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Information on EC 2.7.7.1 - nicotinamide-nucleotide adenylyltransferase
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EC Tree
2.7.7.1 nicotinamide-nucleotide adenylyltransferaseIUBMB Comments
Nicotinate nucleotide can also act as acceptor. See also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase.
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Word Map
- 2.7.7.1
- degeneration
-
axon
-
wallerian
- neurodegenerative
-
neuroprotective
-
leber
- amaurosis
- nampt
-
self-destruct
-
axotomy
-
axonopathy
- tiazofurin
- medicine
- drug development
- pharmacology
The enzyme appears in viruses and cellular organisms
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine triphosphate-nicotinamide mononucleotide transadenylase
-
-
-
-
adenylyltransferase, nicotinamide mononucleotide
-
-
-
-
Arabidopsis thaliana nicotinate/nicotinamide mononucleotide adenyltransferase
-
ATP:NMN adenylyltransferase
-
-
-
-
diphosphopyridine nucleotide pyrophosphorylase
-
-
-
-
mononucleotide adenylyltransferase
NAD+ pyrophosphorylase
-
-
-
-
NadM-Nudix
NaMNAT
nicotinamide adenine dinucleotide pyrophosphorylase
-
-
-
-
nicotinamide mononucleotide adenylyltransferase
nicotinamide mononucleotide adenylyltransferase 1
nicotinamide mononucleotide adenylyltransferase 2
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
nicotinate/nicotinamide mononucleotide adenyltransferase
NMN adenylyl transferase 1
NMN adenylyltransferase
NMN adenylyltransferase/ADP-ribose pyrophosphatase
NMN AT
NMN/NaMN adenylyltransferase
NMNAT
NMNAT-2
NMNAT1
NMNAT2
NMNAT3
NMNATase
PNAT
-
-
-
-
Pof1
pyridine nucleotide adenylyltransferase
-
-
-
-
Tc00.1047053507047.170
TK0067
additional information
nicotinamide mononucleotide adenylyltransferase
-
-
-
-
nicotinamide mononucleotide adenylyltransferase
-
nicotinamide mononucleotide adenylyltransferase
-
-
nicotinamide mononucleotide adenylyltransferase
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
nicotinamide mononucleotide adenylyltransferase
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
NMN adenylyltransferase
-
-
-
-
NMNAT
-
-
-
-
additional information
the enzyme belongs to the (H/T)IGH motif containing nucleotidyltransferase superfamily, NadM family, bacterial NadM-Nudix subfamily
additional information
the enzyme belongs to the (H/T)IGH motif containing nucleotidyltransferase superfamily, NadM family, bacterial NadM-Nudix subfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + nicotinamide ribonucleotide = diphosphate + NAD+
-
-
-
-
ATP + nicotinamide ribonucleotide = diphosphate + NAD+
catalytic mechanism, overview
ATP + nicotinamide ribonucleotide = diphosphate + NAD+
catalytic mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
nucleotidyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
ATP:nicotinamide-nucleotide adenylyltransferase
Nicotinate nucleotide can also act as acceptor. See also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase.
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CAS REGISTRY NUMBER
COMMENTARY
9032-70-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + nicotinate D-ribonucleotide
diphosphate + nicotinate adenine dinucleotide
-
i.e. nicotinic acid adenine dinucleotide
-
?
ATP + nicotinate mononucleotide
diphosphate + nicotinate adenine dinucleotide
-
-
-
-
?
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
-
-
?
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
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
-
-
?
tiazofurin monophosphate + ATP
tiazofurin adenine dinucleotide + diphosphate
-
-
-
?
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+
?
-
reaction at 76% the rate of nicotinamide ribonucleotide
-
-
?
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+
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
Preiss–Handler-independent pathway
-
-
?
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+
-
final step in biosynthesis of NAD+
-
-
?
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+
Escherichia coli B / ATCC 11303
-
best substrate
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
Escherichia coli B / ATCC 11303
-
reverse reaction at 17% the rate of deamido-NAD+-synthesis
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
Escherichia coli B / ATCC 11303
-
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+
Escherichia coli B / ATCC 11303
-
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
Frog
-
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+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
-
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
?
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+
-
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+
-
i.e. NMN or nicotinamide mononucleotide
-
-
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+
-
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+
-
-
-
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
-
i.e. NMN or nicotinamide mononucleotide
-
-
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+
-
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+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
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+
-
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+
-
-
-
?
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
-
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 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 + nicotinate ribonucleotide
?
-
reaction at 18% the rate of ATP
-
-
?
deoxy-ATP + nicotinate ribonucleotide
?
-
reaction at 30% the rate of ATP
-
-
?
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
Preiss–Handler-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
-
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
?
-
-
NMNAT2 complexes with heat shock protein 90 (HSP90)
-
-
-
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
?
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + tiazofurin
diphosphate + thiazole-4-carboxamide adenine dinucleotide
tiazofurin is a pro-drug that is metabolized by cytosolic nicotinamide mononucleotide adenylyltransferase2
-
-
?
GTP + nicotinamide ribonucleotide
nicotineamide guanine dinucleotide + diphosphate
only isoenzyme NMNAT3
-
-
?
ITP + nicotinamide ribonucleotide
nicotinamide hypoxanthine dinucleotide + diphosphate
only isoenzyme NMNAT3
-
-
?
nicotinate mononucleotide + ATP
nicotinate adenine dinucleotide + diphosphate
Preiss–Handler-dependent pathway
-
-
?
tiazofurin monophosphate + ATP
tiazofurin adenine dinucleotide + diphosphate
-
-
-
?
ATP + nicotinamide mononucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide mononucleotide
diphosphate + NAD+
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
Preiss–Handler-independent pathway
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
-
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+
-
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+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of NAD+
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of 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 + nicotinic acid mononucleotide
diphosphate + deamido-NAD+
-
-
-
?
ATP + nicotinic acid mononucleotide
diphosphate + deamido-NAD+
-
-
-
?
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 from Synechocystis sp. is primarily involved in NAD savage/recycling pathways
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
-
-
-
?
additional information
?
-
-
NAD synthase nicotinamide mononucleotide adenylyltransferase is a stress-response protein that acts as a chaperone for neuronal maintenance and protection
-
-
-
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
?
-
-
NMNAT2 complexes with heat shock protein 90 (HSP90)
-
-
-
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
?
-
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 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
?
-
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
?
-
bifunctional enzyme, that also shows nicotinate-nucleotide adenylyltransferase activity, EC 2.7.7.18
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Cu2+
divalent cations
KCl
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Co2+
-
most effective, 0.5 mM giving the same extent of activation like 10 mM Mg2+
Co2+
isoform NMNAT3 is predominantly activated by Co2+ ions (5 mM)
Co2+
-
10 mM, the enzyme requires divalent cations for the activity. MgCl2 is the most effective additive. can replace Mg2+ with 51% of the activity compared to 10 mM Mg2+
Co2+
-
metal ion required. Order of decreasing effectiveness: Co2+, Ni2+, Mg2+, Zn2+, Mn2+, isoform yNMNAT-2; metal ion required. Order of decreasing effectiveness: Ni2+, Zn2+, Co2+, Mg2+, Mn2+, isoform yNMNAT-1
Cu2+
-
10 mM, the enzyme requires divalent cations for the activity. MgCl2 is the most effective additive. can replace Mg2+ with 28% of the activity compared to 10 mM Mg2+
divalent cations
-
requirement, particularly Mg2+, Co2+ and Ni2+, strong inhibition by some metal ions
Mg2+
presence of a metal ion cluster in the active site of the enzyme's Nudix domain, structure analysis and determination of the metal ion positions
Mg2+
most effective ion with isozymes NMNAT2 and NMNAT3; most effective ion with isozymes NMNAT2 and NMNAT3; most effective ion with isozymes NMNAT2 and NMNAT3; most effective ion with NMNAT2 and NMNAT3; most effective ion with NMNAT2 and NMNAT3; most effective ion with NMNAT2 and NMNAT3
Mg2+
isoform NMNAT2 is predominantly activated by Mg2+ ions (0.5 mM)
Mg2+
-
10 mM, the enzyme requires divalent cations for the activity. MgCl2 is the most effective additive. It can be replaced by CoCl2, ZnCl2, CuCl2, and MnCl2 to some extent
Mg2+
-
metal ion required. Order of decreasing effectiveness: Co2+, Ni2+, Mg2+, Zn2+, Mn2+, isoform yNMNAT-2; metal ion required. Order of decreasing effectiveness: Ni2+, Zn2+, Co2+, Mg2+, Mn2+, isoform yNMNAT-1
Mn2+
presence of a metal ion cluster in the active site of the enzyme's Nudix domain, structure analysis and determination of the metal ion positions
Mn2+
-
10 mM, the enzyme requires divalent cations for the activity. MgCl2 is the most effective additive. can replace Mg2+ with 8% of the activity compared to 10 mM Mg2+
Mn2+
-
metal ion required. Order of decreasing effectiveness: Co2+, Ni2+, Mg2+, Zn2+, Mn2+, isoform yNMNAT-2; metal ion required. Order of decreasing effectiveness: Ni2+, Zn2+, Co2+, Mg2+, Mn2+, isoform yNMNAT-1
Ni2+
-
most effective, 0.5 mM giving the same extent of activation like 10 mM Mg2+
Ni2+
-
metal ion required. Order of decreasing effectiveness: Co2+, Ni2+, Mg2+, Zn2+, Mn2+, isoform yNMNAT-2; metal ion required. Order of decreasing effectiveness: Ni2+, Zn2+, Co2+, Mg2+, Mn2+, isoform yNMNAT-1
Zn2+
most effective ion with isozyme NMNAT1; most effective ion with isozyme NMNAT1; most effective ion with isozyme NMNAT1; most effective ion with NMNAT1; most effective ion with NMNAT1; most effective ion with NMNAT1
Zn2+
isoform NMNAT1 is predominantly activated by Zn2+ ions (0.05 mM)
Zn2+
-
10 mM, the enzyme requires divalent cations for the activity. MgCl2 is the most effective additive. can replace Mg2+ with 30% of the activity compared to 10 mM Mg2+
Zn2+
-
metal ion required. Order of decreasing effectiveness: Co2+, Ni2+, Mg2+, Zn2+, Mn2+, isoform yNMNAT-2; metal ion required. Order of decreasing effectiveness: Ni2+, Zn2+, Co2+, Mg2+, Mn2+, isoform yNMNAT-1
additional information
NMNAT activity requires the presence of divalent cations.; NMNAT activity requires the presence of divalent cations.; NMNAT activity requires the presence of divalent cations.
additional information
NMNAT activity requires the presence of divalent cations.; NMNAT activity requires the presence of divalent cations.; NMNAT activity requires the presence of divalent cations.
additional information
NMNAT activity requires the presence of divalent cations.; NMNAT activity requires the presence of divalent cations.; NMNAT activity requires the presence of divalent cations.
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaAD+
i.e. nicotinic acid adenine dinucleotide, product inhibition, competitive for isozyme NMNAT3, and mixed-type for isozymes NMNAT1 and NMNAT2 NMN, and vice versa against ATP; i.e. nicotinic acid adenine dinucleotide, product inhibition, competitive for isozyme NMNAT3, and mixed-type for isozymes NMNAT1 and NMNAT2 NMN, and vice versa against ATP; i.e. nicotinic acid adenine dinucleotide, product inhibition, competitive for isozyme NMNAT3, and mixed-type for isozymes NMNAT1 and NMNAT2 NMN, and vice versa against ATP
P1-(adenosine-5')-P3-(nicotinamide-riboside-5')-triphosphate
-
P1-(adenosine-5')-P4-(nicotinamide-riboside-5')-tetraphosphate
-
P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate
-
P1-(nicotinamide-riboside-5')-P3-(adenosine-5')-triphosphate
i.e. Np3AD; i.e. Np3AD; i.e. Np3AD
P1-(nicotinamide-riboside-5')-P4-(adenosine-5')-tetraphosphate
i.e. Np4AD; i.e. Np4AD; i.e. Np4AD
P1-(nicotinate-riboside-5')-P4-(adenosine-5')-tetraphosphate
i.e. Nap4AD; i.e. Nap4AD; i.e. Nap4AD
diphosphate
product inhibition, noncompetitive for isozyme NMNAT1, and mixed-type for isozymes NMNAT2 and NMNAT3, both versus ATP and NMN; product inhibition, noncompetitive for isozyme NMNAT1, and mixed-type for isozymes NMNAT2 and NMNAT3, both versus ATP and NMN; product inhibition, noncompetitive for isozyme NMNAT1, and mixed-type for isozymes NMNAT2 and NMNAT3, both versus ATP and NMN
gallotannin
IC50: 0.002 mM, NMNAT3; IC50: 0.01 mM; IC50: 0.055 mM, NMNAT2
-
gallotannin
polyphenolic plant metabolite that inhibits all three human NMNATs; polyphenolic plant metabolite that inhibits all three human NMNATs; polyphenolic plant metabolite that inhibits all three human NMNATs
-
NAD+
product inhibition, competitive for isozyme NMNAT3, and mixed-type for isozymes NMNAT1 and NMNAT2 NMN, and vice versa against ATP; product inhibition, competitive for isozyme NMNAT3, and mixed-type for isozymes NMNAT1 and NMNAT2 NMN, and vice versa against ATP; product inhibition, competitive for isozyme NMNAT3, and mixed-type for isozymes NMNAT1 and NMNAT2 NMN, and vice versa against ATP
P1-(adenosine-5')-P4-(nicotinamide ribose-5')tetraphosphate
-
no effect at 0.1 mM
P1-(adenosine-5')-P4-(nicotinamide ribose-5')tetraphosphate
-
60% inhibition at 0.1 mM
additional information
-
no inhibition by pyrimidine or purine bases, oxy- and deoxynucleosides, cAMP, halogenated and methylated nucleobases, oxy- and deoxyribose, oxy- and deoxyribose 5-phosphate, D-alpha-glucose, D-alpha-glucose 1-phosphate, D-alpha-glucose 6-phosphate, D-alpha-glucose 1,6-diphosphate, D-alpha-fructose, D-alpha-fructose 1,6-diphosphate, alpha-nicotinamide ribonucleotide; product inhibition study
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
epigallocatechin gallate
0.05 mM, 10% activation, NMNAT1; 0.05 mM, 1.4fold activation, NMNAT3; 0.05 mM, 2.28fold activation, NMNAT2
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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
0.0421
ATP
NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3
0.0585
ATP
NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1
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
NMNAT2; pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2; 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
0.189
ATP
pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method
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
0.0252
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
0.1176
nicotinamide ribonucleotide
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
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
NMNAT2; pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2
0.0677
nicotinic acid mononucleotide
NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1
0.111
nicotinic acid mononucleotide
NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3
0.0213
NMN
NMNAT2; pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2
0.0223
NMN
NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1
0.0662
NMN
NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3
0.13
NMNH
NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3
0.294
NMNH
NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1
0.304
NMNH
NMNAT2; pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2
0.37
tiazofurin riboside 5'-monophosphate
pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1
2.1
tiazofurin riboside 5'-monophosphate
pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3
100
tiazofurin riboside 5'-monophosphate
above, pH 7.5, 37°C, isozyme NMNAT2; above, pH 7.5, 37°C, isozyme NMNAT2; above, pH 7.5, 37°C, isozyme NMNAT2
additional information
additional information
initial and steady-state kinetics, kinetic mechanisms of the three NMNAT isozymes, overview; initial and steady-state kinetics, kinetic mechanisms of the three NMNAT isozymes, overview; 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; initial and steady-state kinetics, kinetic mechanisms of the three NMNAT isozymes, overview; 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; initial and steady-state kinetics, kinetic mechanisms of the three NMNAT isozymes, overview; initial and steady-state kinetics, kinetic mechanisms of the three NMNAT isozymes, overview
-
additional information
additional information
-
4.82 Vmax/KM NMN; 7.16 Vmax/KM NaMN
-
additional information
additional information
4.82 Vmax/KM NMN; 7.16 Vmax/KM NaMN
-
additional information
additional information
steady state kinetics
-
additional information
additional information
steady state kinetics
-
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.74
ATP
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.969
ATP
pH 7.4, 37°C, recombinant enzyme, kinetics following Hanes-Woolf method
0.984
ATP
pH 7.4, 37°C, recombinant enzyme, kinetics following Eadie-Hofstee method
1.174
ATP
pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method
2.33
ATP
isoform NMNAT2, in 30 mM HEPES/KOH, pH 7.5, at 37°C
2.5
ATP
pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3
8.8
ATP
pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2
15
ATP
isoform NMNAT1, in 30 mM HEPES/KOH, pH 7.5, at 37°C
53.9
ATP
pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1
0.654
nicotinamide ribonucleotide
-
wild type enzyme, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
0.718
nicotinamide ribonucleotide
pH 7.4, 37°C, recombinant enzyme, kinetics following Hanes-Woolf method
0.73
nicotinamide ribonucleotide
pH 7.4, 37°C, recombinant enzyme, kinetics following Eadie-Hofstee method
0.75
nicotinamide ribonucleotide
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.76
nicotinamide ribonucleotide
pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method
2.87
nicotinamide ribonucleotide
isoform NMNAT2, in 30 mM HEPES/KOH, pH 7.5, at 37°C
2.97 - 3.04
nicotinamide ribonucleotide
pH 7.5, 26°C, recombinant isozyme GlNMNAT-A
7.21
nicotinamide ribonucleotide
-
mutant enzyme C164S/C165S, in 50 mM HEPES-NaOH, pH 7.5, temperature not specified in the publication
15.5
nicotinamide ribonucleotide
isoform NMNAT1, in 30 mM HEPES/KOH, pH 7.5, at 37°C
35.33
nicotinamide ribonucleotide
pH 10.0, 30°C, recombinant enzyme
3.8
nicotinic acid mononucleotide
pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3
6.9
nicotinic acid mononucleotide
pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2
42.9
nicotinic acid mononucleotide
pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1
2.5
NMN
pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3
8.8
NMN
pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2
53.8
NMN
pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1
3.3
NMNH
pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2
7.2
NMNH
pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3
18.6
NMNH
pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1
0.42
tiazofurin riboside 5'-monophosphate
pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3; pH 7.5, 37°C, isozyme NMNAT3
0.55
tiazofurin riboside 5'-monophosphate
pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2; pH 7.5, 37°C, isozyme NMNAT2
14.9
tiazofurin riboside 5'-monophosphate
pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1; pH 7.5, 37°C, isozyme NMNAT1
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.218
ATP
pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method
6.549
ATP
pH 7.4, 37°C, recombinant enzyme, kinetics following Eadie-Hofstee method
7.481
ATP
pH 7.4, 37°C, recombinant enzyme, kinetics following Hanes-Woolf method
20
ATP
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
30
ATP
isoform NMNAT2, in 30 mM HEPES/KOH, pH 7.5, at 37°C
450
ATP
isoform NMNAT1, in 30 mM HEPES/KOH, pH 7.5, at 37°C
0.771
nicotinamide ribonucleotide
pH 7.4, 37°C, recombinant enzyme, kinetics following Lineweaver-Burk method
0.789
nicotinamide ribonucleotide
pH 7.4, 37°C, recombinant enzyme, kinetics following Eadie-Hofstee method
0.951
nicotinamide ribonucleotide
pH 7.4, 37°C, recombinant enzyme, kinetics following Hanes-Woolf method
10
nicotinamide ribonucleotide
isoform NMNAT3, in 30 mM HEPES/KOH, pH 7.5, at 37°C
70
nicotinamide ribonucleotide
isoform NMNAT2, in 30 mM HEPES/KOH, pH 7.5, at 37°C
610
nicotinamide ribonucleotide
isoform NMNAT1, in 30 mM HEPES/KOH, pH 7.5, at 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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; pH 7.5, 37°C, isozyme NMNAT2, versus substrate NMN; 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; pH 7.5, 37°C, isozyme NMNAT2, versus substrate ATP; 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; pH 7.5, 37°C, isozyme NMNAT3, versus substrate ATP; 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; pH 7.5, 37°C, isozyme NMNAT1, versus substrate ATP; 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; pH 7.5, 37°C, isozyme NMNAT3, versus substrate NMN; 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; pH 7.5, 37°C, isozyme NMNAT1, versus substrate NMN; 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; pH 7.5, 37°C, isozyme NMNAT2, versus substrate ATP; 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; pH 7.5, 37°C, isozyme NMNAT2, versus substrate NMN; 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; pH 7.5, 37°C, isozyme NMNAT3, versus substrate ATP; 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; pH 7.5, 37°C, isozyme NMNAT1, versus substrate NMN; 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; pH 7.5, 37°C, isozyme NMNAT1, versus substrate ATP; 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; pH 7.5, 37°C, isozyme NMNAT3, versus substrate NMN; 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; pH 7.5, 37°C, isozyme NMNAT3, versus substrate NaMN; 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; pH 7.5, 37°C, isozyme NMNAT3, versus substrate ATP; 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; pH 7.5, 37°C, isozyme NMNAT1, versus substrate NaMN; 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; pH 7.5, 37°C, isozyme NMNAT3, versus substrate ATP; 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; pH 7.5, 37°C, isozyme NMNAT1, versus substrate ATP; 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; pH 7.5, 37°C, isozyme NMNAT1, versus substrate NMN; 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; pH 7.5, 37°C, isozyme NMNAT1, versus substrate ATP; 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; pH 7.5, 37°C, isozyme NMNAT3, versus substrate NMN; 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; pH 7.5, 37°C, isozyme NMNAT2, versus substrate NaMN; 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; pH 7.5, 37°C, isozyme NMNAT2, versus substrate ATP; 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; pH 7.5, 37°C, isozyme NMNAT2, versus substrate NMN; 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; pH 7.5, 37°C, isozyme NMNAT2, versus substrate ATP; pH 7.5, 37°C, isozyme NMNAT2, versus substrate ATP
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15.4
-
recombinant enzyme, purification step: Superose 12, with dATP as substrate
51
-
recombinant enzyme, purification step: Superose 12, with NMN and ATP as substrate
74.2
76.5
-
recombinant enzyme, purification step: Superose 12, with nicotinic acid mononucleotide as substrate
8.8
74.2
-
recombinant enzyme YLR328W, purification step: phenyl Superose
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
7.4
7.5
7.8 - 8.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 65
-
about half-maximal activity at 30°C and about 60% of maximal activity at 65°C, erythrocytes
37 - 97
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2
4.7 - 4.8
-
isoelectric focusing, LKB 8100 ampholine column filled with a linear gradient of glycerol containing 1% ampholine carrier ampholytes
5.4
5.5
-
isoelectric focusing with either pH 3-10 or pH 4-6 gradient, erythrocytes
6.2
6.2
-
in the presence of 4 M urea, multiple pIs in its absence at pH 4.2, 4.9 and 6.2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
