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 + deamido-NAD+ + Asn
AMP + diphosphate + NAD+ + Asp
-
-
-
-
?
ATP + deamido-NAD+ + Gln + hydroxylamine
AMP + diphosphate + hydroxamate analog + ?
-
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + L-Glu
ATP + deamido-NAD+ + L-glutamine + H2O
AMP + diphosphate + NAD+ + L-glutamate
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
NADsyn1 uses not only ammonia but also glutamine. The Vmax/KM-value for NADsyn1 with glutamine is 6.3fold higher than the Vmax/Km-value for NH3
-
-
?
ATP + deamido-NAD+ + NH3 + H2O
AMP + diphosphate + NAD+
ATP + deamido-NAD+ + NH4+
AMP + diphosphate + NAD+
ATP + deamido-NAD+ + NH4+ + H2O
AMP + diphosphate + NAD+
-
-
-
?
ATP + deamido-NMN + L-Gln
AMP + diphosphate + NMN + L-Glu
poor substrate
-
-
?
Gln + hydroxylamine
AMP + diphosphate + hydroxamate analog + ?
-
-
-
?
additional information
?
-
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + L-Glu
-
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + L-Glu
-
-
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + L-Glu
-
-
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + L-Glu
-
-
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + L-Glu
-
-
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + L-Glu
-
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + L-Glu
-
-
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + L-Glu
-
-
-
-
?
ATP + deamido-NAD+ + L-glutamine + H2O
AMP + diphosphate + NAD+ + L-glutamate
-
-
-
?
ATP + deamido-NAD+ + L-glutamine + H2O
AMP + diphosphate + NAD+ + L-glutamate
-
-
-
?
ATP + deamido-NAD+ + L-glutamine + H2O
AMP + diphosphate + NAD+ + L-glutamate
NADsyn1 uses not only ammonia but also glutamine. The Vmax/KM-value for NADsyn1 with glutamine is 6.3fold higher than the Vmax/Km-value for NH3
-
-
?
ATP + deamido-NAD+ + L-glutamine + H2O
AMP + diphosphate + NAD+ + L-glutamate
-
-
-
?
ATP + deamido-NAD+ + L-glutamine + H2O
AMP + diphosphate + NAD+ + L-glutamate
-
-
-
?
ATP + deamido-NAD+ + L-glutamine + H2O
AMP + diphosphate + NAD+ + L-glutamate
-
-
-
?
ATP + deamido-NAD+ + L-glutamine + H2O
AMP + diphosphate + NAD+ + L-glutamate
-
last step in NAD+ biosynthesis
-
?
ATP + deamido-NAD+ + L-glutamine + H2O
AMP + diphosphate + NAD+ + L-glutamate
-
-
-
?
ATP + deamido-NAD+ + L-glutamine + H2O
AMP + diphosphate + NAD+ + L-glutamate
-
-
-
-
?
ATP + deamido-NAD+ + NH3 + H2O
AMP + diphosphate + NAD+
-
-
-
?
ATP + deamido-NAD+ + NH3 + H2O
AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + NH3 + H2O
AMP + diphosphate + NAD+
-
NAD+ synthase is able to use ammonia or glutamine as nitrogen source
-
?
ATP + deamido-NAD+ + NH3 + H2O
AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + NH4+
AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + NH4+
AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + NH4+
AMP + diphosphate + NAD+
-
-
-
-
?
additional information
?
-
enzyme NadE1 uses glutamine as a preferential nitrogen donor, poor activity with NH3
-
-
?
additional information
?
-
-
enzyme NadE1 uses glutamine as a preferential nitrogen donor, poor activity with NH3
-
-
?
additional information
?
-
enzyme NadE1 uses glutamine as a preferential nitrogen donor, poor activity with NH3
-
-
?
additional information
?
-
-
no activity with NH4+ as nitrogen donor at 3 mM NH4+
-
-
?
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.
4.3
deamido-NMN
pH 7.5, 30°C
additional information
additional information
-
0.015
ATP
-
pH 7.5
0.031
ATP
pH 8.5, 30°C, recombinant His-tagged enzyme
0.089
ATP
37°C, wild-type NADsyn1
0.1 - 2
ATP
pH and temperature not specified in the publication
0.12
ATP
37°C, NADsyn1 C175S mutant
0.12
ATP
-
wild-type, glutamine-dependent reaction
0.6
ATP
-
mutant C176A, ammonia-dependent reaction
0.79
ATP
-
37°C, pH 8.0, recombinant NadE-679
0.8
ATP
-
wild-type enzyme
0.8
ATP
-
mutant enzyme E52A
1.3
ATP
-
37°C, pH 8.5, recombinant NadE-738
1.3
ATP
-
mutant enzyme C176A
1.4
ATP
-
wild-type, ammonia-dependent reaction
0.01
deamido-NAD+
pH 8.5, 30°C, recombinant His-tagged enzyme
0.017
deamido-NAD+
pH 7.5, 30°C
0.021
deamido-NAD+
-
pH 8.3, 37°C
0.04
deamido-NAD+
-
pH 7.5
0.049
deamido-NAD+
37°C, wild-type NADsyn1
0.13
deamido-NAD+
-
wild-type, glutamine-dependent reaction
0.19
deamido-NAD+
-
pH 7.6
0.2
deamido-NAD+
37°C, NADsyn1 C175S mutant
0.5
deamido-NAD+
-
wild-type enzyme
0.52
deamido-NAD+
-
37°C, pH 8.0, recombinant NadE-679
0.65
deamido-NAD+
-
mutant C176A, ammonia-dependent reaction
0.7
deamido-NAD+
-
wild-type, ammonia-dependent reaction
1.4
deamido-NAD+
-
mutant enzyme C176A
1.4
deamido-NAD+
-
mutant enzyme E52A
2.9
deamido-NAD+
-
37°C, pH 8.5, recombinant NadE-738
2
Gln
-
-
0.001
L-Gln
-
pH 7.5
0.42
L-Gln
-
pH 8.3, 37°C
1.3
L-Gln
-
wild-type, glutamine-dependent reaction
1.6
L-Gln
-
wild-type enzyme
7.8
L-Gln
-
mutant D656A, glutamine-dependent reaction
20
L-Gln
-
wild-type, ammonia-dependent reaction
0.365
L-glutamine
pH 8.5, 30°C, recombinant His-tagged enzyme
1.1
L-glutamine
-
37°C, pH 8.8, recombinant NadE-738
1.4
L-glutamine
-
mutant enzyme Y601A, at 37°C
1.44
L-glutamine
37°C, wild-type NADsyn1
1.5
L-glutamine
pH and temperature not specified in the publication
1.6
L-glutamine
-
37°C, pH 8.5, recombinant NadE-679
3.5
L-glutamine
-
mutant enzyme Y532A/Y601A, at 37°C
5.3
L-glutamine
-
wild type enzyme, at 37°C
0.089
NH3
-
mutant D656A, ammonia-dependent reaction
13.1
NH3
37°C, wild-type NADsyn1
15
NH3
-
mutant C176A, ammonia-dependent reaction
23.9
NH3
37°C, NADsyn1 C175S mutant
1.6
NH4+
-
mutant enzyme E52A
2.3
NH4+
-
mutant enzyme C176A
2.5
NH4+
-
37°C, pH 8.0, recombinant NadE-679
2.7
NH4+
-
wild-type enzyme
27
NH4+
-
37°C, pH 8.5, recombinant NadE-738
additional information
additional information
Michaelis-Menten and Hanes-Woolf kinetics, kinetic analysis
-
additional information
additional information
-
Michaelis-Menten and Hanes-Woolf kinetics, kinetic analysis
-
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.
0.0002
-
mutant enzyme R112L, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
0.0011
-
mutant enzyme D593A/F622A, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
0.0087
-
mutant enzyme L604N, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
0.015
-
mutant enzyme L604A/L519A, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
0.024
-
mutant enzyme R112S, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
0.033
-
recombinant NadE-738, nitrogen donor glutamine
0.0533
-
mutant enzyme I111A, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
0.09
-
glutamine-dependent activity
0.0931
-
mutant enzyme Y601A, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
0.1
-
recombinant NadE-738, nitrogen donor NH4+
0.112
-
mutant enzyme E177A, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
0.23
-
NH3 dependent activity
0.288
-
mutant enzyme F622A, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
0.293
-
mutant enzyme L604A, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
0.435
-
mutant enzyme D593A, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
0.44
-
recombinant NadE-679, nitrogen donor glutamine
0.644
-
mutant enzyme M621A, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
0.67
-
recombinant NadE-679, nitrogen donor NH4+
2.33
-
wild type enzyme, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
additional information
-
coupled enzyme assay for the measurement of recombinant human NAD+ synthetase by employing lactate dehydrogenase in a cycling/amplification reaction linked ultimately to the fluorescence generation of resorufin from reazurin via diaphorase
0.0017
-
mutant enzyme Y532A/M621A, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
0.0017
-
mutant enzyme Y532A/Y601A, at 37°C, with 2 mM ATP, 5 mM MgCl2, 50 mM Tris-HCl, pH 8.0, 56 mM KCl, and 0.2 mg/ml bovine serum albumin
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.
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
-
-
brenda
-
-
brenda
-
wild-type Nicotiana sylvestris and the CMSII mutant that lacks respiratory complex I show different NADS mRNA expression pattern
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
-
traces
brenda
-
-
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
-
-
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
-
-
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
-
traces
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
-
-
brenda
the major sites of NADsyn1 gene expression are the small intestine, kidney, liver, and testis, whereas the skeletal muscle, spleen, lung, heart, and brain show a weak signal
brenda
-
traces
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
metabolism
due to the presence of an additional glutamine transferase domain, abNadE can efficiently utilize l-glutamine (as well as ammonia) for the amidation of NAD precursor
physiological function
nadE, encoding glutamine-dependent NAD synthetase, is dispensable when the nondeamidating salvage pathway of nicotinamide salvage/recycling functions as the only route of NAD biogenesis
evolution
most residues lining the ATP-binding site are conserved among the glutamine-dependent NAD+ synthetases, whereas residues not conserved, such as Leu399 andGly366, interact with the adenine ring and the adenylyl ribose with the backbone oxygen and nitrogen
evolution
-
most residues lining the ATP-binding site are conserved among the glutamine-dependent NAD+ synthetases, whereas residues not conserved, such as Leu399 andGly366, interact with the adenine ring and the adenylyl ribose with the backbone oxygen and nitrogen
-
malfunction
a homolog of the human SIRT6-like gene, SRT2, is upregulated in the NAD+ synthase mutant, which shows a longer vegetative life span than wild-type cells
malfunction
nadE is dispensable when the nondeamidating salvage pathway functions as the only route of NAD biogenesis
additional information
the enzyme contains glutaminase and synthetase active sites, structures and ligand binding, overview. The ATP-binding site is located in a deep cleft formed solely by a single subunit next to the nicotinic acidadenine dinucleotide-binding site
additional information
-
the enzyme contains glutaminase and synthetase active sites, structures and ligand binding, overview. The ATP-binding site is located in a deep cleft formed solely by a single subunit next to the nicotinic acidadenine dinucleotide-binding site
additional information
-
the enzyme contains glutaminase and synthetase active sites, structures and ligand binding, overview. The ATP-binding site is located in a deep cleft formed solely by a single subunit next to the nicotinic acidadenine dinucleotide-binding site
-
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.
C175S
in contrast with the wild-type NADsyn1, the activity of the mutant NADsyn1 (C175S-NADsyn1) is not detected when glutamine is used as a substrate, whereas the activity remains unaltered with NH4Cl
D656A
-
strong decrease in catalytic efficiency
E52A
-
complete loss of glutamine-dependent activity, retains 30% of its NH3-dependent activity
K121A
-
complete loss of glutamine-dependent and NH3-dependent activity
L486A
site-directed mutagenesis
L486F
site-directed mutagenesis
Y58A
site-directed mutagenesis
C176A
-
site-directed mutagenesis, inactive mutant, analysis of ligand binding structures
-
L486A
-
site-directed mutagenesis
-
L486F
-
site-directed mutagenesis
-
Y58A
-
site-directed mutagenesis
-
D593A
-
poor synthetase activity
D593A/F622A
-
synthetase dead
E177A
-
poor synthetase activity
F622A
-
poor synthetase activity
I111A
-
poor synthetase activity
L529A/L604A
-
poor synthetase activity
L604A
-
poor synthetase activity
L604N
-
poor synthetase activity
M621A
-
synthetase mutant that depresses all activities
R112L
-
poor synthetase activity that inhibit substrate synergism
R112S
-
poor synthetase activity that inhibit substrate synergism
Y532A/Y601A
-
synthetase dead
Y601A
-
poor synthetase activity
Y601A/M621A
-
synthetase dead
S740I
Chlamydomonas cells bearing a NAD+ synthase mutation have a defective NAD+ de novo synthesis pathway. Mutant cells show longer vegitative life span than wild-type cells. Up-regulation of a sirtuin gene is linked to the extended life span in the mutant strain
S740I
mutant fails to grow on Sager and Granick rich medium without nicotinamide or Sager and Garnick medium supplemented with 3-acetylpyridine. Mutants grows well on media supplied with either nicotinamide or NMN. Addition of nicotinic acid shows very weak rescue of the nic- mutant phenotype. Addition of 3-hydroxyanthranilate cannot rescue the growth defect. Sirtuin SRT2 levels are 2- to 2.5fold increased in the mutant with concomitant increase in reproductive capactiy
C176A
-
complete loss of glutamine-dependent activity, retains 90% of its NH3-dependent activity
C176A
-
activity smilar to wild-type
C176A
site-directed mutagenesis, inactive mutant, analysis of ligand binding structures
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.
Rising, K.A.; Schramm, C.L.
Enzymatic synthesis of NAD+ with the specific incorporation of atomic labels
J. Am. Chem. Soc.
116
6531-6536
1994
Saccharomyces cerevisiae
-
brenda
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
Yu, C.K.; Dietrich, L.S.
Purification and properties of yeast nicotinamide adenine dinucleotide synthetase
J. Biol. Chem.
247
4794-4802
1972
Saccharomyces cerevisiae
brenda
Zerez, C.R.; Wong, M.D.; Tanaka, K.R.
Partial purification and properties of nicotinamide adenine dinucleotide synthetase from human erythrocytes: evidence that enzyme activity is a sensitive indicator of lead exposure
Blood
75
1576-1582
1990
Homo sapiens
brenda
Shibata, K.; Hayakawa, T.; Iwai, K.
Tissue distribution of the enzymes concerned with the biosynthesis of NAD in rats
Agric. Biol. Chem.
50
3037-3041
1986
Rattus norvegicus
-
brenda
Cantoni, R.; Branzoni, M.; Labo, M.; Rizzi, M.; Riccardi, G.
The MTCY428.08 gene of Mycobacterium tuberculosis codes for NAD+ synthetase
J. Bacteriol.
180
3218-3221
1998
Mycobacterium tuberculosis
brenda
Hara, N.; Yamada, K.; Terashima, M.; Osago, H.; Shimoyama, M.; Tsuchiya, M.
Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency
J. Biol. Chem.
278
10914-10921
2003
Homo sapiens (Q6IA69), Homo sapiens
brenda
Bellinzoni, M.; De Rossi, E.; Branzoni, M.; Milano, A.; Peverali, F.A.; Rizzi, M.; Riccardi, G.
Heterologous expression, purification, and enzymatic activity of Mycobacterium tuberculosis NAD(+) synthetase
Protein Expr. Purif.
25
547-557
2002
Mycobacterium tuberculosis
brenda
Bembenek, M.E.; Kuhn, E.; Mallender, W.D.; Pullen, L.; Li, P.; Parsons, T.
A fluorescence-based coupling reaction for monitoring the activity of recombinant human NAD synthetase
Assay Drug Dev. Technol.
3
533-541
2005
Homo sapiens
brenda
Bellinzoni, M.; Buroni, S.; Pasca, M.R.; Guglierame, P.; Arcesi, F.; De Rossi, E.; Riccardi, G.
Glutamine amidotransferase activity of NAD+ synthetase from Mycobacterium tuberculosis depends on an amino-terminal nitrilase domain
Res. Microbiol.
156
173-177
2005
Mycobacterium tuberculosis
brenda
Wojcik, M.; Seidle, H.F.; Bieganowski, P.; Brenner, C.
Glutamine-dependent NAD+ synthetase. How a two-domain, three-substrate enzyme avoids waste
J. Biol. Chem.
281
33395-33402
2006
Saccharomyces cerevisiae
brenda
Boshoff, H.I.; Xu, X.; Tahlan, K.; Dowd, C.S.; Pethe, K.; Camacho, L.R.; Park, T.H.; Yun, C.S.; Schnappinger, D.; Ehrt, S.; Williams, K.J.; Barry, C.E.
Biosynthesis and recycling of nicotinamide cofactors in Mycobacterium tuberculosis. An essential role for NAD in nonreplicating bacilli
J. Biol. Chem.
283
19329-19341
2008
Mycobacterium tuberculosis
brenda
Resto, M.; Yaffe, J.; Gerratana, B.
An ancestral glutamine-dependent NAD(+) synthetase revealed by poor kinetic synergism
Biochim. Biophys. Acta
1794
1648-1653
2009
Thermotoga maritima
brenda
LaRonde-LeBlanc, N.; Resto, M.; Gerratana, B.
Regulation of active site coupling in glutamine-dependent NAD(+) synthetase
Nat. Struct. Mol. Biol.
16
421-429
2009
Mycobacterium tuberculosis
brenda
Sorci, L.; Blaby, I.; De Ingeniis, J.; Gerdes, S.; Raffaelli, N.; de Crecy Lagard, V.; Osterman, A.
Genomics-driven reconstruction of acinetobacter NAD metabolism: insights for antibacterial target selection
J. Biol. Chem.
285
39490-39499
2010
Acinetobacter baumannii, Acinetobacter baumannii (B0V8W9)
brenda
Hager, J.; Pellny, T.K.; Mauve, C.; Lelarge-Trouverie, C.; De Paepe, R.; Foyer, C.H.; Noctor, G.
Conditional modulation of NAD levels and metabolite profiles in Nicotiana sylvestris by mitochondrial electron transport and carbon/nitrogen supply
Planta
231
1145-1157
2010
Nicotiana sylvestris
brenda
Lin, H.; Kwan, A.L.; Dutcher, S.K.
Synthesizing and salvaging NAD: lessons learned from Chlamydomonas reinhardtii
PLoS Genet.
6
e1001105
2010
Chlamydomonas reinhardtii (C4PG67)
brenda
Chuenchor, W.; Doukov, T.I.; Resto, M.; Chang, A.; Gerratana, B.
Regulation of the intersubunit ammonia tunnel in Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase
Biochem. J.
443
417-426
2012
Mycobacterium tuberculosis (P9WJJ3), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WJJ3)
brenda
Laskoski, K.; Santos, A.R.; Bonatto, A.C.; Pedrosa, F.O.; Souza, E.M.; Huergo, L.F.
In vitro characterization of the NAD+ synthetase NadE1 from Herbaspirillum seropedicae
Arch. Microbiol.
198
307-313
2016
Herbaspirillum seropedicae (D8IS59), Herbaspirillum seropedicae, Herbaspirillum seropedicae SmR1 (D8IS59)
brenda