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Information on EC 2.7.7.1 - nicotinamide-nucleotide adenylyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P53204
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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
-
wallerian
- neurodegenerative
-
neuroprotective
- amaurosis
-
leber
- nampt
-
self-destruct
-
axotomy
- riboside
- nadase
- tiazofurin
-
axonopathies
-
pro-degenerative
- analysis
- drug development
- pharmacology
- medicine
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
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, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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
-
-
-
-
nicotinamide mononucleotide adenylyltransferase
-
-
-
-
NMNAT
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
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
9032-70-6
-
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
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
activity observed with dATP, ITP
-
-
r
ATP + 3-acetylpyridine-NAD+
?
-
reaction at 76% the rate of nicotinamide ribonucleotide
-
-
?
ATP + 3-pyridinealdehyde-NAD+
?
-
reaction at 28% the rate of nicotinamide ribonucleotide
-
-
?
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 + nicotinate ribonucleotide
?
-
reaction at 30% the rate of ATP
-
-
?
GTP + nicotinamide ribonucleotide
diphosphate + nicotinamide guanine dinucleotide
-
isoform yNMNAT-2
-
-
?
ITP + nicotinamide ribonucleotide
diphosphate + nicotinamide hypoxanthine dinucleotide
-
isoform yNMNAT-2
-
-
?
nicotinate mononucleotide + ATP
nicotinate adenine dinucleotide + diphosphate
-
-
-
-
?
tiazofurin + ATP
tiazofurin adenine dinucleotide + diphosphate
-
YLR010W
-
-
?
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 + 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
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
-
-
?
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 + nicotinamide ribonucleotide
diphosphate + NAD+
-
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
-
final step in biosynthesis of NAD+
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Ni2+
Zn2+
Co2+
-
metal ion required. Order of decreasing effectiveness: Co2+, Ni2+, Mg2+, Zn2+, Mn2+, isoform yNMNAT-2
Co2+
-
metal ion required. Order of decreasing effectiveness: Ni2+, Zn2+, Co2+, Mg2+, Mn2+, isoform yNMNAT-1
Mg2+
-
metal ion required. Order of decreasing effectiveness: Co2+, Ni2+, Mg2+, Zn2+, Mn2+, isoform yNMNAT-2
Mg2+
-
metal ion required. Order of decreasing effectiveness: Ni2+, Zn2+, Co2+, Mg2+, Mn2+, isoform yNMNAT-1
Mn2+
-
metal ion required. Order of decreasing effectiveness: Co2+, Ni2+, Mg2+, Zn2+, Mn2+, isoform yNMNAT-2
Mn2+
-
metal ion required. Order of decreasing effectiveness: Ni2+, Zn2+, Co2+, Mg2+, Mn2+, isoform yNMNAT-1
Ni2+
-
metal ion required. Order of decreasing effectiveness: Co2+, Ni2+, Mg2+, Zn2+, Mn2+, isoform yNMNAT-2
Ni2+
-
metal ion required. Order of decreasing effectiveness: Ni2+, Zn2+, Co2+, Mg2+, Mn2+, isoform yNMNAT-1
Zn2+
-
metal ion required. Order of decreasing effectiveness: Co2+, Ni2+, Mg2+, Zn2+, Mn2+, isoform yNMNAT-2
Zn2+
-
metal ion required. Order of decreasing effectiveness: Ni2+, Zn2+, Co2+, Mg2+, Mn2+, isoform yNMNAT-1
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.26
nicotinamide ribonucleotide
pH 10.0, 30°C, recombinant enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
35.33
nicotinamide ribonucleotide
pH 10.0, 30°C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
74.2
74.2
-
recombinant enzyme YLR328W, purification step: phenyl Superose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8 - 8.4
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
-
in the presence of 4 M urea, multiple pIs in its absence at pH 4.2, 4.9 and 6.2
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
195000
200000
48000
50000
-
alpha4, 4 * 50000, SDS-PAGE, with or without 2-mercaptoethanol
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
-
alpha4, 4 * 50000, SDS-PAGE, with or without 2-mercaptoethanol
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of a haploid single gene deletion mutant, cells lacking the ORF YCL047C/POF1 display strong cross-feeding activity
additional information
-
construction of a haploid single gene deletion mutant, cells lacking the ORF YCL047C/POF1 display strong cross-feeding activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 20 mM HEPES buffer, pH 7.5, about 20% loss of activity within 1 month
-
4°C, in 20 mM HEPES buffer, pH 7.5, about 30% loss of activity within 2 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
FPLC reveals microheterogeneity, possibly through poly-ADP-ribosylation of the enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Pof1 or YCL047C, DNA and amino acid sequence determination and analysis, sequence comparisons, construction of the POF1-URA3 episomal plasmid (pRS316-POF1) derived from pADH1-POF1, which is constructed in the integrative pPP81 (LEU2) vector, recombinant expression of His-tagged enzyme from plasmid pET28-POF1 in Escherichia coli strain Rosetta (DE3), quantitative PCR expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
Natalini, P.; Santarelli, I.; Ruggieri, S.; Magni, G.
NMN adenylyltransferase from bakers' yeast: further properties
Ital. J. Biochem.
35
150A-152A
1986
Saccharomyces cerevisiae
-
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
Emanuelli, M.; Carnevali, F.; Lorenzi, M.; Raffaelli, N.; Amici, A.; Ruggieri, S.; Magni, G.
Identification and characterization of YLR328W, the Saccharomyces cerevisiae structural gene encoding NMN adenylyltransferase. Expression and characterization of the recombinant enzyme
FEBS Lett.
455
13-17
1999
Saccharomyces cerevisiae
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
Yalowitz, J.A.; Jayaram, H.N.
Modulation of cytotoxicity of benzamide riboside by expression of NMN adenylyltransferase
Curr. Med. Chem.
9
749-758
2002
Saccharomyces cerevisiae, Homo sapiens, Mammalia, Mus musculus
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
Lau, C.; Niere, M.; Ziegler, M.
The NMN/NaMN adenylyltransferase (NMNAT) protein family
Front. Biosci.
14
410-431
2009
Arabidopsis thaliana, Escherichia coli (P0A752), Saccharomyces cerevisiae (P53204), Homo sapiens (Q96T66), Homo sapiens
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