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
ECTree
2.7.7.1 nicotinamide-nucleotide adenylyltransferaseAdvanced search results
results (
results (KM Value
KM Value on EC 2.7.7.1 - nicotinamide-nucleotide adenylyltransferase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.0335
ATP
isoform NMNAT1, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.039
ATP
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.082
ATP
isoform NMNAT2, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.08425
ATP
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wild type enzyme, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
0.113
ATP
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mutant enzyme C164S/C165S, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
0.13
ATP
pH 7.4, 37°C, recombinant enzyme, kinetics following Hanes-Woolf method
0.15
ATP
pH 7.4, 37°C, recombinant enzyme, kinetics following Eadie-Hofstee method
0.189
ATP
pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method
0.456
ATP
mutant C41A/C43A, pH not specified in the publication, temperature not specified in the publication
0.525
ATP
wild-type, pH not specified in the publication, temperature not specified in the publication
0.624
ATP
mutant C43A, pH not specified in the publication, temperature not specified in the publication
1.186
ATP
mutant C41A, pH not specified in the publication, temperature not specified in the publication
0.00295
nicotinamide ribonucleotide
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mutant enzyme C164S/C165S, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
0.00691
nicotinamide ribonucleotide
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wild type enzyme, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
0.025
nicotinamide ribonucleotide
mutant C43A, pH not specified in the publication, temperature not specified in the publication
0.0252
nicotinamide ribonucleotide
isoform NMNAT1, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.0385
nicotinamide ribonucleotide
isoform NMNAT2, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.04
nicotinamide ribonucleotide
wild-type, pH not specified in the publication, temperature not specified in the publication
0.1176
nicotinamide ribonucleotide
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.346
nicotinamide ribonucleotide
mutant C41A/C43A, pH not specified in the publication, temperature not specified in the publication
0.753
nicotinamide ribonucleotide
mutant C41A, pH not specified in the publication, temperature not specified in the publication
0.755
nicotinamide ribonucleotide
pH 7.4, 37°C, recombinant enzyme, kinetics following Hanes-Woolf method
0.926
nicotinamide ribonucleotide
pH 7.4, 37°C, recombinant enzyme, kinetics following Eadie-Hofstee method
0.985
nicotinamide ribonucleotide
pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method
2.26
nicotinamide ribonucleotide
pH 10.0, 30°C, recombinant enzyme
2.53 - 2.72
nicotinamide ribonucleotide
pH 7.5, 26°C, recombinant isozyme GlNMNAT-A
0.0145
nicotinic acid mononucleotide
pH 7.5, 37°C, isozyme NMNAT2
0.0677
nicotinic acid mononucleotide
pH 7.5, 37°C, isozyme NMNAT1
0.111
nicotinic acid mononucleotide
pH 7.5, 37°C, isozyme NMNAT3
0.37
tiazofurin riboside 5'-monophosphate
pH 7.5, 37°C, isozyme NMNAT1
2.1
tiazofurin riboside 5'-monophosphate
pH 7.5, 37°C, isozyme NMNAT3
100
tiazofurin riboside 5'-monophosphate
above, pH 7.5, 37°C, isozyme NMNAT2
additional information
additional information
steady state kinetics
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additional information
additional information
steady state kinetics
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additional information
additional information
7.16 Vmax/KM NaMN
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additional information
additional information
initial and steady-state kinetics, kinetic mechanisms of the three NMNAT isozymes, overview
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additional information
additional information
initial and steady-state kinetics, kinetic mechanisms of the three NMNAT isozymes, overview
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additional information
additional information
initial and steady-state kinetics, kinetic mechanisms of the three NMNAT isozymes, overview
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additional information
additional information
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initial and steady-state kinetics, kinetic mechanisms of the three NMNAT isozymes, overview
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additional information
additional information
Michaelis-Menten kinetics are observed for NMN and ATP, but saturation is not accomplished with NAMN, implying low affinity yet detectable activity with this substrate. Double-reciprocal plots show no cooperativity for this enzyme
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