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2-fluoro-ATP + deamido-NAD+ + NH3
2-fluoro-AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + Asp
AMP + diphosphate + NAD+ + oxaloacetate
ATP + deamido-NAD+ + Glu
AMP + diphosphate + NAD+ + 2-oxoglutarate
ATP + deamido-NAD+ + glutamine
AMP + diphosphate + glutamate + NAD+
-
-
-
?
ATP + deamido-NAD+ + glutamine
AMP + diphosphate + NAD+ + glutamate
-
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + Glu
ATP + deamido-NAD+ + NH3
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
ATP + deamido-NAD+ + NH4+
AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + NH4+
AMP + diphosphate + NAD+ + H+
-
-
-
?
ATP + deamido-NMN + NH3
AMP + diphosphate + NMN
existence of an alternative route of NAD synthesis where the amidation of NaMN to nicotinamide mononucleotide occurs before the adenylylation reaction, which converts the intermediate to the NAD cofactor. The first step is catalyzed by Francisella tularensis NadE
-
-
?
dATP + deamido-NAD+ + NH3
dAMP + diphosphate + NAD+
additional information
?
-
ATP + deamido-NAD+ + Asp
AMP + diphosphate + NAD+ + oxaloacetate
-
slightly active as nitrogen donor
-
-
?
ATP + deamido-NAD+ + Asp
AMP + diphosphate + NAD+ + oxaloacetate
-
slightly active as nitrogen donor
-
-
?
ATP + deamido-NAD+ + Glu
AMP + diphosphate + NAD+ + 2-oxoglutarate
-
slightly active as nitrogen donor
-
-
?
ATP + deamido-NAD+ + Glu
AMP + diphosphate + NAD+ + 2-oxoglutarate
-
slightly active as nitrogen donor
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + Glu
-
ineffective as amide donor
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + Glu
-
-
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + Glu
-
-
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + Glu
-
-
-
-
?
ATP + deamido-NAD+ + NH3
?
-
-
-
-
?
ATP + deamido-NAD+ + NH3
?
-
last step in the metabolic pathway for the biosynthesis of NAD+
-
-
?
ATP + deamido-NAD+ + NH3
?
-
-
-
-
?
ATP + deamido-NAD+ + NH3
?
-
last step in the metabolic pathway for the biosynthesis of NAD+
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
dependent on NH3
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
NAD-adenylate intermediate, two step reaction
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
NAD-adenylate intermediate, key two step reaction in NAD+ biosynthesis
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
NH3 is the preferred nitrogen donor
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
NH3 is the preferred nitrogen donor
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
-
ir
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
E07950
-
-
ir
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
E07950
specific for NH3, no activity with L-glutamine or other L-amino acids, no activity with urea, uric acid, or creatinine
-
ir
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
E07950
-
-
ir
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
E07950
specific for NH3, no activity with L-glutamine or other L-amino acids, no activity with urea, uric acid, or creatinine
-
ir
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
last step of NAD synthesis
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
no activity with glutamine as the amide donor
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
last step of NAD synthesis
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
no activity with glutamine as the amide donor
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
NH3 is the preferred nitrogen donor
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
?
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
-
-
-
?
dATP + deamido-NAD+ + NH3
dAMP + diphosphate + NAD+
-
20% of the activity relative to ATP
-
-
?
dATP + deamido-NAD+ + NH3
dAMP + diphosphate + NAD+
-
20% of the activity relative to ATP
-
-
?
additional information
?
-
-
2 possible substrates, NH3 or glutamine, to perform the final step in the Preiss-Handler pathway for NAD+ biosynthesis
-
?
additional information
?
-
-
enzyme induces lymphocyte polyclonal activation, it stimulates murine B cells after in vitro treatment of spleen cell cultures
-
?
additional information
?
-
-
enzyme induces lymphocyte polyclonal activation, it stimulates murine B cells after in vitro treatment of spleen cell cultures
-
?
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0.011
1-(4-benzyloxyphenoxy)-8-(2-guanidino-2-phenyl-1-ethyloxy)-octane
Bacillus subtilis
-
in 58.5 mM HEPPS buffer, 18.5 mM NH4Cl, 19.5 mM KCl, 9.75 mM MgCl2, 1% (v/v) EtOH, at pH 8.5
0.011
1-(4-benzyloxyphenoxy)-8-(2-guanidino-3-phenyl-1-propyloxy)-octane
Bacillus subtilis
-
in 58.5 mM HEPPS buffer, 18.5 mM NH4Cl, 19.5 mM KCl, 9.75 mM MgCl2, 1% (v/v) EtOH, at pH 8.5
0.038
1-(4-benzyloxyphenoxy)-8-(2-N,N,N-trimethylammonium-2-phenyl-1-ethyloxy)octane
Bacillus subtilis
-
in 58.5 mM HEPPS buffer, 18.5 mM NH4Cl, 19.5 mM KCl, 9.75 mM MgCl2, 1% (v/v) EtOH, at pH 8.5
0.021
1-(4-benzyloxyphenoxy)-8-(2-N,N,N-trimethylammonium-3-phenyl-1-propyloxy)octane
Bacillus subtilis
-
in 58.5 mM HEPPS buffer, 18.5 mM NH4Cl, 19.5 mM KCl, 9.75 mM MgCl2, 1% (v/v) EtOH, at pH 8.5
0.019
8-(4-benzyloxyphenoxy)-1-octyl 2-(N,N,N-trimethylammonium)-3-(1H-indol-3-yl)propionate
Bacillus subtilis
-
in 58.5 mM HEPPS buffer, 18.5 mM NH4Cl, 19.5 mM KCl, 9.75 mM MgCl2, 1% (v/v) EtOH, at pH 8.5
0.053
8-(4-benzyloxyphenoxy)-1-octyl 2-(N,N,N-trimethylammonium)-3-(4-hydroxyphenyl)propionate
Bacillus subtilis
-
in 58.5 mM HEPPS buffer, 18.5 mM NH4Cl, 19.5 mM KCl, 9.75 mM MgCl2, 1% (v/v) EtOH, at pH 8.5
0.037 - 0.22
8-(4-benzyloxyphenoxy)-1-octyl 2-(N,N,N-trimethylammonium)-3-phenylpropionate
0.045
N-[8-(4-benzyloxyphenoxy)-1-octyl]-2-(N,N,N-trimethylammonium)-2-phenylacetamide
Bacillus subtilis
-
in 58.5 mM HEPPS buffer, 18.5 mM NH4Cl, 19.5 mM KCl, 9.75 mM MgCl2, 1% (v/v) EtOH, at pH 8.5
0.04
N-[8-(4-benzyloxyphenoxy)-1-octyl]-2-(N,N,N-trimethylammonium)-3-phenylpropionamide
Bacillus subtilis
-
in 58.5 mM HEPPS buffer, 18.5 mM NH4Cl, 19.5 mM KCl, 9.75 mM MgCl2, 1% (v/v) EtOH, at pH 8.5
0.019
N-[8-(4-benzyloxyphenoxy)-1-octyl]-2-guanidino-2-phenylacetamide
Bacillus subtilis
-
in 58.5 mM HEPPS buffer, 18.5 mM NH4Cl, 19.5 mM KCl, 9.75 mM MgCl2, 1% (v/v) EtOH, at pH 8.5
0.012
N-[8-(4-benzyloxyphenoxy)-1-octyl]-2-guanidino-3-phenylpropionamide
Bacillus subtilis
-
in 58.5 mM HEPPS buffer, 18.5 mM NH4Cl, 19.5 mM KCl, 9.75 mM MgCl2, 1% (v/v) EtOH, at pH 8.5
0.037
8-(4-benzyloxyphenoxy)-1-octyl 2-(N,N,N-trimethylammonium)-3-phenylpropionate
Bacillus subtilis
-
in 58.5 mM HEPPS buffer, 18.5 mM NH4Cl, 19.5 mM KCl, 9.75 mM MgCl2, 1% (v/v) EtOH, at pH 8.5, in the presence of 0.01% Triton X-100
0.22
8-(4-benzyloxyphenoxy)-1-octyl 2-(N,N,N-trimethylammonium)-3-phenylpropionate
Bacillus subtilis
-
in 58.5 mM HEPPS buffer, 18.5 mM NH4Cl, 19.5 mM KCl, 9.75 mM MgCl2, 1% (v/v) EtOH, at pH 8.5
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0.0003
-
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
0.0027
-
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
0.0033
-
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
0.0043
-
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
0.008
-
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
0.009
-
partially purified recombinant His-tagged enzyme expressed in insect cells, substrate NH4+
0.0143
-
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
0.015
-
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
-
purified recombinant HIs-tagged enzyme expressed in Escherichia coli, substrate glutamine
0.0485
-
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
-
purified recombinant His-tagged enzyme expressed in Escherichia coli, substrate NH4+
0.152
-
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
0.183
-
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
0.25
-
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
0.49
-
purified recombinant His-tagged enzyme
0.631
-
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
0.67
-
purified recombinant His-tagged truncated enzyme expressed in Escherichia coli, substrate NH4+
0.741
-
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
1.5
-
recombinant enzyme, at 37°C
1.59
E07950
purified native enzyme
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hanging drop vapour diffusion method using 8-12% PEG 8000, 0.505 M ammonium sulfate, 6% glycerol, 100 mM magnesium chloride, 0.05% n-octyl-beta-D-glucopyranoside, 100 mM HEPES, pH 7
enzyme in complex with ATP, ATP-Tl+, ATP-Mn2+, or NAD-adenylate, hanging-drop vapour diffusion method, 15 mg/ml protein, 5 mM ATP, 20 mM NAD+ in 0.1 M sodium acetate, pH 5.2, 22% PEG 400, and 50 mM MgCl2, thallium acetate, or MnCl2 20°C, 24 h before data collection the crystale are soaked in a cryoprotectant buffer, X-ray diffraction structure determination at 1.3 A resolution, structure analysis and modeling
free enzyme form at 2.6 A resolution and in a complex with ATP at 2.0 A resolution
-
purified recombinant enzyme complexed with substrates, vapour diffusion method at 5.2 under earth gravity at pH 5.2, and microseeding under space microgravity, the latter in protein solution containing 15 mg/ml protein, 2.5 mM ATP, 5 mM deamido-NAD+, 50 mM Tris, pH 8.5, 50 mM MgCl2, 25% PEG 400 v/v, 9 days, X-ray diffractio structure determination at 1.0 A resolution and analysis of the crystal structures at pH 5.2 and pH 8.5
purified recombinant enzyme, in complex with 4 different substrates: complex I is formed by enzyme and deamido-NAD, complex II is formed by enzyme and ATP, complex III is formed by enzyme, deamido-NAD and ATP, complex is formed by enzyme and substrate analogue alpha,beta-methylene-adenosine triphosphate, crystallization from protein solution: 15 mg/ml protein, 20 mM sodium acetate, pH 5.2, 50 mM MgCl2, 2.5 mM 2-mercaptoethanol, plus equal volume of 0.1 M sodium acetate, pH 5.2, 21-23% PEG 400, 50 mM MgCl2, at room temperature, addition of substrates at different concentrations, formation of complex IV at different pH-values, in the reservoir solution: 50 mM HEPES, pH 7.5, 0.1 M MgCl2, 20-26% PEG 400, 2 mM AMP-CPP, X-ray diffraction structure determination at resolution 1.9-2.3, structure analysis
-
purified recombinant detagged enzyme, sitting drop vapor diffusion method, mixing of 30 mg/ml protein in 0.2 M NaCl, 20 mM Tris-HCl, pH 8.0, 1 mM DTT, 5 mM MgCl2, and 5% glycerol, with reservoir solution containing 20% PEG 4000, 0.2 M lithium sulfate, 0.1 M MES, pH 6.0, 23°C, 3 days, method optimization, X-ray diffraction structure determination and analysis at 2.60 A resolution, molecular replacement
28 mg/ml purified recombinant enzyme, pure or in complex with substrates NAD+ and ATP, hanging-drop vapour diffusion method, 22°C room temperature, protein in 0.01 M HEPES, pH 7.5, 5 mM MgCl2, 3 mM DTT, precipitant solution: 0.1 M HEPES, pH 7.5, 1.5 M lithium sulfate, X-ray diffraction structure determination at 2.0 A resolution, compex structure determination via molecular replacement method
-
crystal structures of the enzyme alone and in complex with natural substrates and with the reaction product NAD+
-
crystal structures of apo- and complex forms with deamido-NAD+ and ATP to a resolution of 2.3 and 1.7 respectively. Hanging drop vapor diffusion method. Crystals of SeMet-containing NAD+ synthase belong to space group C2 with unit cell dimensions of a = 92.3, b = 47.5, c = 64.0, and beta = 110°. Crystals of NAD+ synthetase complexed with deamido-NAD+ belong to space group P3(1), with unit cell dimensions of a = b = 63.4, c = 125.7 A
-
purified recombinant His-tagged enzyme enzyme, hanging drop vapour diffusion method, mixing of 0.002-0.004 ml of 10 mg/ml protein in 20 mM TrisHCl, pH 8.5, 200 mM NaCl, and 5% glycerol, with 0.002-0.004 ml of reservoir solution containing 200 mM CaCl2, 100 mM TrisHCl, pH 7.5, 22% PEG 4000, and equilibration against 0.4 ml of reservoir solution, 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.03 A resolution
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Hughes, K.T.; Baldomero, M.O.; Roth, J.R.
Structural gene for NAD synthetase in Salmonella typhimurium
J. Bacteriol.
170
2113-2120
1988
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Zalkin, H.
NAD synthetase
Methods Enzymol.
113
297-302
1985
Escherichia coli
brenda
Lambrecht, R.H.D.; Slegers, G.; Claeys, A.; Vuye, A.
Purification and immobilization of NAD+ synthetase from Escherichia coli
Enzyme Microb. Technol.
7
493-498
1985
Escherichia coli
-
brenda
Spencer, R.L.; Preiss, J.
Biosynthesis of diphosphopyridine nucleotide. The purification and the properties of diphosphopyridine nucleotide synthetase from Escherichia coli
J. Biol. Chem.
242
385-392
1967
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Rizzi, M.; Nessi, C.; Bolognesi, M.; Coda, A.; Galizzi, A.
Crystallization of NAD+ synthetase from Bacillus subtilis
Proteins Struct. Funct. Genet.
26
236-238
1996
Bacillus subtilis
brenda
Nessi, C.; Albertini, A.M.; Speranza, M.L.; Galizzi, A.
The outB gene of Bacillus subtilis codes for NAD synthetase
J. Biol. Chem.
17
6181-6185
1995
Bacillus subtilis
brenda
Willison, J.C.; Tissot, G.
The Escherichia coli efg gene and the Rhodobacter capsulatus adgA gene code for NH3-dependent NAD synthetase
J. Bacteriol.
176
3400-3402
1994
Escherichia coli, Rhodobacter capsulatus
brenda
Rizzi, M.; Nessi, C.; Mattevi, A.; Coda, A.; Bolognesi, M.; Galizzi, A.
Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis
EMBO J.
15
5125-5134
1996
Bacillus subtilis
brenda
Devedjiev, Y.; Symersky, J.; Singh, R.; Jedrzejas, M.; Brouillette, C.; Brouillette, W.; Muccio, D.; Chattopadhyay, D.; DeLucas, L.
Stabilization of active-site loops in NH3-dependent NAD+ synthetase from Bacillus subtilis
Acta Crystallogr. Sect. D
57
806-812
2001
Bacillus subtilis
brenda
Symersky, J.; Devedjiev, Y.; Moore, K.; Brouillette, C.; DeLucas, L.
NH3-dependent NAD+ synthetase from Bacillus subtilis at 1 A resolution
Acta Crystallogr. Sect. D
58
1138-1146
2002
Bacillus subtilis (P08164), Bacillus subtilis
brenda
Yamaguchi, F.; Koga, S.; Yoshioka, I.; Takahashi, M.; Sakuraba, H.; Ohshima, T.
Stable ammonia-specific NAD synthetase from Bacillus stearothermophilus: purification, characterization, gene cloning, and applications
Biosci. Biotechnol. Biochem.
66
2052-2059
2002
Geobacillus stearothermophilus (E07950), Geobacillus stearothermophilus, Geobacillus stearothermophilus H-804 (E07950)
brenda
Veiga-Malta, I.; Duarte, M.; Dinis, M.; Madureira, P.; Ferreira, P.; Videira, A.
Identification of NAD+ synthetase from Streptococcus sobrinus as a B-cell-stimulatory protein
J. Bacteriol.
186
419-426
2004
Streptococcus sobrinus, Streptococcus sobrinus 6715
brenda
Ozment, C.; Barchue, J.; DeLucas, L.J.; Chattopadhyay, D.
Structural study of Escherichia coli NAD synthetase: overexpression, purification, crystallization, and preliminary crystallographic analysis
J. Struct. Biol.
127
279-282
1999
Escherichia coli
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
Rizzi, M.; Bolognesi, M.; Coda, A.
A novel deamido-NAD+-binding site revealed by the trapped NAD-adenylate intermediate in the NAD+ synthetase structure
Structure
6
1129-1140
1998
Bacillus subtilis (P08164), Bacillus subtilis
brenda
Yamaguchi, F.; Etoh, T.; Takahashi, M.; Misaki, H.; Sakuraba, H.; Ohshima, T.
A new enzymatic cycling method for ammonia assay using NAD synthetase
Clin. Chim. Acta
352
165-173
2005
Geobacillus stearothermophilus
brenda
Jauch, R.; Humm, A.; Huber, R.; Wahl, M.C.
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