5
nicotinate beta-D-ribonucleotide
0.065 - 2.48
nicotinic acid ribonucleotide
0.037
ATP
mutant C41A, pH not specified in the publication, temperature not specified in the publication
0.082
ATP
wild-type, pH not specified in the publication, temperature not specified in the publication
0.7
ATP
mutant C43A, pH not specified in the publication, temperature not specified in the publication
1.92
ATP
mutant C41A/C43A, pH not specified in the publication, temperature not specified in the publication
1.5
beta-nicotinate D-ribonucleotide
mutant Y84V/Y118D, pH 7.5, 30°C
4.9
beta-nicotinate D-ribonucleotide
wild-type, pH 7.5, 30°C
25
beta-nicotinate D-ribonucleotide
mutant A86W/Y118N, pH 7.5, 30°C
0.002
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant W117A
0.015
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant L164Q
0.02
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant K47A
0.03
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant W117F
0.13
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant L164A
0.2
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant T86A
0.22
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant T12A
0.36
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant P44A
0.37
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant W45A
4.7
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant Q46A
5.5
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant wild-type enzyme
0.065
nicotinic acid ribonucleotide
wild-type, pH not specified in the publication, temperature not specified in the publication
0.112
nicotinic acid ribonucleotide
mutant C41A, pH not specified in the publication, temperature not specified in the publication
1.033
nicotinic acid ribonucleotide
mutant C43A, pH not specified in the publication, temperature not specified in the publication
2.48
nicotinic acid ribonucleotide
mutant C41A/C43A, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.86 - 332
beta-nicotinate D-ribonucleotide
0.0008 - 14
nicotinate beta-D-ribonucleotide
0.35 - 12.83
nicotinic acid ribonucleotide
0.008
ATP
pH 7.5, 37°C, recombinant mutant L164Q
0.03
ATP
mutant C41A, pH not specified in the publication, temperature not specified in the publication
0.08
ATP
pH 7.5, 37°C, recombinant mutant L164A
0.17
ATP
wild-type, pH not specified in the publication, temperature not specified in the publication
1.17
ATP
mutant C43A, pH not specified in the publication, temperature not specified in the publication
1.3
ATP
pH 7.5, 37°C, recombinant mutant W117F
3
ATP
pH 7.5, 37°C, recombinant mutant K47A
4.17
ATP
mutant C41A/C43A, pH not specified in the publication, temperature not specified in the publication
5
ATP
pH 7.5, 37°C, recombinant mutant T12A
18
ATP
pH 7.5, 37°C, recombinant mutant T86A
21
ATP
pH 7.5, 37°C, recombinant mutant P44A
34
ATP
pH 7.5, 37°C, recombinant mutant W45A
134
ATP
pH 7.5, 37°C, recombinant wild-type enzyme
142
ATP
pH 7.5, 37°C, recombinant mutant Q46A
0.86
beta-nicotinate D-ribonucleotide
mutant Y84V/Y118D, pH 7.5, 30°C
44
beta-nicotinate D-ribonucleotide
wild-type, pH 7.5, 30°C
332
beta-nicotinate D-ribonucleotide
mutant A86W/Y118N, pH 7.5, 30°C
0.0008
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant W117A
0.007
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant K47A
0.03
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant W117F
0.04
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant L164Q
0.07
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant T86A
0.4
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant P44A
0.4
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant T12A
0.4
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant W45A
2.5
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant L164A
12
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant wild-type enzyme
14
nicotinate beta-D-ribonucleotide
pH 7.5, 37°C, recombinant mutant Q46A
0.35
nicotinic acid ribonucleotide
mutant C41A, pH not specified in the publication, temperature not specified in the publication
3
nicotinic acid ribonucleotide
wild-type, pH not specified in the publication, temperature not specified in the publication
9.38
nicotinic acid ribonucleotide
mutant C43A, pH not specified in the publication, temperature not specified in the publication
12.83
nicotinic acid ribonucleotide
mutant C41A/C43A, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.036
2-(2,4-dimethylphenyl)-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]quinoline-4-carboxamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.035
2-(2,4-dimethylphenyl)-N-[4-[(5-methyl-1,2-oxazol-3-yl)sulfamoyl]phenyl]quinoline-4-carboxamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.033
2-(2-chlorophenyl)-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]quinoline-4-carboxamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.049
2-(4-bromophenyl)-N-[4-[(4-methylpyrimidin-2-yl)sulfamoyl]phenyl]quinoline-4-carboxamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.017
2-(furan-2-yl)-N-[3-(3,4,5,6-tetrahydropyridin-2-ylsulfamoyl)phenyl]quinoline-4-carboxamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.074
2-(furan-2-yl)-N-[3-methoxy-4-(morpholin-4-ylsulfonyl)phenyl]quinoline-4-carboxamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.051
2-(furan-2-yl)-N-[3-methyl-4-(morpholin-4-ylsulfonyl)phenyl]quinoline-4-carboxamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.056
2-(pyridin-4-yl)-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]quinoline-4-carboxamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.043
2-phenyl-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]quinoline-4-carboxamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.024
3-(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)-N-[4-(1,3-thiazol-2-ylsulfamoyl)phenyl]benzamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.013
4,4'-[cyclohexa-2,5-diene-1,4-diylidenebis[(E)methylylidene(E)diazene-2,1-diyl]]bis[N-(2-chlorophenyl)-4-oxobutanamide]
Bacillus anthracis
pH 7.5, 22°C
0.025
4-[2-(anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide
Bacillus anthracis
pH 7.5, 22°C
0.096
4-[ethyl(phenyl)sulfamoyl]-N-[5-(2-methoxyphenyl)-1,3,4-oxadiazol-2-yl]benzamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.015
K891-0166
Streptococcus pyogenes
pH 7.5, 37°C
0.049
N-[3-(3,4-dihydro-2H-pyrrol-5-ylsulfamoyl)phenyl]-2-(furan-2-yl)quinoline-4-carboxamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.13
N-[3-[1-(6-chloro-4-phenylquinazolin-2-yl)-5-(furan-2-yl)-4,5-dihydro-1H-pyrazol-3-yl]phenyl]methanesulfonamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.046
N-[4-(3,4-dihydro-2H-pyrrol-5-ylsulfamoyl)phenyl]-2-(furan-2-yl)quinoline-4-carboxamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.18
N-[4-(4-iodophenyl)-1,3-thiazol-2-yl]-3-[(phenylsulfonyl)amino]benzamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.116
N-[4-(4-methoxyphenyl)-1,3-thiazol-2-yl]-3-[(phenylsulfonyl)amino]benzamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.13
N-[4-[(3,4-dimethyl-1,2-oxazol-5-yl)sulfamoyl]-3-methylphenyl]-2-(4-methoxyphenyl)quinoline-4-carboxamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.13
N-[4-[(3,4-dimethyl-1,2-oxazol-5-yl)sulfamoyl]-3-methylphenyl]-2-(4-methylphenyl)quinoline-4-carboxamide
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
0.024
S-(4-bromo-8-chloronaphthalen-1-yl) [4-(1,3-thiazol-2-ylsulfamoyl)phenyl]carbamothioate
Mycobacterium tuberculosis
pH 7.5, 37°C, recombinant wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
in complex with inhibitors 4-[2-(anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide, 4,4'-[cyclohexa-2,5-diene-1,4-diylidenebis[(E)methylylidene(E)diazene-2,1-diyl]]bis[N-(2-chlorophenyl)-4-oxobutanamide], and [(2E)-1-[4-[(2-chlorophenyl)amino]-4-oxobutanoyl]-2-(naphthalen-1-ylmethylidene)hydrazino]acetic acid. 4-[2-(Anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide binds at an enzyme monomer-monomer interface formed in the crystal of the complex, it sits at a central cleft between strands beta1 and beta4 of the beta sheet, which is the catalytic and substrate binding sites of the enzyme. The structures reveal a common binding site near residues Trp117, Try112, and Met109. This site overlaps but is distinct from the substrate-binding pocket
sitting drop and hanging drop vapour diffusion method, mixing 0.001 ml of 4 mg/ml protein in 50 mM Tris, pH 7.0, 100 mM NaCl, 100 mM Arg, 100 mM Glu, 1% glycerol, 1 mM DTT, and containing 200 mM trehalose, with 0.001 ml of reservoir solution containing 2.1 M ammonium sulfate, 100 mM HEPES pH 7.0, 2% PEG 400 and 10 mM MgCl2, cryoprotection by 25% glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution, usage molecular replacement and of self-interaction chromatography for process optimization
crystals of the apo-enzyme belong to space group: P21 with 58.5% solvent and contain four molecules of NaMN AT in the asymmetric subunit, crystals in complex with deamido-NAD+ belong to space group: P212121 with 55.6% solvent and contain six molecules of NaMN AT in the asymmetric subunit, conditions: polyethylene glycol 3350 and 100 mM MgCl2
-
crystallization of the apo-enzyme to space group: P1 with 44% sovent, and in complex with deamido-NAD+ with 42.4% solvent in space group I222, hanging-drop vapour-diffusion method at 20°C in 100 mM Tris, pH 7, 200 mM NaCl and 800 mM sodium citrate
homology modeling of structure, based on structures of isoform NMNAT1 and NMNAT3 and molecular docking of potential inhibitors
structure of isoform NMNAT3 to 2 A resolution
purified recombinant wild-type and W117A mutant enzymes, sitting drop vapour diffusion method at 20°C, microcrystal seeding using hanging drops, mixing of 10 mg/ml protein in 20 mM Tris, pH 7.8, 200 mM NaCl, and 5% v/v glycerol with well solution containing 1.2-1.5 M MgSO4, 0.1 M MES buffer, pH 6.0-6.5, microseeds are added to the drops 1 h later, macrocrystals growth within 3-5 days., X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement
structures of NaMNAT in the product-bound state with nicotinic acid adenine dinucleotide and complexed with an alpha,beta-non-hydrolizable ATP analog to a resolution of 2.2 A and 2.5 A, respectively. NaMNAT possesses two cysteine residues within the active site likely to be involved in redox regulation of NaMNAT activity. NaMNAT is capable of utilizing nicotinic acid adenine dinucleotide and nicotinamide mononucleotide, reactions of EC 2.7.7.18 and EC 2.7.7.1, resectively, with a slight preference for nicotinic acid adenine dinucleotide
crystal structure of NaMN-bound form at 1.7 A, ATP-bound form at 2.0 A, apo-form at 2.0 A. The substrate-unbound and substrate-complexed structures are all in the fully open conformation. There is little conformational change upon binding each of the substrates. A conformational change is necessary to bring the two substrates closer together for initiating the catalysis. The authors suggest that such a conformational change likely occurs only after both substrates are simultaneously bound in the active site
Crystals of saNaMNAT were initially obtained at 22°C from polyethylene glycol 3000 and phosphatecitrate buffer.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
A86W/Y118N
increase in activity, and mutant accepts nicotinamide ribonucleotide as substrate
Y84V/Y118D
mutant prefers nicotinamide ribonucleotide over nicotinic acid ribonucleotide bas substrate
A86W/Y118N
-
increase in activity, and mutant accepts nicotinamide ribonucleotide as substrate
-
Y84V/Y118D
-
mutant prefers nicotinamide ribonucleotide over nicotinic acid ribonucleotide bas substrate
-
R232Q
mutation impairs NAD synthase and chaperone functions
E198P/L217R
mutation disrupts the dimer interface, leading to a mixture of dimer and monomer in solution
D14A
site-directed mutagenesis, almost inactive mutant
H17A
site-directed mutagenesis, almost inactive mutant
H20A
site-directed mutagenesis, almost inactive mutant
K47A
site-directed mutagenesis, the mutant shows a decrease in Km for ATP and a 6fold increase in Km for nicotinate beta-D-ribonucleotide and a nearly abolished enzyme activity
L164A
site-directed mutagenesis, the L164A mutant elutes as both a monomer and a dimer during purification, the mutant shows 40fold reduced activity compared to the wild-type enzyme
L164Q
site-directed mutagenesis, the L164Q mutant elutes as both a monomer and a dimer during purification, almost inactive mutant
P44A
site-directed mutagenesis, the mutant shows a decrease in Km for ATP
Q46A
site-directed mutagenesis
T12A
site-directed mutagenesis, the T12A mutant elutes as a dimer and as an aggregated protein during purification, the mutant shows highly reduced activity compared to the wild-type enzyme
T86A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
W117A
site-directed mutagenesis, the mutant shows a 10fold higher expression level compared to the wild-type enzyme in Escherichia coli, three-dimensional structure determination and analysis, the mutant shows highly reduced activity compared to the wild-type enzyme
W117F
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
W45A
site-directed mutagenesis
D14A
-
site-directed mutagenesis, almost inactive mutant
-
H17A
-
site-directed mutagenesis, almost inactive mutant
-
H20A
-
site-directed mutagenesis, almost inactive mutant
-
K47A
-
site-directed mutagenesis, the mutant shows a decrease in Km for ATP and a 6fold increase in Km for nicotinate beta-D-ribonucleotide and a nearly abolished enzyme activity
-
P44A
-
site-directed mutagenesis, the mutant shows a decrease in Km for ATP
-
C41A
active site mutant, increase in Km values
C41A/C43A
active site mutant
C43A
active site mutant, 10fold increase in vmax value
D110A
site-directed mutagenesis replacing the conserved catalytic site, inactive mutant
additional information
-
mutation in the nadD gene, renamed nadD72, leads to a temparature-sensitive strain which cannot grow on minimal medium
additional information
generation of mutants lacking residues Glu107-Lys146. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoforms NMNAT1 are distributed throughout the cytoplasm
additional information
generation of mutants lacking residues Glu107-Lys146. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoforms NMNAT1 are distributed throughout the cytoplasm
additional information
generation of mutants lacking residues Glu107-Lys146. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoforms NMNAT1 are distributed throughout the cytoplasm
additional information
generation of mutants lacking residues Leu105-Ala125 of isoform NMNAT3. Overexpression of the construct results in a strong increase in overall enzymic activity compared with non-transfected cells
additional information
generation of mutants lacking residues Leu105-Ala125 of isoform NMNAT3. Overexpression of the construct results in a strong increase in overall enzymic activity compared with non-transfected cells
additional information
generation of mutants lacking residues Leu105-Ala125 of isoform NMNAT3. Overexpression of the construct results in a strong increase in overall enzymic activity compared with non-transfected cells
additional information
generation of mutants lacking residues Val109-Leu192. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoform NMNAT2 are distributed throughout the cytoplasm
additional information
generation of mutants lacking residues Val109-Leu192. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoform NMNAT2 are distributed throughout the cytoplasm
additional information
generation of mutants lacking residues Val109-Leu192. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoform NMNAT2 are distributed throughout the cytoplasm
additional information
mutation R232Q in one allele plus a single duplication of a cytosine at position 403 in exon 5 resulting in a frameshift and premature stop after 44 amino acids lead to a loss of NMNAT2 function, identified in fetus with akinesia deformation sequence, severely reduced skeletal muscle mass and hydrops fetalis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Wagner, R.; Wagner, K.G.
The pyridine-nucleotide cycle in tobacco. Enzyme activities for the de-novo synthesis of NAD
Planta
165
532-537
1985
Nicotiana tabacum
brenda
Imsande, J.
Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia coli
J. Biol. Chem.
236
1494-1497
1961
Escherichia coli
brenda
Dahmen, W.; Webb, B.; Preiss, J.
The deamido-diphosphopyridine nucleotide and diphosphopyridine nucleotide pyrophosphorylases of Escherichia coli and yeast
Arch. Biochem. Biophys.
120
440-450
1967
Escherichia coli, Saccharomyces cerevisiae
brenda
Zhang, H.; Zhou, T.; Kurnasov, O.; Cheek, S.; Grishin, N.V.; Osterman, A.
Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD
Structure
10
69-79
2002
Escherichia coli (P0A752), Escherichia coli
brenda
Stancek, M.; Isaksson, L.A.; Ryden-Aulin, M.
fusB is an allele of nadD, encoding nicotinate mononucleotide adenylyltransferase in Escherichia coli
Microbiology
149
2427-2433
2003
Escherichia coli
brenda
Olland, A.M.; Underwood, K.W.; Czerwinski, R.M.; Lo, M.C.; Aulabaugh, A.; Bard, J.; Stahl, M.L.; Somers, W.S.; Sullivan, F.X.; Chopra, R.
Identification, characterization, and crystal structure of Bacillus subtilis nicotinic acid mononucleotide adenylyltransferase
J. Biol. Chem.
277
3698-3707
2002
Bacillus subtilis
brenda
Yoon, H.J.; Kim, H.L.; Mikami, B.; Suh, S.W.
Crystal structure of nicotinic acid mononucleotide adenylyltransferase from Pseudomonas aeruginosa in its Apo and substrate-complexed forms reveals a fully open conformation
J. Mol. Biol.
351
258-265
2005
Pseudomonas aeruginosa (Q9HX21), Pseudomonas aeruginosa
brenda
Han, S.; Forman, M.D.; Loulakis, P.; Rosner, M.H.; Xie, Z.; Wang, H.; Danley, D.E.; Yuan, W.; Schafer, J.; Xu, Z.
Crystal structure of nicotinic acid mononucleotide adenylyltransferase from Staphyloccocus aureus: structural basis for NaAD interaction in functional dimer
J. Mol. Biol.
360
814-825
2006
Methanothermobacter thermautotrophicus, Bacillus subtilis (P54455), Staphylococcus aureus (Q5HFG7), Staphylococcus aureus, Staphylococcus aureus COL (Q5HFG7)
brenda
Hashida, S.N.; Takahashi, H.; Kawai-Yamada, M.; Uchimiya, H.
Arabidopsis thaliana nicotinate/nicotinamide mononucleotide adenyltransferase (AtNMNAT) is required for pollen tube growth
Plant J.
49
694-703
2007
Arabidopsis thaliana
brenda
Lu, S.; Smith, C.D.; Yang, Z.; Pruett, P.S.; Nagy, L.; McCombs, D.; Delucas, L.J.; Brouillette, W.J.; Brouillette, C.G.
Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis
Acta Crystallogr. Sect. F
64
893-898
2008
Bacillus anthracis (A0A6L7H177), Bacillus anthracis
brenda
Zhai, R.G.; Rizzi, M.; Garavaglia, S.
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme
Cell. Mol. Life Sci.
66
2805-2818
2009
Bacillus anthracis, Escherichia coli, Homo sapiens, Pseudomonas aeruginosa
brenda
Lau, C.; Niere, M.; Ziegler, M.
The NMN/NaMN adenylyltransferase (NMNAT) protein family
Front. Biosci.
14
410-431
2009
Arabidopsis thaliana, Escherichia coli (P0A752), Saccharomyces cerevisiae (P53204), Homo sapiens (Q96T66)
brenda
Gou, D.; Liang, L.; Liu, R.; Zhang, C.; Wu, M.; Ma, J.; Chen, K.; Zhu, J.; Jiang, M.
Effect of overexpression of nicotinic acid mononucleotide adenylyltransferase on succinic acid production in Escherichia coli NZN111
Chin. J. Biotechnol.
28
1059-1069
2012
Escherichia coli
brenda
Lau, C.; Dolle, C.; Gossmann, T.; Agledal, L.; Niere, M.; Ziegler, M.
Isoform-specific targeting and interaction domains in human nicotinamide mononucleotide adenylyltransferases
J. Biol. Chem.
285
18868-18876
2010
Homo sapiens (Q96T66), Homo sapiens (Q9BZQ4), Homo sapiens (Q9HAN9)
brenda
Huang, N.; Kolhatkar, R.; Eyobo, Y.; Sorci, L.; Rodionova, I.; Osterman, A.L.; Mackerell, A.D.; Zhang, H.
Complexes of bacterial nicotinate mononucleotide adenylyltransferase with inhibitors: implication for structure-based drug design and improvement
J. Med. Chem.
53
5229-5239
2010
Bacillus anthracis (C3L5T6), Bacillus anthracis, Bacillus anthracis CDC 684 (C3L5T6)
brenda
Sorci, L.; Blaby,I.K.; Rodionova, I.A.; De Ingeniis, J.; Tkachenko, S.; de Crcy-Lagard, V.; Osterman, A.L.
uinolinate salvage and insights for targeting NAD biosynthesis in group A streptococci
J. Bacteriol.
195
726-732
2013
Streptococcus pyogenes (Q5XDT7), Streptococcus pyogenes ATCC BAA-946 (Q5XDT7)
brenda
Forero-Baena, N.; Sanchez-Lancheros, D.; Buitrago, J.; Bustos, V.; Ramirez-Hernandez, M.
Identification of a nicotinamide/nicotinate mononucleotide adenylyltransferase in Giardia lamblia (GlNMNAT)
Biochim. Open
1
61-69
2015
Giardia intestinalis (A8BIC5)
brenda
Orsomando, G.; Agostinelli, S.; Bramucci, M.; Cappellacci, L.; Damiano, S.; Lupidi, G.; Maggi, F.; Ngahang Kamte, S.; Biapa Nya, P.; Papa, F.; Petrelli, D.; Quassinti, L.; Sorci, L.; Vitali, L.; Petrelli, R.
Mexican sunflower (Tithonia diversifolia, Asteraceae) volatile oil as a selective inhibitor of Staphylococcus aureus nicotinate mononucleotide adenylyltransferase (NadD)
Ind. Crops Prod.
85
181-189
2016
Staphylococcus aureus (P65502), Staphylococcus aureus N315 (P65502)
-
brenda
Rodionova, I.A.; Zuccola, H.J.; Sorci, L.; Aleshin, A.E.; Kazanov, M.D.; Ma, C.T.; Sergienko, E.; Rubin, E.J.; Locher, C.P.; Osterman, A.L.
Mycobacterial nicotinate mononucleotide adenylyltransferase: structure, mechanism, and implications for drug discovery
J. Biol. Chem.
290
7693-7706
2015
Mycobacterium tuberculosis (P9WJJ5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJJ5)
brenda
O'Hara, J.K.; Kerwin, L.J.; Cobbold, S.A.; Tai, J.; Bedell, T.A.; Reider, P.J.; Llinas, M.
Targeting NAD+ metabolism in the human malaria parasite Plasmodium falciparum
PLoS ONE
9
e94061
2014
Plasmodium falciparum (Q8IE38), Plasmodium falciparum
brenda
Wang, X.; Zhou, Y.; Wang, L.; Liu, W.; Liu, Y.; Peng, C.; Zhao, Z.
Engineering Escherichia coli nicotinic acid mononucleotide adenylyltransferase for fully active amidated NAD biosynthesis
Appl. Environ. Microbiol.
83
e00692
2017
Escherichia coli (A0A140NE60), Escherichia coli, Escherichia coli BL21-DE3 (A0A140NE60)
brenda
Rossi, F.; Geiszler, P.C.; Meng, W.; Barron, M.R.; Prior, M.; Herd-Smith, A.; Loreto, A.; Lopez, M.Y.; Faas, H.; Pardon, M.C.; Conforti, L.
NAD-biosynthetic enzyme NMNAT1 reduces early behavioral impairment in the htau mouse model of tauopathy
Behav. Brain Res.
339
140-152
2018
Mus musculus (Q9EPA7)
brenda
Ma, X.; Zhu, Y.; Lu, J.; Xie, J.; Li, C.; Shin, W.; Qiang, J.; Liu, J.; Dou, S.; Xiao, Y.; Wang, C.; Jia, C.; Long, H.; Yang, J.; Fang, Y.; Jiang, L.; Zhang, Y.; Zhang, S.; Zhai, R.; Liu, C.; Li, D.
Nicotinamide mononucleotide adenylyl transferase uses its NAD+ substrate-binding site to chaperone phosphorylated TAU
eLife
9
e51859
2020
Mus musculus (Q99JR6), Drosophila melanogaster (Q9VC03)
brenda
Lukacs, M.; Gilley, J.; Zhu, Y.; Orsomando, G.; Angeletti, C.; Liu, J.; Yang, X.; Park, J.; Hopkin, R.J.; Coleman, M.P.; Zhai, R.G.; Stottmann, R.W.
Severe biallelic loss-of-function mutations in nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) in two fetuses with fetal akinesia deformation sequence
Exp. Neurol.
320
112961
2019
Homo sapiens (Q9BZQ4)
brenda
Contreras Rodriguez, L.E.; Ziegler, M.; Ramirez Hernandez, M.H.
Kinetic and oligomeric study of Leishmania braziliensis nicotinate/nicotinamide mononucleotide adenylyltransferase
Heliyon
6
e03733
2020
Leishmania braziliensis
brenda
Orsomando, G.; Agostinelli, S.; Bramucci, M.; Cappellacci, L.; Damiano, S.; Lupidi, G.; Maggi, F.; Ngahang Kamte, S.; Biapa Nya, P.; Papa, F.; Petrelli, D.; Quassinti, L.; Sorci, L.; Vitali, L.; Petrelli, R.
Mexican sunflower (Tithonia diversifolia, Asteraceae) volatile oil as a selective inhibitor of Staphylococcus aureus nicotinate mononucleotide adenylyltransferase (NadD)
Ind. Crops Prod.
85
181-189
2016
Staphylococcus aureus, Staphylococcus aureus ATCC 25923
-
brenda
Konishi, K.; Ueda, S.; Kawano, M.; Osawa, S.; Tamura, T.; Hokazono, E.; Kayamori, Y.; Sakasegawa, S.I.
Characterization and application of a novel nicotinamide mononucleotide adenylyltransferase from Thermus thermophilus HB8
J. Biosci. Bioeng.
125
385-389
2018
Thermus thermophilus (Q5SHF0)
brenda
Bathke, J.; Fritz-Wolf, K.; Brandstaedter, C.; Burkhardt, A.; Jortzik, E.; Rahlfs, S.; Becker, K.
Structural and functional characterization of Plasmodium falciparum nicotinic acid nononucleotide adenylyltransferase
J. Mol. Biol.
428
4946-4961
2016
Plasmodium falciparum (Q8IE38), Plasmodium falciparum
brenda
Eren, G.
Homology modeling of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 Insights into isoenzyme-specific differences using molecular docking simulatons
Lett. Drug Des. Discov.
14
727-736
2017
Homo sapiens (Q9BZQ4)
-
brenda
Pottorf, T.; Mann, A.; Fross, S.; Mansel, C.; Vohra, B.P.S.
Nicotinamide mononucleotide adenylyltransferase 2 maintains neuronal structural integrity through the maintenance of golgi structure
Neurochem. Int.
121
86-97
2018
Mus musculus (Q8BNJ3)
brenda