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Information on EC 2.7.7.1 - nicotinamide-nucleotide adenylyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A752

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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:
Escherichia coli
UNIPROT: P0A752
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The taxonomic range for the selected organisms is: Escherichia coli
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
NMN/NaMN adenylyltransferase
-
adenosine triphosphate-nicotinamide mononucleotide transadenylase
-
-
-
-
adenylyltransferase, nicotinamide mononucleotide
-
-
-
-
ATP:NMN adenylyltransferase
-
-
-
-
diphosphopyridine nucleotide pyrophosphorylase
-
-
-
-
NAD+ pyrophosphorylase
-
-
-
-
nicotinamide adenine dinucleotide pyrophosphorylase
-
-
-
-
nicotinamide mononucleotide adenylyltransferase
-
-
-
-
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
nicotinate nucleotide can also act as acceptor, see also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
NMN adenylyl transferase 1
-
-
NMN adenylyltransferase
-
-
-
-
NMNAT
PNAT
-
-
-
-
pyridine nucleotide adenylyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
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
-
-
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
show the reaction diagram
-
-
-
r
ATP + 3-acetylpyridine-NAD+
?
show the reaction diagram
-
poor substrate
-
-
?
ATP + 3-pyridinealdehyde-NAD+
?
show the reaction diagram
-
poor substrate
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
ATP + nicotinate ribonucleotide
diphosphate + nicotinic acid-adenine dinucleotide
show the reaction diagram
ATP + nicotinic acid mononucleotide
diphosphate + nicotinic acid adenine dinucleotide
show the reaction diagram
-
-
-
-
r
deoxy-ATP + nicotinamide ribonucleotide
?
show the reaction diagram
-
-
-
-
?
deoxy-ATP + nicotinate ribonucleotide
?
show the reaction diagram
-
reaction at 18% the rate of ATP
-
-
?
nicotinate mononucleotide + ATP
nicotinate adenine dinucleotide + diphosphate
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
-
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
-
activation, 25 mM, NAD+-synthesis, not deamido-NAD+-synthesis
Mg2+
-
requirement
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
deamide-NAD+ as substrate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NH4Cl
-
activation, can substitute for KCl
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
nicotinamide mononucleotide
-
0.5 - 0.52
ATP
-
37°C, pH 7.5
0.0045
deamido-NAD+
-
37°C, pH 7.5
1.1
diphosphate
-
37°C, pH 7.5
0.37
NAD+
-
37°C, pH 7.5
0.147 - 9.4
nicotinamide ribonucleotide
0.08
nicotinate ribonucleotide
-
37°C, pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.76 - 6.6
nicotinamide ribonucleotide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 48
nicotinamide ribonucleotide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0038
-
NAD+-synthesis
0.004
-
NAD+ as substrate
0.024
-
deamido-NAD+ as substrate
0.068
-
deamido-NAD+-synthesis
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A86W/Y118N
increase in activity with nicotinic acid ribonucleotide, and mutant accepts nicotinamide ribonucleotide as substrate
S136D
-
overexpession
W169A
-
catalytically inactive
Y84V/Y118D
mutant prefers nicotinamide ribonucleotide over nicotinic acid ribonucleotide as substrate
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
5 min 54% loss of activity
60
-
5 min 95% loss of activity
PURIFICATION (Commentary)
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
Manually annotated by BRENDA team
Berger, F.; Lau, C.; Ziegler, M.
Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1
Proc. Natl. Acad. Sci. USA
104
3765-3770
2007
Escherichia coli, Homo sapiens
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
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
Manually annotated by BRENDA team
Wang, X.; Zhou, Y.; Wang, L.; Liu, W.; Liu, Y.; Peng, C.; Zhao, Z.
Engineering Escherichia coli nicotinic acid mononucleotide adenylyltransferase for fully active amidated NAD biosynthesis
Appl. Environ. Microbiol.
83
e00692
2017
Escherichia coli (A0A140NE60), Escherichia coli BL21-DE3 (A0A140NE60)
Manually annotated by BRENDA team