2.7.7.18: nicotinate-nucleotide adenylyltransferase
This is an abbreviated version!
For detailed information about nicotinate-nucleotide adenylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.18
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2.7.7.18
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anthracis
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falciparum
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plasmodium
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salvage
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adenylylation
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malaria
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broad-spectrum
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nadp
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deamidated
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medicine
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drug development
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analysis
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synthesis
- 2.7.7.18
- anthracis
- falciparum
-
plasmodium
-
salvage
-
adenylylation
-
malaria
-
broad-spectrum
- nadp
-
deamidated
- medicine
- drug development
- analysis
- synthesis
Reaction
Synonyms
adenylyltransferase, nicotinate mononucleotide, Arabidopsis thaliana nicotinate/nicotinamide mononucleotide adenyltransferase, AtNMNAT, deamido-NAD+ pyrophosphorylase, deamidonicotinamide adenine dinucleotide pyrophosphorylase, GlNMNAT, M6_Spy0291, nadD, NaMN AT, NaMN-ATase, NaMNAT, nicotinamide/nicotinate mononucleotide adenylyltransferase, nicotinamide/nicotinic acid mononucleotide adenylyltransferase, nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, nicotinate mononucleotide adenylyltransferase, nicotinate/nicotinamide mononucleotide adenyltransferase, nicotinic acid mononucleotide adenylyltransferase, NMN/NaMN adenylyltransferase, NMN/NaMN adenylyltransferase 2, NMN/NaMN adenylyltransferase 3, NMNAT, NMNAT1, NMNAT2, NMNAT3, PF3D7_1327600, PfNMNAT, sp.NadD, TTHA1780
ECTree
2.7.7.18 nicotinate-nucleotide adenylyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.7.18 - nicotinate-nucleotide adenylyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
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increase in activity, and mutant accepts nicotinamide ribonucleotide as substrate
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Y84V/Y118D
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mutant prefers nicotinamide ribonucleotide over nicotinic acid ribonucleotide bas substrate
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E198P/L217R
mutation disrupts the dimer interface, leading to a mixture of dimer and monomer in solution
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
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
K47A
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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
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P44A
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site-directed mutagenesis, the mutant shows a decrease in Km for ATP
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D110A
site-directed mutagenesis replacing the conserved catalytic site, inactive mutant
additional information
additional information
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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
