2.7.7.1: nicotinamide-nucleotide adenylyltransferase
This is an abbreviated version!
For detailed information about nicotinamide-nucleotide adenylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.1
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2.7.7.1
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degeneration
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wallerian
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neurodegenerative
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neuroprotective
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amaurosis
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leber
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nampt
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self-destruct
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axotomy
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riboside
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nadase
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tiazofurin
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axonopathies
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pro-degenerative
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analysis
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drug development
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pharmacology
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medicine
- 2.7.7.1
- degeneration
-
wallerian
- neurodegenerative
-
neuroprotective
- amaurosis
-
leber
- nampt
-
self-destruct
-
axotomy
- riboside
- nadase
- tiazofurin
-
axonopathies
-
pro-degenerative
- analysis
- drug development
- pharmacology
- medicine
Reaction
Synonyms
adenosine triphosphate-nicotinamide mononucleotide transadenylase, adenylyltransferase, nicotinamide mononucleotide, Arabidopsis thaliana nicotinate/nicotinamide mononucleotide adenyltransferase, AtNMNAT, ATP:NMN adenylyltransferase, diphosphopyridine nucleotide pyrophosphorylase, Drosophila NMNAT, GlNMNAT, hNMNAT, hNMNAT-1, hNMNAT-2, human nicotinamide mononucleotide adenylyl-transferase, m-nonN-Nmnat1, mononucleotide adenylyltransferase, More, NAD synthase, NAD+ pyrophosphorylase, nadD, NadM-Nudix, NadR, NaMNAT, nicotinamide 5'-mononucleotide adenylyltransferase, nicotinamide 5'-mononucleotide adenylyltransferase-2, nicotinamide 5-mononucleotide adenylyltransferase-2, nicotinamide adenine dinucleotide pyrophosphorylase, nicotinamide mononucleotide adenylyl-transferase, nicotinamide mononucleotide adenylyltransferase, nicotinamide mononucleotide adenylyltransferase 1, nicotinamide mononucleotide adenylyltransferase 2, nicotinamide mononucleotide adenylyltransferase type 1, nicotinamide mononucleotide adenylyltransferase1, nicotinamide mononucleotide adenylyltransferase2, nicotinamide/nicotinate mononucleotide adenylyltransferase, nicotinamide/nicotinic acid mononucleotide adenylyltransferase, nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, nicotinate/nicotinamide mononucleotide adenyltransferase, NMN adenylyl transferase 1, NMN adenylyltransferase, NMN adenylyltransferase/ADP-ribose pyrophosphatase, NMN AT, NMN-adenylyltransferase, NMN/NaMN adenylyltransferase, NMN/NaMN adenylyltransferase 2, NMN/NaMN adenylyltransferase 3, NMNAT, NMNAT-2, NMNAT1, NMNAT2, NMNAT3, NMNATase, non-nuclear-localized-Nmnat1, PF3D7_1327600, PNAT, Pof1, pyridine nucleotide adenylyltransferase, Tc00.1047053507047.170, TK0067, TTHA1780, yNMNAT-1, yNMNAT-2
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2.7.7.1 nicotinamide-nucleotide adenylyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.7.1 - nicotinamide-nucleotide adenylyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A86W/Y118N
increase in activity with nicotinic acid ribonucleotide, and mutant accepts nicotinamide ribonucleotide as substrate
Y84V/Y118D
mutant prefers nicotinamide ribonucleotide over nicotinic acid ribonucleotide as substrate
A86W/Y118N
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increase in activity with nicotinic acid ribonucleotide, 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 as substrate
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C164A/C165A
the isoform NMAT2 mutant is consistently more strongly expressed than the wild type protein
C164S/C165S
the mutant protein is not palmitoylated (soluble), appears diffuse in the cytoplasm and does not colocalize with GM130. However, the mutant is fully active and shows even higher kcat values compared to the wild type enzyme
H24A
protein expressed from the mutant construct is greatly reduced in activity compared with the wild-type protein
W92G
protein expressed from the mutant construct is greatly reduced in activity compared with the wild-type protein
H16A
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slower turnover and higher KM-value for ATP then wild-type
H19A
R11A
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slower turnover and higher KM-value for ATP then wild-type
R11K
R136A
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slower turnover and higher KM-value for ATP then wild-type
R136K
R47E
site-directed mutagenesis, like the wild-type enzyme, the enzyme mutant traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the native enzyme complex
R47K
site-directed mutagenesis, like the wild-type enzyme, the enzyme mutant traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the native enzyme complex
R11K
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site-directed mutagenesis, like the wild-type enzyme, the enzyme mutant traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the native enzyme complex, the mutant shows similar activity and kinetics compared to the wild-type enzyme
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R136K
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site-directed mutagenesis, like the wild-type enzyme, the enzyme mutant traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the native enzyme complex, the mutant shows similar activity and kinetics compared to the wild-type enzyme
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R47E
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site-directed mutagenesis, like the wild-type enzyme, the enzyme mutant traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the native enzyme complex
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R47K
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site-directed mutagenesis, like the wild-type enzyme, the enzyme mutant traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the native enzyme complex
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C164S/C165S
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the mutant protein is not palmitoylated (soluble), appears diffuse in the cytoplasm and does not colocalize with GM130. However, the mutant is fully active and shows even higher kcat values compared to the wild type enzyme
E198P/L217R
mutation disrupts the dimer interface, leading to a mixture of dimer and monomer in solution
WldS(W258A)
the chimeric WldS protein is composed of the N-terminal 70 aa of Ufd2a/Ube4b, an ubiquitin-chain assembly factor, fused to the complete sequence of NMNAT1, the W258A mutation disrupts the NAD-synthesizing activity
additional information
H19A
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slower turnover but lower KM-value for ATP then wild-type
R11K
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slower turnover and higher KM-value for ATP then wild-type
R11K
site-directed mutagenesis, like the wild-type enzyme, the enzyme mutant traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the native enzyme complex, the mutant shows similar activity and kinetics compared to the wild-type enzyme
R136K
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slower turnover and higher KM-value for ATP then wild-type
R136K
site-directed mutagenesis, like the wild-type enzyme, the enzyme mutant traps a molecule of NADP+ in the active site. This NADP+ molecule is bound in a conformation different from that displayed by NAD+ in the native enzyme complex, the mutant shows similar activity and kinetics compared to the wild-type enzyme
additional information
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overexpression of NAD synthase nicotinamide mononucleotide adenylyltransferase protects against spinocerebellar ataxia-induced neurodegeneration
additional information
H1299 human non-small lung cancer cell line, which lacks expression of endogenous p53 due to homozygous partial deletion of the p53 gene, is used to construct a stable cell line expressing wild-type p53 under the control of doxycycline. mRNA levels of NAD+ synthetic enzymes, including NAMPT, NMNAT1, NMNAT2, and NMNAT3, are compared in the presence or absence of p53 by semi-quantitative PCR: only the NMNAT2 mRNA level is significantly elevated by ectopic p53 expression. Although genes NMNAT1 and NMNAT3 are also induced, their expression levels are significantly lower than those of NMNAT?2
additional information
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H1299 human non-small lung cancer cell line, which lacks expression of endogenous p53 due to homozygous partial deletion of the p53 gene, is used to construct a stable cell line expressing wild-type p53 under the control of doxycycline. mRNA levels of NAD+ synthetic enzymes, including NAMPT, NMNAT1, NMNAT2, and NMNAT3, are compared in the presence or absence of p53 by semi-quantitative PCR: only the NMNAT2 mRNA level is significantly elevated by ectopic p53 expression. Although genes NMNAT1 and NMNAT3 are also induced, their expression levels are significantly lower than those of NMNAT?2
additional information
isozyme NMNAT1 knockdown by expression of NMNAT1 specific siRNA. NMNAT1 knockdown promotes glucose starvation-induced cell death
additional information
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isozyme NMNAT1 knockdown by expression of NMNAT1 specific siRNA. NMNAT1 knockdown promotes glucose starvation-induced cell death
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
additional information
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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
additional information
naturally occuring mutant mice, wldS, showing delayed Wallerian degeneration phenotype, suggest that axonal degeneration is an active process, the wldS mutation comprises an 85 kb tandem triplicon, which causes overexpression of the chimeric WldS protein composed of the N-terminal 70 aa of Ufd2a/Ube4b, an ubiquitin-chain assembly factor, fused to the complete sequence of NMNAT1
additional information
naturally occuring mutant mice, wldS, showing delayed Wallerian degeneration phenotype, suggest that axonal degeneration is an active process, the wldS mutation comprises an 85 kb tandem triplicon, which causes overexpression of the chimeric WldS protein composed of the N-terminal 70 aa of Ufd2a/Ube4b, an ubiquitin-chain assembly factor, fused to the complete sequence of NMNAT1
additional information
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naturally occuring mutant mice, wldS, showing delayed Wallerian degeneration phenotype, suggest that axonal degeneration is an active process, the wldS mutation comprises an 85 kb tandem triplicon, which causes overexpression of the chimeric WldS protein composed of the N-terminal 70 aa of Ufd2a/Ube4b, an ubiquitin-chain assembly factor, fused to the complete sequence of NMNAT1
additional information
NMNAT1 overexpression reduces brain infarction size and improves behavioral outcomes in mice with ischemic stroke
additional information
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NMNAT1 overexpression reduces brain infarction size and improves behavioral outcomes in mice with ischemic stroke
additional information
construction of a haploid single gene deletion mutant, cells lacking the ORF YCL047C/POF1 display strong cross-feeding activity
additional information
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construction of a haploid single gene deletion mutant, cells lacking the ORF YCL047C/POF1 display strong cross-feeding activity
additional information
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construction of a haploid single gene deletion mutant, cells lacking the ORF YCL047C/POF1 display strong cross-feeding activity
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