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Information on EC 2.7.7.1 - nicotinamide-nucleotide adenylyltransferase and Organism(s) Saccharolobus solfataricus and UniProt Accession P57084

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IUBMB Comments
Nicotinate nucleotide can also act as acceptor. See also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase.
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This record set is specific for:
Saccharolobus solfataricus
UNIPROT: P57084
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Word Map
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
Synonyms
nmnat2, nmnat, nmnat1, nmnat3, nicotinamide mononucleotide adenylyltransferase, nmn adenylyltransferase, nicotinamide mononucleotide adenylyltransferase 1, nicotinamide mononucleotide adenylyltransferase 2, namnat, hnmnat-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosine triphosphate-nicotinamide mononucleotide transadenylase
-
-
-
-
adenylyltransferase, nicotinamide mononucleotide
-
-
-
-
ATP:NMN adenylyltransferase
-
-
-
-
diphosphopyridine nucleotide pyrophosphorylase
-
-
-
-
NAD+ pyrophosphorylase
-
-
-
-
nicotinamide adenine dinucleotide pyrophosphorylase
-
-
-
-
nicotinamide mononucleotide adenylyltransferase
NMN adenylyltransferase
-
-
-
-
NMNAT
PNAT
-
-
-
-
pyridine nucleotide adenylyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-70-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
i.e. NMN or nicotinamide mononucleotide
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
show the reaction diagram
i.e. nicotinate mononucleotide
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
show the reaction diagram
-
i.e. nicotinate mononucleotide
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
-
final step in biosynthesis of NAD+
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SO42-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008
ATP
-
70°C, pH 7.4
0.017
nicotinic acid mononucleotide
-
70°C, pH 7.4
0.0014
NMN
-
70°C, pH 7.4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 97
activity shows a continuous increase up to 97°C
37 - 97
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18600
x * 18600, SDS-PAGE
18600
-
x * 18600, SDS-PAGE
66000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 18600, SDS-PAGE
?
-
x * 18600, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
stable at least 2 h
90
-
half-life is 30 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
chaotropic anions are strong destabilizers of the enzyme
increasing ionic strenght of NaCl and KCl stabilizes the thermal stability of the enzyme
chaotropic anions are strong destabilizers of the enzyme
-
dithiothreitol has no effect up to 50°C but destabilizes the enzyme at higher temperatures
-
increasing ionic strenght of NaCl and KCl stabilizes the thermal stability of the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several weeks without loss in activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Raffaelli, N.; Pisani, F.M.; Lorenzi, T.; Emanuelli, M.; Amici, A.; Ruggieri, S.; Magni, G.
Nicotinamide-mononucleotide adenylyltransferase from Methanococcus jannaschii
Methods Enzymol.
331
292-298
2001
Methanocaldococcus jannaschii, Saccharolobus solfataricus
Manually annotated by BRENDA team
Magni, G.; Raffaelli, N.; Emanuelli, M.; Amici, A.; Natalini, P.; Ruggieri, S.
Nicotinamide-mononucleotide adenylyltransferases from yeast and other microorganisms
Methods Enzymol.
280
248-255
1997
Saccharomyces cerevisiae, Saccharolobus solfataricus
Manually annotated by BRENDA team
Raffaelli, N.; Lorenzi, T.; Emanuelli, M.; Amici, A.; Ruggieri, S.; Magni, G.
Nicotinamide-mononucleotide adenylyltransferase from Sulfolobus solfataricus
Methods Enzymol.
331
281-292
2001
Saccharolobus solfataricus
Manually annotated by BRENDA team
Raffaelli, N.; Amici, A.; Emanuelli, M.; Ruggieri, S.; Magni, G.
Pyridine dinucleotide biosynthesis in archaebacteria: presence of NMN adenylyltransferase in Sulfolobus solfataricus
FEBS Lett.
355
233-236
1994
Saccharolobus solfataricus
Manually annotated by BRENDA team
Raffaelli, N.; Pisani, F.M.; Lorenzi, T.; Emanuelli, M.; Amici, A.; Ruggieri, S.; Magni, G.
Characterization of nicotinamide mononucleotide adenylyltransferase from thermophilic archaea
J. Bacteriol.
179
7718-7723
1997
Methanocaldococcus jannaschii, Saccharolobus solfataricus (P57084), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (P57084)
Manually annotated by BRENDA team
Magni, G.; Amici, A.; Emanuelli, M.; Orsomando, G.; Raffaelli, N.; Ruggieri, S.
Structure and function of nicotinamide mononucleotide adenylyltransferase
Curr. Med. Chem.
11
873-885
2004
Bacillus subtilis, Bos taurus, Haemophilus influenzae, Homo sapiens, Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus, Saccharolobus solfataricus, Saccharomyces cerevisiae
Manually annotated by BRENDA team