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ADP + nicotinamide ribonucleotide
NAD+ + phosphate
AMP + nicotinamide ribonucleotide
NAD+
ATP + 3-acetylpyridine-NAD+
?
ATP + 3-pyridinealdehyde-NAD+
?
ATP + beta-NMNH
diphosphate + ?
-
-
-
-
r
ATP + nicotinamide mononucleotide
diphosphate + NAD+
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
ATP + nicotinate D-ribonucleotide
diphosphate + deamino-NAD+
-
-
-
-
?
ATP + nicotinate D-ribonucleotide
diphosphate + nicotinate adenine dinucleotide
-
i.e. nicotinic acid adenine dinucleotide
-
?
ATP + nicotinate mononucleotide
diphosphate + nicotinate adenine dinucleotide
-
-
-
-
?
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
ATP + nicotinic acid mononucleotide
diphosphate + deamido-NAD+
ATP + nicotinic acid mononucleotide
diphosphate + nicotinic acid adenine dinucleotide
ATP + NMN
diphosphate + NAD+
ATP + NMNH
diphosphate + NADH
-
-
-
?
ATP + tiazofurin
diphosphate + thiazole-4-carboxamide adenine dinucleotide
tiazofurin is a pro-drug that is metabolized by cytosolic nicotinamide mononucleotide adenylyltransferase2
-
-
?
ATP + tiazofurin 5'-monophosphate
?
i.e. TrMP, substrate od isozymes NMNAT1 and NMNAT3, but not of isozyme NMNAT2
-
-
?
ATP + tiazofurin monophosphate
?
i.e. TrMP, substrate od isozymes NMNAT1 and NMNAT3, but not of isozyme NMNAT2
-
-
?
CTP + nicotinamide ribonucleotide
diphosphate + nicotinamide cytosine dinucleotide
-
isoform yNMNAT-2
-
-
?
dATP + nicotinamide ribonucleotide
diphosphate + ?
-
isoform yNMNAT-1
-
-
?
dATP + nicotinamide ribonucleotide
diphosphate + nicotinamide deoxyadenosine dinucleotide
-
isoform yNMNAT-2
-
-
?
deoxy-ATP + nicotinamide ribonucleotide
?
deoxy-ATP + nicotinate ribonucleotide
?
diphosphate + NAD+
ATP + nicotinamide ribonucleotide
GTP + nicotinamide ribonucleotide
?
-
-
-
?
GTP + nicotinamide ribonucleotide
diphosphate + NGD+
GTP + nicotinamide ribonucleotide
diphosphate + nicotinamide guanine dinucleotide
-
isoform yNMNAT-2
-
-
?
GTP + nicotinamide ribonucleotide
nicotineamide guanine dinucleotide + diphosphate
only isoenzyme NMNAT3
-
-
?
GTP + NMN
diphosphate + NGD+
substrates of isozyme NMNAT3
i.e. nicotinamide guanosine dinucleotide
-
?
ITP + nicotinamide ribonucleotide
?
-
-
-
?
ITP + nicotinamide ribonucleotide
diphosphate + nicotinamide hypoxanthine dinucleotide
ITP + nicotinamide ribonucleotide
nicotinamide hypoxanthine dinucleotide + diphosphate
only isoenzyme NMNAT3
-
-
?
ITP + NMN
diphosphate + inosine nicotinamide dinucleotide
substrates of isozyme NMNAT3
i.e. nicotinamide hypoxanthine dinucleotide
-
?
nicotinamide hypoxanthine dinucleotide + diphosphate
?
98% of the activity with NAD+, NMNAT3
-
-
?
nicotinamide hypoxanthine dinucleotide + diphosphate
ITP + nicotinamide ribonucleotide
nicotinate mononucleotide + ATP
nicotinate adenine dinucleotide + diphosphate
nicotinic acid adenine dinucleotide phosphate + diphosphate
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
NMN + ATP
NAD+ + diphosphate
-
-
-
?
tiazofurin + ATP
tiazofurin adenine dinucleotide + diphosphate
tiazofurin monophosphate + ATP
tiazofurin adenine dinucleotide + diphosphate
-
-
-
?
additional information
?
-
ADP + nicotinamide ribonucleotide
NAD+ + phosphate
-
at 70°C, ATP is a prominent donor. At 90°C the activity with ADP is 17.5% of the activity with ATP as substrate
-
-
?
ADP + nicotinamide ribonucleotide
NAD+ + phosphate
-
at 70°C, ATP is a prominent donor. At 90°C the activity with ADP is 17.5% of the activity with ATP as substrate
-
-
?
AMP + nicotinamide ribonucleotide
NAD+
-
at 70°C, ATP is a prominent donor. At 90°C the activity with ADP is 50.6% of the activity with ATP as substrate
-
-
?
AMP + nicotinamide ribonucleotide
NAD+
-
at 70°C, ATP is a prominent donor. At 90°C the activity with ADP is 50.6% of the activity with ATP as substrate
-
-
?
ATP + 3-acetylpyridine-NAD+
?
-
poor substrate
-
-
?
ATP + 3-acetylpyridine-NAD+
?
-
reaction at 76% the rate of nicotinamide ribonucleotide
-
-
?
ATP + 3-pyridinealdehyde-NAD+
?
-
poor substrate
-
-
?
ATP + 3-pyridinealdehyde-NAD+
?
-
reaction at 28% the rate of nicotinamide ribonucleotide
-
-
?
ATP + nicotinamide mononucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide mononucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
PreissHandler-independent pathway
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
best substrate
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
reverse reaction at 17% the rate of deamido-NAD+-synthesis
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
no substrates are deamino-NAD+, NADP+, adenosine diphosphoribose, 3-acetylpyridine-deamino-NAD+, 3-pyridinealdehyde-deamino-NAD+, alpha-isomer of NAD+, ITP, GTP, UTP, CTP, or TTP
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
very poor substrate for wild-type
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
best substrate
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
reverse reaction at 17% the rate of deamido-NAD+-synthesis
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
no substrates are deamino-NAD+, NADP+, adenosine diphosphoribose, 3-acetylpyridine-deamino-NAD+, 3-pyridinealdehyde-deamino-NAD+, alpha-isomer of NAD+, ITP, GTP, UTP, CTP, or TTP
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
very poor substrate for wild-type
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
Frog
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
Frog
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
best substrate
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
strongly stereospecific: beta-, not alpha-anomer of nicotinamide ribonucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
key reaction of pyridine nucleotide metabolism
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
central enzyme of NAD biosynthetic pathway
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
NMNAT1
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
NMNAT2
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
NMNAT3
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
the enzyme plays a key role in NAD+ biosynthesis
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
the enzyme plays a key role in NAD+ biosynthesis
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
pheasant
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
pheasant
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
at 70°C, ATP is a prominent donor. However, above 80°C, a relatively small, but significant, NMNAT activity is detected when ATP was replaced by ADP or AMP in the reaction mixture
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
at 70°C, ATP is a prominent donor. However, above 80°C, a relatively small, but significant, NMNAT activity is detected when ATP was replaced by ADP or AMP in the reaction mixture
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
best substrate
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
no substrates are deamino-NAD+, NADP+, adenosine diphosphoribose, 3-acetylpyridine-deamino-NAD+, 3-pyridinealdehyde-deamino-NAD+, alpha-isomer of NAD+, ITP, GTP, UTP, CTP, or TTP
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
isoform yNMNAT-1
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
isoform yNMNAT-2
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
stereochemistry: catalyses nucleotidyl transfer from adenosine (R)-5'-triphosphate to nicotinamide mononucleotide with inversion of configuration at the alpha-phosphate giving (S)-NAD+
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
best substrate
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
Frog
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
less efficient
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
pheasant
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
less efficient
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
-
reaction at 77% the rate of nicotinamide ribonucleotide
-
-
r
ATP + nicotinic acid mononucleotide
diphosphate + deamido-NAD+
-
-
-
r
ATP + nicotinic acid mononucleotide
diphosphate + deamido-NAD+
-
-
-
?
ATP + nicotinic acid mononucleotide
diphosphate + deamido-NAD+
-
-
-
?
ATP + nicotinic acid mononucleotide
diphosphate + nicotinic acid adenine dinucleotide
-
-
-
-
r
ATP + nicotinic acid mononucleotide
diphosphate + nicotinic acid adenine dinucleotide
-
-
-
-
r
ATP + nicotinic acid mononucleotide
diphosphate + nicotinic acid adenine dinucleotide
-
-
-
-
r
ATP + nicotinic acid mononucleotide
diphosphate + nicotinic acid adenine dinucleotide
-
-
-
-
r
ATP + nicotinic acid mononucleotide
diphosphate + nicotinic acid adenine dinucleotide
-
-
-
r
ATP + nicotinic acid mononucleotide
diphosphate + nicotinic acid adenine dinucleotide
-
-
-
r
ATP + nicotinic acid mononucleotide
diphosphate + nicotinic acid adenine dinucleotide
-
-
-
-
r
ATP + nicotinic acid mononucleotide
diphosphate + nicotinic acid adenine dinucleotide
-
-
-
-
r
ATP + nicotinic acid mononucleotide
diphosphate + nicotinic acid adenine dinucleotide
-
-
-
-
r
ATP + NMN
diphosphate + NAD+
the enzyme likely plays a central role in the pathway of NAD de novo synthesis in Francisella tularensis
-
-
?
ATP + NMN
diphosphate + NAD+
the enzyme is a bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase, structural aspects of the catalytic mechanism, overview
-
-
?
ATP + NMN
diphosphate + NAD+
-
-
-
?
ATP + NMN
diphosphate + NAD+
ATP binds before NMN with nuclear isozyme NMNAT1 and Golgi apparatus NMNAT2, but the opposite order is observed with the mitochondrial isozyme NMNAT3
-
-
?
ATP + NMN
diphosphate + NAD+
the enzyme from Synechocystis sp. is primarily involved in NAD savage/recycling pathways
-
-
?
ATP + NMN
diphosphate + NAD+
the enzyme is a bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase, structural aspects of the catalytic mechanism, overview
-
-
?
deoxy-ATP + nicotinamide ribonucleotide
?
-
-
-
-
?
deoxy-ATP + nicotinamide ribonucleotide
?
-
-
-
?
deoxy-ATP + nicotinamide ribonucleotide
?
-
-
-
-
?
deoxy-ATP + nicotinate ribonucleotide
?
-
reaction at 18% the rate of ATP
-
-
?
deoxy-ATP + nicotinate ribonucleotide
?
-
reaction at 30% the rate of ATP
-
-
?
diphosphate + NAD+
ATP + nicotinamide ribonucleotide
-
-
-
r
diphosphate + NAD+
ATP + nicotinamide ribonucleotide
-
-
-
-
r
GTP + nicotinamide ribonucleotide
diphosphate + NGD+
19% of the activity with GTP, reverse reaction with 57% of the activity with NAD+, NMNA3
-
-
r
GTP + nicotinamide ribonucleotide
diphosphate + NGD+
3% of the activity with GTP, reverse reaction with 5% of the activity with NAD+, NMNAT2
-
-
r
GTP + nicotinamide ribonucleotide
diphosphate + NGD+
7% of the activity with GTP, reverse reaction with 26% of the activity with NAD+, NMNAT1
-
-
r
ITP + nicotinamide ribonucleotide
diphosphate + nicotinamide hypoxanthine dinucleotide
27% of the activity with ATP, NMNAT3
-
-
?
ITP + nicotinamide ribonucleotide
diphosphate + nicotinamide hypoxanthine dinucleotide
5% of the activity with ATP, NMNAT2
-
-
?
ITP + nicotinamide ribonucleotide
diphosphate + nicotinamide hypoxanthine dinucleotide
6% of the activity with ATP, NMNAT1
-
-
?
ITP + nicotinamide ribonucleotide
diphosphate + nicotinamide hypoxanthine dinucleotide
-
isoform yNMNAT-2
-
-
?
NADH + diphosphate
?
53% of the activity with NAD+, NMNAT1
-
-
?
NADH + diphosphate
?
98% of the activity with NAD+, NMNAT2
-
-
?
NADH + diphosphate
?
99% of the activity with NAD+, NMNAT3
-
-
?
nicotinamide hypoxanthine dinucleotide + diphosphate
ITP + nicotinamide ribonucleotide
37% of the activity with NAD+, NMNAT2
-
-
?
nicotinamide hypoxanthine dinucleotide + diphosphate
ITP + nicotinamide ribonucleotide
55% of the activity with NAD+, NMNAT1
-
-
?
nicotinate mononucleotide + ATP
nicotinate adenine dinucleotide + diphosphate
PreissHandler-dependent pathway
-
-
?
nicotinate mononucleotide + ATP
nicotinate adenine dinucleotide + diphosphate
-
-
-
-
?
nicotinate mononucleotide + ATP
nicotinate adenine dinucleotide + diphosphate
-
-
-
-
?
nicotinic acid adenine dinucleotide phosphate + diphosphate
?
93% of the activity with NAD+, NMNAT1
-
-
?
nicotinic acid adenine dinucleotide phosphate + diphosphate
?
98% of the activity with NAD+, NMNAT2
-
-
?
nicotinic acid adenine dinucleotide phosphate + diphosphate
?
as active as with NAD+, NMNAT3
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
activity observed with GTP, ITP
-
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
activity observed with dATP, ITP
-
-
r
tiazofurin + ATP
tiazofurin adenine dinucleotide + diphosphate
-
-
-
-
?
tiazofurin + ATP
tiazofurin adenine dinucleotide + diphosphate
-
-
-
?
tiazofurin + ATP
tiazofurin adenine dinucleotide + diphosphate
-
YLR010W
-
-
?
additional information
?
-
-
NAD synthase nicotinamide mononucleotide adenylyltransferase is a stress-response protein that acts as a chaperone for neuronal maintenance and protection
-
-
?
additional information
?
-
-
NAD synthase nicotinamide mononucleotide adenylyltransferase displays chaperone function both in biochemical assays and cultured cells. It is upregulated in the brain upon overexpression of poly-glutamine expanded protein and recruited with the chaperone Hsp70 into protein aggregates.
-
-
?
additional information
?
-
bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18
-
-
?
additional information
?
-
bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18
-
-
?
additional information
?
-
isozyme NMNAT1 directly interacts with nucleolar protein nucleomethylin, NML
-
-
?
additional information
?
-
-
isozyme NMNAT1 directly interacts with nucleolar protein nucleomethylin, NML
-
-
?
additional information
?
-
NMNAT2 complexes with heat shock protein 90 (HSP90)
-
-
?
additional information
?
-
-
bifunctional enzyme, additionally catalyzes the reaction with nicotinate ribonucleotide, reaction of EC 2.7.7.18
-
-
-
additional information
?
-
bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18. The enzyme reversibly catalyzes two closely related reactions: the biosyntheses of NAD+ and its nicotinic acid analogue (NaAD+) from their respective mononucleotide precursors and ATP
-
-
?
additional information
?
-
-
bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18. The enzyme reversibly catalyzes two closely related reactions: the biosyntheses of NAD+ and its nicotinic acid analogue (NaAD+) from their respective mononucleotide precursors and ATP
-
-
?
additional information
?
-
the wild-type enzyme 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 enzyme complex. Binding structure of wild-type and mutant enzymes with NAD+ and NADP+, detailed overview
-
-
?
additional information
?
-
-
the wild-type enzyme 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 enzyme complex. Binding structure of wild-type and mutant enzymes with NAD+ and NADP+, detailed overview
-
-
?
additional information
?
-
bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18. The enzyme reversibly catalyzes two closely related reactions: the biosyntheses of NAD+ and its nicotinic acid analogue (NaAD+) from their respective mononucleotide precursors and ATP
-
-
?
additional information
?
-
the wild-type enzyme 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 enzyme complex. Binding structure of wild-type and mutant enzymes with NAD+ and NADP+, detailed overview
-
-
?
additional information
?
-
-
the following substrates are inert: GDP, CDP, UDP, IDP, GTP, CTP, ITP, IMP, CMP, TTP, and UTP
-
-
?
additional information
?
-
-
the following substrates are inert: GDP, CDP, UDP, IDP, GTP, CTP, ITP, IMP, CMP, TTP, and UTP
-
-
?
additional information
?
-
the amino acid sequence of Pof1 indicates that it is a putative nicotinamide mononucleotide adenylyltransferase (NMNAT). Unlike other yeast NMNATs, Pof1 exhibits NMN-specific adenylyltransferase activity
-
-
?
additional information
?
-
-
the amino acid sequence of Pof1 indicates that it is a putative nicotinamide mononucleotide adenylyltransferase (NMNAT). Unlike other yeast NMNATs, Pof1 exhibits NMN-specific adenylyltransferase activity
-
-
?
additional information
?
-
the amino acid sequence of Pof1 indicates that it is a putative nicotinamide mononucleotide adenylyltransferase (NMNAT). Unlike other yeast NMNATs, Pof1 exhibits NMN-specific adenylyltransferase activity
-
-
?
additional information
?
-
no donors: ADP, AMP, TMP, GMP, CMP, UMP and IMP
-
-
-
additional information
?
-
bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18
-
-
?
additional information
?
-
-
bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18
-
-
?
additional information
?
-
the enzyme shows activity for both NAMN and NMN, substrates used by NMNAT in the presence of ATP to form NAD+ and NAAD, respectively
-
-
?
additional information
?
-
-
the enzyme shows activity for both NAMN and NMN, substrates used by NMNAT in the presence of ATP to form NAD+ and NAAD, respectively
-
-
?
additional information
?
-
bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18
-
-
?
additional information
?
-
the enzyme shows activity for both NAMN and NMN, substrates used by NMNAT in the presence of ATP to form NAD+ and NAAD, respectively
-
-
?
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0.27
3-acetylpyridine-NAD+
-
37°C, pH 7.5
0.74
3-pyridinealdehyde-NAD+
-
37°C, pH 7.5
0.041
ADP-ribose
pH 8.2, 37°C
0.625
beta-NMNH
-
37°C, pH 7.4
0.0045 - 0.029
deamido-NAD+
0.083 - 166.6
diphosphate
0.021 - 0.7
nicotinamide mononucleotide
0.00295 - 178.5
nicotinamide ribonucleotide
0.08
nicotinate D-ribonucleotide
-
nicotinamide ribonucleotide
0.08 - 5
nicotinate ribonucleotide
0.0145 - 0.15
nicotinic acid mononucleotide
0.91
nicotinic acid-adenine dinucleotide
-
37°C, pH 7.4
0.0304
reduced nicotinamide mononucleotide
-
0.055
tiazofurin
-
YGR010W
0.37 - 100
tiazofurin monophosphate
0.37 - 100
tiazofurin riboside 5'-monophosphate
additional information
additional information
-
0.0008
ATP
-
70°C, pH 7.4
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
0.0421
ATP
pH 7.5, 37°C, isozyme NMNAT3
0.0585
ATP
pH 7.5, 37°C, isozyme NMNAT1
0.06
ATP
-
37°C, pH 7.5, + nicotinate ribonucleotide
0.08
ATP
-
65°C, pH 7.5, H19A
0.082
ATP
isoform NMNAT2, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.08425
ATP
-
wild type enzyme, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
0.0889
ATP
pH 7.5, 37°C, isozyme NMNAT2
0.113
ATP
-
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
0.1596
ATP
wild-type, pH 7.5, 42°C
0.16
ATP
-
65°C, pH 7.5, wild-type
0.189
ATP
pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method
0.19
ATP
-
isoform yNMNAT-1
0.21
ATP
-
65°C, pH 7.5, R11K
0.23
ATP
-
+ nicotinamide ribonucleotide, immobilized enzyme
0.33
ATP
-
65°C, pH 7.5, R11A
0.456
ATP
mutant C41A/C43A, pH not specified in the publication, temperature not specified in the publication
0.46
ATP
-
65°C, pH 7.5, R136K
0.5 - 0.52
ATP
-
37°C, pH 7.5
0.5 - 0.52
ATP
-
37°C, pH 7.6
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
1.1
ATP
-
65°C, pH 7.5, H16A
1.18
ATP
-
tiazofurin as second substrate, YGR010W
1.186
ATP
mutant C41A, pH not specified in the publication, temperature not specified in the publication
1.4
ATP
-
65°C, pH 7.5, R136A
1.4
ATP
-
isoform yNMNAT-2
1.48 - 1.52
ATP
pH 7.5, 26°C, recombinant isozyme GlNMNAT-A
1.8209
ATP
mutant R232Q, pH 7.5, 42°C
0.0045
deamido-NAD+
-
37°C, pH 7.5
0.029
deamido-NAD+
-
37°C, pH 7.5
0.083
diphosphate
-
0.083
diphosphate
-
isoform yNMNAT-1
0.125
diphosphate
-
37°C, pH 7.6
0.167
diphosphate
-
37°C, pH 7.4
0.65
diphosphate
-
37°C, pH 7.5
1.1
diphosphate
-
37°C, pH 7.5
5
diphosphate
-
isoform yNMNAT-2
166.6
diphosphate
-
pH 7.4, 20°C
0.023
NAD+
-
isoform yNMNAT-2
0.067 - 0.069
NAD+
-
37°C, pH 7.5
0.067 - 0.069
NAD+
-
37°C, pH 7.6
0.073
NAD+
-
isoform yNMNAT-1
412.2
NAD+
-
pH 7.4, 20°C
0.021
nicotinamide mononucleotide
range 0.021-0.032 mM
0.17
nicotinamide mononucleotide
-
0.7
nicotinamide mononucleotide
-
0.00295
nicotinamide ribonucleotide
-
mutant enzyme C164S/C165S, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
0.00691
nicotinamide ribonucleotide
-
wild type enzyme, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
0.016
nicotinamide ribonucleotide
pH 7.4, 23°C
0.0223
nicotinamide ribonucleotide
wild-type, pH 7.5, 42°C
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
0.03
nicotinamide ribonucleotide
hNMNAT-2
0.032
nicotinamide ribonucleotide
NMNAT2
0.034
nicotinamide ribonucleotide
NMNAT1
0.038
nicotinamide ribonucleotide
-
37°C, pH 7.6
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
0.061
nicotinamide ribonucleotide
-
pH 7.0, 70°C
0.11
nicotinamide ribonucleotide
-
isoform yNMNAT-1
0.1176
nicotinamide ribonucleotide
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.12
nicotinamide ribonucleotide
-
-
0.13
nicotinamide ribonucleotide
-
isoform yNMNAT-2
0.147 - 0.2
nicotinamide ribonucleotide
-
-
0.147 - 0.2
nicotinamide ribonucleotide
-
37°C, pH 7.5
0.147 - 0.2
nicotinamide ribonucleotide
-
37°C, pH 7.6
0.147 - 0.2
nicotinamide ribonucleotide
-
37°C, pH 7.6
0.1789
nicotinamide ribonucleotide
-
pH 7.4, 20°C
0.209
nicotinamide ribonucleotide
NMNAT3
0.263
nicotinamide ribonucleotide
pH 8.0, 37°C
0.28
nicotinamide ribonucleotide
-
immobilized enzyme
0.346
nicotinamide ribonucleotide
mutant C41A/C43A, pH not specified in the publication, temperature not specified in the publication
0.4
nicotinamide ribonucleotide
-
37°C, pH 7.5
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
0.76
nicotinamide ribonucleotide
mutant A86W/Y118N, pH 7.5, 30°C
0.8
nicotinamide ribonucleotide
mutant Y84V/Y118D, pH 7.5, 30°C
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
9.4
nicotinamide ribonucleotide
wild-type, pH 7.5, 30°C
178.5
nicotinamide ribonucleotide
mutant R232Q, pH 7.5, 42°C
0.08
nicotinate ribonucleotide
-
37°C, pH 7.5
0.13
nicotinate ribonucleotide
-
37°C, pH 7.5
5
nicotinate ribonucleotide
-
-
5
nicotinate ribonucleotide
-
37°C, pH 7.6
0.0145
nicotinic acid mononucleotide
NMNAT2
0.0145
nicotinic acid mononucleotide
pH 7.5, 37°C, isozyme NMNAT2
0.015
nicotinic acid mononucleotide
-
0.017
nicotinic acid mononucleotide
-
70°C, pH 7.4
0.0677
nicotinic acid mononucleotide
NMNAT1
0.0677
nicotinic acid mononucleotide
pH 7.5, 37°C, isozyme NMNAT1
0.111
nicotinic acid mononucleotide
NMNAT3
0.111
nicotinic acid mononucleotide
pH 7.5, 37°C, isozyme NMNAT3
0.116
nicotinic acid mononucleotide
-
-
0.116
nicotinic acid mononucleotide
37°C
0.15
nicotinic acid mononucleotide
-
37°C, pH 7.4
0.000019
NMN
-
-
0.000019
NMN
-
37°C, pH 7.6
0.0014
NMN
-
70°C, pH 7.4
0.0213
NMN
pH 7.5, 37°C, isozyme NMNAT2
0.0223
NMN
pH 7.5, 37°C, isozyme NMNAT1
0.0662
NMN
pH 7.5, 37°C, isozyme NMNAT3
0.0719
NMN
-
25°C, pH 8.76
0.0752
NMN
-
25°C, pH 7.95
0.0791
NMN
-
25°C, pH 8.44
0.08
NMN
-
65°C, pH 7.5, wild-type
0.0877
NMN
-
25°C, pH 7.63
0.0879
NMN
-
25°C, pH 7.16
0.09
NMN
-
65°C, pH 7.5, H19A
0.105
NMN
-
25°C, pH 6.21
0.106
NMN
-
25°C, pH 9.55
0.108
NMN
-
25°C, pH 6.66
0.11
NMN
-
65°C, pH 7.5, R136A
0.1129
NMN
-
25°C, pH 9.4
0.13
NMN
-
65°C, pH 7.5, R11K
0.139
NMN
-
25°C, pH 5.85
0.14
NMN
-
65°C, pH 7.5, R136K and R11A
0.187
NMN
-
25°C, pH 5.53
0.2
NMN
-
65°C, pH 7.5, H16A
0.201
NMN
-
25°C, pH 9.77
0.298
NMN
-
25°C, pH 10.35
0.336
NMN
-
25°C, pH 10.55
0.594
NMN
-
25°C, pH 4.95
0.13
NMNH
NMNAT3
0.13
NMNH
pH 7.5, 37°C, isozyme NMNAT3
0.294
NMNH
pH 7.5, 37°C, isozyme NMNAT1
0.304
NMNH
pH 7.5, 37°C, isozyme NMNAT2
0.37
tiazofurin monophosphate
NMNAT1
2.01
tiazofurin monophosphate
NMNAT3
100
tiazofurin monophosphate
NMNAT2
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
-
additional information
additional information
steady state kinetics
-
additional information
additional information
4.82 Vmax/KM NMN
-
additional information
additional information
-
4.82 Vmax/KM NMN
-
additional information
additional information
7.16 Vmax/KM NaMN
-
additional information
additional information
-
7.16 Vmax/KM NaMN
-
additional information
additional information
initial and steady-state kinetics, kinetic mechanisms of the three NMNAT isozymes, overview
-
additional information
additional information
initial and steady-state kinetics, kinetic mechanisms of the three NMNAT isozymes, overview
-
additional information
additional information
initial and steady-state kinetics, kinetic mechanisms of the three NMNAT isozymes, overview
-
additional information
additional information
-
initial and steady-state kinetics, kinetic mechanisms of the three NMNAT isozymes, overview
-
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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0.0315 - 0.089
P1-(adenosine-5')-P3-(nicotinamide-riboside-5')-triphosphate
0.0328 - 0.3283
P1-(adenosine-5')-P3-(nicotinic-acid-riboside-5')-triphosphate
0.0242 - 0.0736
P1-(adenosine-5')-P4-(nicotinamide-riboside-5')-tetraphosphate
0.0217 - 0.6576
P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate
0.0315 - 0.089
P1-(nicotinamide-riboside-5')-P3-(adenosine-5')-triphosphate
0.0242 - 0.0736
P1-(nicotinamide-riboside-5')-P4-(adenosine-5')-tetraphosphate
0.0217 - 0.6576
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
0.16
diphosphate
product inhibition of NMNAT2, substrate NMN
0.175
diphosphate
product inhibition of NMNAT1, substrate ATP
0.334
diphosphate
product inhibition of NMNAT3, substrate ATP
0.361
diphosphate
product inhibition of NMNAT2, substrate ATP
0.39
diphosphate
product inhibition of NMNAT1, substrate NMN
1
diphosphate
product inhibition of NMNAT3, substrate NMN
0.023
NaAD+
product inhibition of NMNAT2, substrate ATP
0.041
NaAD+
product inhibition of NMNAT2, substrate NMN
0.205
NaAD+
product inhibition of NMNAT3, substrate ATP
0.305
NaAD+
product inhibition of NMNAT1, substrate ATP
0.364
NaAD+
product inhibition of NMNAT3, substrate NMN
0.502
NaAD+
product inhibition of NMNAT1, substrate NMN
0.067
NAD+
product inhibition of NMNAT2, substrate NMN
0.095
NAD+
product inhibition of NMNAT2, substrate ATP
0.418
NAD+
product inhibition of NMNAT1, substrate NMN
0.749
NAD+
product inhibition of NMNAT1, substrate ATP
1.017
NAD+
product inhibition of NMNAT3, substrate NMN
1.418
NAD+
product inhibition of NMNAT3, substrate ATP
0.0315
P1-(adenosine-5')-P3-(nicotinamide-riboside-5')-triphosphate
substrate: NMN, isoenzyme: NMNAT2
0.0359
P1-(adenosine-5')-P3-(nicotinamide-riboside-5')-triphosphate
substrate: ATP, isoenzyme: NMNAT2
0.0406
P1-(adenosine-5')-P3-(nicotinamide-riboside-5')-triphosphate
substrate: ATP, isoenzyme: NMNAT3
0.0563
P1-(adenosine-5')-P3-(nicotinamide-riboside-5')-triphosphate
substrate: ATP, isoenzyme: NMNAT1
0.0668
P1-(adenosine-5')-P3-(nicotinamide-riboside-5')-triphosphate
substrate: NMN, isoenzyme: NMNAT3
0.089
P1-(adenosine-5')-P3-(nicotinamide-riboside-5')-triphosphate
substrate: NMN, isoenzyme: NMNAT1
0.0328
P1-(adenosine-5')-P3-(nicotinic-acid-riboside-5')-triphosphate
substrate: ATP, isoenzyme: NMNAT3
0.0591
P1-(adenosine-5')-P3-(nicotinic-acid-riboside-5')-triphosphate
substrate: ATP, isoenzyme: NMNAT1
0.0679
P1-(adenosine-5')-P3-(nicotinic-acid-riboside-5')-triphosphate
substrate: NMN, isoenzyme: NMNAT1
0.0883
P1-(adenosine-5')-P3-(nicotinic-acid-riboside-5')-triphosphate
substrate: NMN, isoenzyme: NMNAT3
0.1745
P1-(adenosine-5')-P3-(nicotinic-acid-riboside-5')-triphosphate
substrate: ATP, isoenzyme: NMNAT2
0.3283
P1-(adenosine-5')-P3-(nicotinic-acid-riboside-5')-triphosphate
substrate: NMN, isoenzyme: NMNAT2
0.0242
P1-(adenosine-5')-P4-(nicotinamide-riboside-5')-tetraphosphate
substrate: ATP, isoenzyme: NMNAT2
0.0258
P1-(adenosine-5')-P4-(nicotinamide-riboside-5')-tetraphosphate
substrate: NMN, isoenzyme: NMNAT2
0.0298
P1-(adenosine-5')-P4-(nicotinamide-riboside-5')-tetraphosphate
substrate: ATP, isoenzyme: NMNAT3
0.0311
P1-(adenosine-5')-P4-(nicotinamide-riboside-5')-tetraphosphate
substrate: NMN, isoenzyme: NMNAT1
0.0492
P1-(adenosine-5')-P4-(nicotinamide-riboside-5')-tetraphosphate
substrate: ATP, isoenzyme: NMNAT1
0.0736
P1-(adenosine-5')-P4-(nicotinamide-riboside-5')-tetraphosphate
substrate: NMN, isoenzyme: NMNAT3
0.0217
P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate
substrate: NMN, isoenzyme: NMNAT3
0.0369
P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate
substrate: NMN, isoenzyme: NMNAT1
0.0431
P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate
substrate: ATP, isoenzyme: NMNAT3
0.0845
P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate
substrate: ATP, isoenzyme: NMNAT1
0.1257
P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate
substrate: NMN, isoenzyme: NMNAT2
0.6576
P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate
substrate: ATP, isoenzyme: NMNAT2
0.0315
P1-(nicotinamide-riboside-5')-P3-(adenosine-5')-triphosphate
pH 7.5, 37°C, isozyme NMNAT2, versus substrate NMN
0.0359
P1-(nicotinamide-riboside-5')-P3-(adenosine-5')-triphosphate
pH 7.5, 37°C, isozyme NMNAT2, versus substrate ATP
0.0406
P1-(nicotinamide-riboside-5')-P3-(adenosine-5')-triphosphate
pH 7.5, 37°C, isozyme NMNAT3, versus substrate ATP
0.0563
P1-(nicotinamide-riboside-5')-P3-(adenosine-5')-triphosphate
pH 7.5, 37°C, isozyme NMNAT1, versus substrate ATP
0.0668
P1-(nicotinamide-riboside-5')-P3-(adenosine-5')-triphosphate
pH 7.5, 37°C, isozyme NMNAT3, versus substrate NMN
0.089
P1-(nicotinamide-riboside-5')-P3-(adenosine-5')-triphosphate
pH 7.5, 37°C, isozyme NMNAT1, versus substrate NMN
0.0242
P1-(nicotinamide-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT2, versus substrate ATP
0.0258
P1-(nicotinamide-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT2, versus substrate NMN
0.0298
P1-(nicotinamide-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT3, versus substrate ATP
0.0311
P1-(nicotinamide-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT1, versus substrate NMN
0.0492
P1-(nicotinamide-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT1, versus substrate ATP
0.0736
P1-(nicotinamide-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT3, versus substrate NMN
0.0217
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT3, versus substrate NaMN
0.0328
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT3, versus substrate ATP
0.0369
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT1, versus substrate NaMN
0.0431
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT3, versus substrate ATP
0.0591
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT1, versus substrate ATP
0.0679
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT1, versus substrate NMN
0.0845
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT1, versus substrate ATP
0.0883
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT3, versus substrate NMN
0.1257
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT2, versus substrate NaMN
0.1745
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT2, versus substrate ATP
0.3283
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT2, versus substrate NMN
0.6576
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
pH 7.5, 37°C, isozyme NMNAT2, versus substrate ATP
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malfunction
-
absisic acid-induced oxidative stress causes stomatal cell death in a nicotinamide mononucleotide adenyltransferase mutant. Stomata partially lose their ability to close leading to drought susceptibility and the stomata are less responsive to opening cues
malfunction
-
enzyme loss results in ubiquitination, mislocalization and aggregation of the Bruchpilot protein, and subsequent active zone degeneration
malfunction
-
nicotinamide mononucleotide adenylyltransferase 2 (Nmat2) homozygous deletion mutants show an approximate 60% reduction of spinal motoneurons in the lumbar region and a more than 80% reduction in the sensory neurons of the dorsal root ganglion. In the absence of Nmnat2, major target organs and tissues (e.g., muscle) are not functionally innervated resulting in perinatal lethality
malfunction
colorectal cancer cells, that exhibit low levels of NMNAT2 and are refractory to tiazofurin, can be rendered sensitive to Tiazofurin by overexpressing NMNAT2
malfunction
deletion of POF1 significantly lowers NAD+ levels and decreases the efficiency of nicotinamide riboside utilization, resistance to oxidative stress, and nicotinamide riboside-induced life span extension
malfunction
gain-of-function mutations in the mouse nicotinamide mononucleotide adenylyltransferase type 1, Nmnat1, produce two remarkable phenotypes: protection against traumatic axonal degeneration and reduced hypoxic brain injury, the mechanism involves the mitochondrial unfolded protein response (mitoUPR) factor, penotype, overview
malfunction
knockdown of NMNAT-2 significantly reduces cellular NAD+ levels and protects cells from p53-dependent cell death upon DNA damage. p53 knockdown abolishes NMNAT-2 expression upon actinomycin D treatment. In NMNAT-2-knockdown cells, actinomycin D treatment does not result in enhanced immunoreactivity
malfunction
NMNAT1 overexpression reduces cell death and apoptosis both in vitro and in vivo. NMNAT1 knockdown exacerbates cell death and apoptosis. NMNAT1 overexpression regulates neuron survival via AMPK activation, as NMNAT1 overexpression enhances AMPKactivity in OGD-treated cortical neurons, and AMPK inhibitor blocks LV-NMNAT1-induced neuroprotection in OGD-treated cortical neurons
malfunction
the chromosomal region encoding the nuclear NAD+ synthesis enzyme NMNAT1 is frequently deleted in human cancer, which may contribute to tumor development. Knockdown of NMNAT1 enhances rRNA transcription and promotes cell death after nutrient deprivation. Heterozygous deletion of NMNAT1 in lung tumor cell lines correlates with low expression level and increased sensitivity to DNA damage. NMNAT1 knockdown stimulates p53 acetylation level before and after DNA damage with doxorubicin
malfunction
-
deletion of POF1 significantly lowers NAD+ levels and decreases the efficiency of nicotinamide riboside utilization, resistance to oxidative stress, and nicotinamide riboside-induced life span extension
-
metabolism
gene expression of NAD+ synthesizing enzymes in the NAD+ salvage pathways can be modulated by p53
metabolism
NAD+ biosynthesis is performed by de novo and salvage pathways, which converge on the step that is catalysed by the enzyme nicotinamide mononucleotide adenylyltransferase, NMNAT
metabolism
nicotinamide mononucleotide adenylyltransferase (NMNAT) catalyzes the biosynthesis of NAD+ and NaAD+
metabolism
NMNAT1 catalyzes NAD+ synthesis in the last step of a salvage synthesis pathway that recycles nicotinamide (NAM) back to NAD+. NMNAT1 deletion in tumors may contribute to transformation by increasing rRNA synthesis, but may also increase sensitivity to nutrient stress and DNA damage
metabolism
the enzyme is essentially involved in the NAD biosynthesis via two different pathways, overview
metabolism
-
NAD+ biosynthesis is performed by de novo and salvage pathways, which converge on the step that is catalysed by the enzyme nicotinamide mononucleotide adenylyltransferase, NMNAT
-
metabolism
-
nicotinamide mononucleotide adenylyltransferase (NMNAT) catalyzes the biosynthesis of NAD+ and NaAD+
-
physiological function
-
NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes
physiological function
-
NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes
physiological function
-
NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes
physiological function
-
NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes
physiological function
-
NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes
physiological function
-
NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes
physiological function
-
NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes
physiological function
NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes
physiological function
NMNAT appears to be a multifunctional protein that sits both at the core of central metabolism and at the crossroads of multiple cellular processes
physiological function
NMNAT1 is an enzyme in the NAD biosynthetic pathway that generates NAD in the nucleus
physiological function
-
nicotinamide mononucleotide adenylyltransferase (NMAT)is a stress response protein regulated by the heat shock factor/hypoxia-inducible factor 1alpha pathway. NMAT is a stress response protein required for thermotolerance and mitigation of oxidative stress-induced shortened lifespan
physiological function
-
nicotinamide mononucleotide adenylyltransferase 2 regulates axon integrity in the mouse embryo
physiological function
-
overexpression of isoform Nmnat2 is toxic to primary neurons resulting in pervasive cell death
physiological function
overexpression of isoform Nmnat2 is toxic to primary neurons resulting in pervasive cell death
physiological function
-
the enzyme has both NAD synthase and chaperone function. The enzyme is essential for maintaining neuronal integrity under normal conditions and protects against several neurodegenerative conditions. Enzyme overexpression significantly suppresses both behavioral and morphological deficits associated with tauopathy by means of reducing the levels of hyperphosphorylated tau oligomers and rescueing age-dependent vacuolization induced by tau expression. The enzyme interacts with phosphorylated tau in vivo and promotes the ubiquitination and clearance of toxic tau species. Apoptosis activation is significantly reduced in brains overexpressing the enzyme, and neurodegeneration is suppressed
physiological function
-
the enzyme is essential for the maintenance of NAD homeostasis enabling sustainable stomatal movement. The enzyme is responsible for tolerance to stressful signalling in guard cells during stomatal closure
physiological function
-
the enzyme is required for maintaining active zone structural integrity in Drosophila by interacting with the active zone protein Bruchpilot and shielding it from activity-induced ubiquitin-proteasome-mediated degradation. The enzyme specifically maintains active zone structure by direct protein-protein interaction
physiological function
the enzyme plays a key role in NAD+ biosynthesis
physiological function
isozyme nicotinamide mononucleotide adenylyltransferase 1 protects neural cells against ischemic injury in primary cultured neuronal cells and mouse brain with ischemic stroke through AMP-activated protein kinase activation. NMNAT1 overexpression reduces brain infarction size and improves behavioral outcomes in mice with ischemic stroke. Role and mechanism of NMNAT1 in the regulation of neural ischemic injuries by using cultured cortical neurons with oxygen-glucose deprivation of ischemic injury in vitro and mouse transient middle cerebral artery occlusion (MCAO) model of stroke in vivo, overview
physiological function
nicotinamide mononucleotide adenylyltransferase (NMNAT1) regulates ribosomal RNA transcription and plays a role in preventing cell death after damage. It interacts with the nucleolar repressor protein nucleomethylin. Isozyme NMNAT1 participates in the regulation of rRNA biosynthesis, possibly by producing a local supply of NAD+. And NMNAT1 may be regulated by recruitment into complexes that consume NAD+. The enzyme is recruited into a ternary complex containing the NAD+-dependent deacetylase SirT1. NMNAT1 expression stimulates the deacetylase function of SirT1 to deacetylate p53. Nucleolar protein nucleomethylin, NML, promotes interaction between SirT1 and NMNAT1, and NMNAT1 is recruited to the nucleolar transcriptional repressor complex eNoSC by NML
physiological function
nicotinamide mononucleotide adenylyltransferase catalyzes the central step in nicotinamide adenine dinucleotide (NAD+) biosynthesis, making it essential for survival
physiological function
the enzyme is a target for the tumor suppressor p53, a major player in cancer signaling pathways, that is an important regulator of cellular metabolism. Determination of an important functional role of NMNAT-2 in p53-mediated signaling. Enzyme NMNAT-2 plays an important role in p53-mediated cell death upon DNA damage
physiological function
tiazofurin is a pro-drug that is metabolized by cytosolic nicotinamide mononucleotide adenylyltransferase2 (NMNAT2) to thiazole-4-carboxamide adenine dinucleotide, a potent inhibitor of inosine 5'-monophosphate dehydrogenase required for cellular guanylate synthesis. Resistance of colorectal cancer cell-kill to Tiazofurin can be overcome by sequentially overexpressing hNMNAT2 and then facilitating the uptake of Tiazofurin by folate-tethered nanoparticles, which enter cells via folate receptors
physiological function
the enzyme nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) acts not only as a NAD synthase involved in axonal maintenance but as a molecular chaperone helping neurons to overcome protein unfolding and protein aggregation, molecular mechanism, overview. NMNAT2 acts as a molecular chaperone that cooperates with HSP90 to refold denatured proteins (foldase activity) and independently prevents protein unfolding (holdase activity). In vertebrates, the isoform NMNAT2, highly expressed in the brain, functions as a cytosolic protein bound to Golgi-derived vesicles through the palmitoylation of several cysteine residues. NMNAT2 seems to be essential for axonal growth or maintenance during embryogenesis. Enzyme NMNAT2 complexes with heat shock protein 90 (HSP90), an abundant and ubiquitous molecular chaperone that plays an essential role in maintaining protein homeostasis
physiological function
the enzyme is involved in the salvage pathways for NAD+ biosynthesis
physiological function
crossing of htau mice, which express non-mutant human tau isoforms and represent a model of tauopathy relevant to Alzheimer's disease, with Nmnat1 transgenic and knockout mice. In the resulting offspring until the age of 6 months, overexpression of NMNAT1 ameliorates the early deficit in food burrowing characteristic of htau mice. At 6 months of age, htau mice do not show neurodegenerative changes in both the cortex and hippocampus, and these are not induced by downregulating NMNAT1 levels. Modulating NMNAT1 levels produces a corresponding effect on NMNAT enzymatic activity but does not alter NAD levels in htau mice
physiological function
Golgi fragmentation in cultured dorsal root ganglion neurons results in caspase dependent axon degeneration and neuronal cell death. NMNAT2 depletion in these neurons causes Golgi fragmentation and caspase dependent axon degeneration. NMNAT2 depletion does not cause ATP loss in the axons. Cytosolic Nmnat1 overexpression inhibits the axon degeneration induced by Golgi fragmentation or NMNAT2 depletion
physiological function
NMNAT overexpression strains show increased colony growth on different carbon sources, and intracellular Ca2+ concentrations are increased by 2- to 2.30fold, respectively, compared with wild-type. In the overexpressing strains, endo-beta-glucanase activity and beta-glucosidase activity are increased
physiological function
NMNAT serves as a chaperone of phosphorylated Tau to prevent its amyloid aggregation in vitro as well as mitigate its pathology in Drosophila tauopathy models overexpressing human Tau. NMNAT adopts its enzymatic pocket to specifically bind the phosphorylated sites of Tau, which can be competitively disrupted by the enzymatic substrates of NMNAT. NMNAT serves as a cochaperone of Hsp90 for the specific recognition of phosphorylated Tau over Tau
physiological function
NMNAT shows strong interaction with phosphorylated truncated Tau protein. The binding affinity of NMNAT3 to phosphorylated Tau is about one order of magnitude higher than that to Tau.The phosphorylated Ser residues of Tau are the primary binding sites. Substrates (i.e. NMN and ATP) and the chaperone client phosphorylated Tau share the same binding pocket with a partial overlap at the phosphate-binding site
physiological function
NMNAT3 is a target and binding partner of sirtuin SIRT3. SIRT3 physically interacts with and deacetylates NMNAT3, thereby enhancing the enzyme activity of NMNAT3 and contributing to SIRT3-mediated anti-hypertrophic effects. NMNAT3 regulates the activity of SIRT3 via synthesis of mitochondrial NAD+
physiological function
-
the enzyme plays a key role in NAD+ biosynthesis
-
physiological function
-
the enzyme is involved in the salvage pathways for NAD+ biosynthesis
-
additional information
residues Arg11 and Arg136 are implicated in binding the phosphate groups of the ATP substrate. Residue Arg47 does not interact with either NMN or ATP substrates directly, but is deemed to play a role in binding as it is proximal to Arg11 and Arg136, plasticity of the active site
additional information
-
residues Arg11 and Arg136 are implicated in binding the phosphate groups of the ATP substrate. Residue Arg47 does not interact with either NMN or ATP substrates directly, but is deemed to play a role in binding as it is proximal to Arg11 and Arg136, plasticity of the active site
additional information
structural homology modeling using human NMNAT3, PDB ID 1NUP, B chain, as a template, overview
additional information
-
structural homology modeling using human NMNAT3, PDB ID 1NUP, B chain, as a template, overview
additional information
-
residues Arg11 and Arg136 are implicated in binding the phosphate groups of the ATP substrate. Residue Arg47 does not interact with either NMN or ATP substrates directly, but is deemed to play a role in binding as it is proximal to Arg11 and Arg136, plasticity of the active site
-
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Dahmen, W.; Webb, B.; Preiss, J.
The deamido-diphosphopyridine nucleotide and diphosphopyridine nucleotide pyrophosphorylases of Escherichia coli and yeast
Arch. Biochem. Biophys.
120
440-450
1967
Escherichia coli, Escherichia coli B / ATCC 11303, Saccharomyces cerevisiae
brenda
Emanuelli, M.; Natalini, P.; Raffaelli, N.; Ruggieri, S.; Vita, A.; Magni, G.
NAD biosynthesis in human placenta: purification and characterization of homogeneous NMN adenylyltransferase
Arch. Biochem. Biophys.
298
29-34
1992
Homo sapiens
brenda
Sestini, S.; Ricci, C.; Micheli, V.; Pompucci, G.
Nicotinamide mononucleotide adenylyltransferase activity in human erythrocytes
Arch. Biochem. Biophys.
302
206-211
1993
Homo sapiens
brenda
Uhr, M.L.; Smulson, M.
NMN adenylyltransferase: its association with chromatin and with poly(ADP-ribose) polymerase
Eur. J. Biochem.
128
435-443
1982
Homo sapiens, Sus scrofa
brenda
Ting, H.H.; Whish, W.J.D.
A preliminary study of immobilized NAD pyrophosphorylase
Biochem. Soc. Trans.
8
635
1980
Sus scrofa
brenda
Atkinson, M.R.; Jackson, J.F.; Morton, R.K.
Nicotinamide mononucleotide adenylyltransferase of pig-liver nuclei: the effects of nicotine mononucleotide concentration and pH on dinucleotide synthesis
Biochem. J.
80
318-323
1961
Sus scrofa
brenda
Ferro, A.M.; Kuehl, L.
Adenosine triphosphate: nicotinamide mononucleotide adenylyltransferase of pig liver. Purification and properties
Biochim. Biophys. Acta
410
285-298
1975
Bos taurus, Rattus norvegicus, Sus scrofa
brenda
Lowe, G.; Tansley, G.
The stereochemical course of nucleotidyl transfer catalysed by NAD pyrophosphorylase
Eur. J. Biochem.
132
117-120
1983
Sus scrofa
brenda
Cantarow, W.; Stollar, B.D.
Nicotinamide mononucleotide adenylytransferase, a nonhistone chromatin protein. Purification and properties of the chicken erythrocyte enzyme
Arch. Biochem. Biophys.
180
26-34
1977
Anser sp., Gallus gallus, Gadidae, Frog, Meleagris gallopavo, pheasant
brenda
Ruggieri, S.; Gregori, L.; Natalini, P.; Vita, A.; Magni, G.
Recent observations on the structure and the properties of yeast NMN adenylyltransferase
Experientia
44
27-29
1988
Saccharomyces cerevisiae
brenda
Natalini, P.; Ruggieri, S.; Raffaelli, N.; Magni, G.
Nicotinamide mononucleotide adenylyltransferase. Molecular and enzymatic properties of the homogeneous enzyme from bakers yeast
Biochemistry
25
3725-3729
1986
Saccharomyces cerevisiae
brenda
Magni, G.; Natalini, P.; Santarelli, I.; Vita, A.; Raffaelli, N.; Ruggieri, S.
NAD pyrophosphorylase from yeast chromatin. Purification and properties
Basic Appl. Histochem.
31
255-271
1987
Saccharomyces cerevisiae
brenda
Natalini, P.; Santarelli, I.; Ruggieri, S.; Magni, G.
NMN adenylyltransferase from bakers' yeast: further properties
Ital. J. Biochem.
35
150A-152A
1986
Saccharomyces cerevisiae
-
brenda
Kono, M.; Shimizu, C.; Matsui, T.; Matsuura, F.
Purification of NAD pyrophosphorylase from muscle of skipjack and its properties
Nippon Suisan Gakkaishi
44
379-384
1978
Katsuwonus pelamis
-
brenda
Balducci, E.; Orsomando, G.; Polzonetti, V.; Vita, A.; Emanuelli, M.; Raffaelli, N.; Ruggieri, S.; Magni, G.; Natalini, P.
NMN adenylyltransferase from bull testis: purification and properties
Biochem. J.
310
395-400
1995
Bos taurus
brenda
Balducci, E.; Emanuelli, M.; Raffaelli, N.; Ruggieri, S.; Amici, A.; Magni, G.; Orsomando, G.; Polzonetti, V.; Natalini, P.
Assay methods for nicotinamide mononucleotide adenylyltransferase of wide applicability
Anal. Biochem.
228
64-68
1995
Bos taurus
brenda
Raffaelli, N.; Sorci, L.; Amici, A.; Emanuelli, M.; Mazzola, F.; Magni, G.
Identification of a novel human nicotinamide mononucleotide adenylyltransferase
Biochem. Biophys. Res. Commun.
297
835-840
2002
Homo sapiens
brenda
Zhang, X.; Kurnasov, O.V.; Karthikeyan, S.; Grishin, N.V.; Osterman, A.L.; Zhang, H.
Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis
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278
13503-13511
2003
Homo sapiens
brenda
Garavaglia, S.; D'Angelo, I.; Emanuelli, M.; Carnevali, F.; Pierella, F.; Magni, G.; Rizzi, M.
Structure of human NMN adenylyltransferase. A key nuclear enzyme for NAD homeostasis
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277
8524-8530
2002
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Homo sapiens (Q9BZQ4), Homo sapiens
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Homo sapiens (Q9BZQ4)
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Mem. Inst. Oswaldo Cruz
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Trypanosoma cruzi, Trypanosoma cruzi CL Brener
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Homo sapiens (Q9HAN9)
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