Information on EC 6.3.1.5 - NAD+ synthase

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

EC NUMBER
COMMENTARY hide
6.3.1.5
-
RECOMMENDED NAME
GeneOntology No.
NAD+ synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + deamido-NAD+ + NH3 = AMP + diphosphate + NAD+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid amide hydrolysis
-
-
carboxylic
-
amide bond formation
amide group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
NAD biosynthesis I (from aspartate)
-
-
NAD metabolism
-
-
Nicotinate and nicotinamide metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
Deamido-NAD+:ammonia ligase (AMP-forming)
L-Glutamine also acts, more slowly, as amido-donor [cf. EC 6.3.5.1].
CAS REGISTRY NUMBER
COMMENTARY hide
9032-69-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
-
Q2A4B6
Uniprot
Manually annotated by BRENDA team
H-804
E07950
GenBank
Manually annotated by BRENDA team
strain LT2, wild-type and mutant strains which are defective in NAD synthetase
-
-
Manually annotated by BRENDA team
strain LT2, wild-type and mutant strains which are defective in NAD synthetase
-
-
Manually annotated by BRENDA team
strain 8325-4
-
-
Manually annotated by BRENDA team
strain 6715
-
-
Manually annotated by BRENDA team
strain 6715
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
Q2A4B6
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-fluoro-ATP + deamido-NAD+ + NH3
2-fluoro-AMP + diphosphate + NAD+
show the reaction diagram
-
-
-
-
?
ATP + deamido-NAD+ + Asp
AMP + diphosphate + NAD+ + oxaloacetate
show the reaction diagram
-
slightly active as nitrogen donor
-
-
-
ATP + deamido-NAD+ + Glu
AMP + diphosphate + NAD+ + 2-oxoglutarate
show the reaction diagram
-
slightly active as nitrogen donor
-
-
-
ATP + deamido-NAD+ + glutamine
AMP + diphosphate + glutamate + NAD+
show the reaction diagram
-
-
-
?
ATP + deamido-NAD+ + glutamine
AMP + diphosphate + NAD+ + glutamate
show the reaction diagram
-
-
-
?
ATP + deamido-NAD+ + L-Gln
AMP + diphosphate + NAD+ + Glu
show the reaction diagram
ATP + deamido-NAD+ + NH3
?
show the reaction diagram
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
show the reaction diagram
ATP + deamido-NAD+ + NH4+
AMP + diphosphate + NAD+
show the reaction diagram
-
-
-
-
?
ATP + deamido-NAD+ + NH4+
AMP + diphosphate + NAD+ + H+
show the reaction diagram
-
-
-
?
ATP + deamido-NMN + NH3
AMP + diphosphate + NMN
show the reaction diagram
Q2A4B6
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+
show the reaction diagram
-
20% of the activity relative to ATP
-
-
-
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
ATP + deamido-NAD+ + glutamine
AMP + diphosphate + glutamate + NAD+
show the reaction diagram
-
-
-
?
ATP + deamido-NAD+ + NH3
?
show the reaction diagram
ATP + deamido-NAD+ + NH3
AMP + diphosphate + NAD+
show the reaction diagram
ATP + deamido-NAD+ + NH4+
AMP + diphosphate + NAD+ + H+
show the reaction diagram
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
required, 2 binding sites near the bound diphosphate at the ATP-binding site, can be substituted by Tl+
Mn2+
-
can satisfy the metal ion requirement, Mn2+ is more effective than Mg2+ at low concentrations, at high concentrations Mn2+ markedly inhibits, but Mg2+ does not
Tl+
can substitute for K+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(4-benzyloxyphenoxy)-8-(2-guanidino-2-phenyl-1-ethyloxy)-octane
-
-
1-(4-benzyloxyphenoxy)-8-(2-guanidino-3-phenyl-1-propyloxy)-octane
-
-
1-(4-benzyloxyphenoxy)-8-(2-N,N,N-trimethylammonium-2-phenyl-1-ethyloxy)octane
-
-
1-(4-benzyloxyphenoxy)-8-(2-N,N,N-trimethylammonium-3-phenyl-1-propyloxy)octane
-
-
8-(4-benzyloxyphenoxy)-1-octyl 2-(N,N,N-trimethylammonium)-3-(1H-indol-3-yl)propionate
-
-
8-(4-benzyloxyphenoxy)-1-octyl 2-(N,N,N-trimethylammonium)-3-(4-hydroxyphenyl)propionate
-
-
8-(4-benzyloxyphenoxy)-1-octyl 2-(N,N,N-trimethylammonium)-3-phenylpropionate
-
-
adenosine
-
-
ampicillin
-
-
Ciprofloxacin
-
-
clotrimazole
-
-
Decoyinine
-
-
doxycycline
-
-
Methicillin
-
-
Mg2+
-
slightly inhibiting above 5 mM
Mn2+
-
can satisfy the metal ion requirement at low concentrations, at high concentrations Mn2+ markedly inhibits
N-[8-(4-benzyloxyphenoxy)-1-octyl]-2-(N,N,N-trimethylammonium)-2-phenylacetamide
-
-
N-[8-(4-benzyloxyphenoxy)-1-octyl]-2-(N,N,N-trimethylammonium)-3-phenylpropionamide
-
-
N-[8-(4-benzyloxyphenoxy)-1-octyl]-2-guanidino-2-phenylacetamide
-
-
N-[8-(4-benzyloxyphenoxy)-1-octyl]-2-guanidino-3-phenylpropionamide
-
-
Psicofuranine
-
i.e. 9-D-psicofuranosyl-6-aminopurine, each substrate provides some protection
Rifampin
-
-
thrombin
-
enzyme is highly susceptible too proteolytic cleavage
-
additional information
-
clotrimazole does not inhibit in the presence of 0.01% Triton X-100
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00079 - 0.289
ATP
0.00052 - 5.82
deamido-NAD+
0.2
deamido-NMN
Q2A4B6
-
5
Gln
-
-
0.0011 - 0.0016
glutamine
16
L-Gln
-
-
0.065 - 0.91
NH3
0.025 - 0.027
NH4+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 0.25
deamido-NAD+
0.5
deamido-NMN
Francisella tularensis
Q2A4B6
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
43
deamido-NAD+
Francisella tularensis
Q2A4B6
-
1300
2500
deamido-NMN
Francisella tularensis
Q2A4B6
-
14943
additional information
additional information
Homo sapiens
-
the Vmax/KM-value for NADsyn2 with NH3 is 2370fold higher than the Vmax/Km-value for glutamine
2
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011
1-(4-benzyloxyphenoxy)-8-(2-guanidino-2-phenyl-1-ethyloxy)-octane
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0003
-
mutant enzyme R112L, at 37C, 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 37C, 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 37C, 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 37C, 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 37C, 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 37C, 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 37C, 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 37C, 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 37C, 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 37C, 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 37C, 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 37C, 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
0.503
-
-
0.631
-
mutant enzyme E177A, at 37C, 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 37C, 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 37C
1.59
E07950
purified native enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
-
-
8.4 - 8.6
-
-
8.8
-
with substrate glutamine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
active in a broad pH range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
E07950
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
dormant
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Francisella tularensis subsp. holarctica (strain LVS)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
E07950
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 20C, 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
-
28 mg/ml purified recombinant enzyme, pure or in complex with substrates NAD+ and ATP, hanging-drop vapour diffusion method, 22C 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+
-
to 1.9 A resolution
Q2A4B6
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
E07950
40% of the activity at 60C
95
-
10 min, inactivation
100
-
half-life: 13 min
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
-
inhibitory effects toward the enzyme are decreased in the presence of Triton X-100
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, recombinant truncated enzyme, overnight, loss of 59% activity
-
-70C, recombinant truncated enzyme, overnight, loss of 30% activity
-
-80 - 4C, recombinant full length enzyme, several months
-
25C, recombinant truncated enzyme, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme to homogeneity
E07950
Ni HiTrap column chromatography, and Superdex-200 gel filtration or Superdex-75 gel filtration
Ni-NTA Superflow resin chromatography
-
recombinant as His-tagged enzyme from Escherichia coli
-
recombinant enzyme from Escherichia coli, over 95% purity
-
recombinant His-tagged enzyme and recombinant thioredoxin-His6-fusion protein from Escherichia coli and insect cells, the His-tag is cleaved off afterwards
-
recombinantly overexpressed enzyme, to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, functional overexpression in Escherichia coli
E07950
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells
functional expression in Escherichia coli strain M-15 as His-tagged enzyme, secretion to the medium
-
gene OutB, expression in Escherichia coli BL21(DE3)
-
nadE gene, expression of the enzyme as a His-tagged protein and as a thioredoxin-His6-fusion protein in insect cells of Thrichoplusia ni BTI-TN-5B1-4 via baculovirus infection, for large scale production, and in Escherichia coli
-
overexpression in Escherichia coli
-
overexpression in strain BL21(DE3) as HIs-tagged enzyme
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
-
mutant enzyme with a lower temperature optimum and a non-hyperbolic kinetic versus NH4+
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
pharmacology
-
preparation of isotopically labelled [13N]NAD+, a radiopharmaceutical designed for positron emission tomography, by the NAD+ synthetase immobilized on porous glass beads
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