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Information on EC 2.7.7.1 - nicotinamide-nucleotide adenylyltransferase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q57961

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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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Methanocaldococcus jannaschii
UNIPROT: Q57961
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Word Map
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
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
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
adenosine triphosphate-nicotinamide mononucleotide transadenylase
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-
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adenylyltransferase, nicotinamide mononucleotide
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-
-
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ATP:NMN adenylyltransferase
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-
-
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diphosphopyridine nucleotide pyrophosphorylase
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-
-
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NAD+ pyrophosphorylase
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-
-
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nicotinamide adenine dinucleotide pyrophosphorylase
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-
-
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nicotinamide mononucleotide adenylyltransferase
NMN adenylyltransferase
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-
-
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NMNAT
PNAT
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-
-
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pyridine nucleotide adenylyltransferase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
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-
PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-70-6
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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
ATP + nicotinic acid mononucleotide
diphosphate + nicotinic acid adenine dinucleotide
show the reaction diagram
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
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
the enzyme plays a key role in NAD+ biosynthesis
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
most effective, 0.5 mM giving the same extent of activation like 10 mM Mg2+
Ni2+
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most effective, 0.5 mM giving the same extent of activation like 10 mM Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
P1-(adenosine-5')-P3-(nicotinamide ribose-5')triphosphate
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-
P1-(adenosine-5')-P4-(nicotinamide ribose-5')tetraphosphate
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60% inhibition at 0.1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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SO42- has no effect
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19600
-
x * 19600, SDS-PAGE
21500
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x * 21500, SDS-PAGE
72000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of the enzyme in complex with ATP are grown using the hanging-drop vapor-diffusion method. The structure in complex with ATP has been solved by X-ray crystallography at 2.0 A resolution, using a combination of single isomorphous replacement and density modification techniques. The structure reveals a hexamer with 32 point group symmetry composed of alpha/beta topology subunits
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
given its vital role in cell life, the enzyme represents a possible target for the development of new antibacterial agents
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Franchetti, P.; Cappellacci, L.; Pasqualini, M.; Grifantini, M.; Lorenzi, T.; Raffaelli, N.; Magni, G.
Dinucleoside polyphosphate NAD analogs as potential NMN adenylyltransferase inhibitors. Synthesis and biological evaluation
Nucleosides Nucleotides Nucleic Acids
22
865-868
2003
Saccharomyces cerevisiae, Homo sapiens, Methanocaldococcus jannaschii
Manually annotated by BRENDA team
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
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
Zhai, R.G.; Rizzi, M.; Garavaglia, S.
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme
Cell. Mol. Life Sci.
66
2805-2818
2009
Synechocystis sp., Bacillus anthracis, Escherichia coli, Haemophilus influenzae, Homo sapiens, Staphylococcus aureus, Pseudomonas aeruginosa, Methanothermobacter thermautotrophicus (O26253), Methanocaldococcus jannaschii (Q57961)
Manually annotated by BRENDA team
D'Angelo, I.; Raffaelli, N.; Dabusti, V.; Lorenzi, T.; Magni, G.; Rizzi, M.
Structure of nicotinamide mononucleotide adenylyltransferase: a key enzyme in NAD(+) biosynthesis
Structure
8
993-1004
2000
Methanocaldococcus jannaschii (Q57961), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q57961)
Manually annotated by BRENDA team