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Information on EC 2.7.7.18 - nicotinate-nucleotide adenylyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A752

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Escherichia coli
UNIPROT: P0A752 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
nicotinate mononucleotide adenylyltransferase, nicotinic acid mononucleotide adenylyltransferase, pfnmnat, namn at, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NMN/NaMN adenylyltransferase
-
adenylyltransferase, nicotinate mononucleotide
-
-
-
-
deamido-NAD+ pyrophosphorylase
-
-
-
-
deamidonicotinamide adenine dinucleotide pyrophosphorylase
-
-
-
-
NaMN AT
-
-
-
-
NaMN-ATase
-
-
-
-
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
-
nicotinic acid mononucleotide adenylyltransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:nicotinate-ribonucleotide adenylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-98-6
-
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
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
i.e. nicotinate mononucleotide
-
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
show the reaction diagram
-
-
-
r
ATP + 3-acetyl-pyridine-NAD+
?
show the reaction diagram
-
poor substrate
-
-
?
ATP + 3-pyridinealdehyde-NAD+
?
show the reaction diagram
-
poor substrate
-
-
?
ATP + beta-nicotinate D-ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
ATP + nicotinic acid mononucleotide
nicotinic acid adenine dinucleotide + diphosphate
show the reaction diagram
-
-
-
-
r
deoxy-ATP + nicotinamide ribonucleotide
?
show the reaction diagram
-
-
-
-
?
deoxy-ATP + nicotinate ribonucleotide
?
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 + nicotinate ribonucleotide
diphosphate + deamido-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
NH4Cl
-
activation, can substitute for KCl
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
deamido-NAD+ as substrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
nicotinamide mononucleotide
-
0.5
ATP
-
37°C, pH 7.5
0.07 - 1.7
beta-nicotinate D-ribonucleotide
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
0.2
nicotinamide ribonucleotide
-
37°C, pH 7.5
0.03 - 0.08
nicotinate ribonucleotide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 25
beta-nicotinate D-ribonucleotide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.86 - 332
beta-nicotinate D-ribonucleotide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0003
-
3-acetyl-pyridine-NAD+ as substrate
0.0008
-
3-pyridinealdehyde-NAD+ as substrate
0.004
-
NAD+ as substrate
0.024
-
deamido-NAD+ as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of the apo-enzyme to space group: P1 with 44% sovent, and in complex with deamido-NAD+ with 42.4% solvent in space group I222, hanging-drop vapour-diffusion method at 20°C in 100 mM Tris, pH 7, 200 mM NaCl and 800 mM sodium citrate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A86W/Y118N
increase in activity, and mutant accepts nicotinamide ribonucleotide as substrate
Y84V/Y118D
mutant prefers nicotinamide ribonucleotide over nicotinic acid ribonucleotide bas substrate
additional information
-
mutation in the nadD gene, renamed nadD72, leads to a temparature-sensitive strain which cannot grow on minimal medium
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
5 min 54% loss of activity
60
-
5 min 95% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-3°C, 31 days stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli BL21 with a 6 x His-tag
expression in Escherichia coli NZN111 with IdhA and pflB genes inactivated for the production of succinic acid
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
overexpression of enzyme gene under anaerobic conditions in a strain lacking IdhA and pflB gene products leads to 3.21fold increase in NAD+ and 1.67fold increase in NADH in the recombinant strain. Enzyme expression restores cell growth and glucose utilization under anaerobic conditions. After 72 h, the recombinant strain can consume 14 g/l of lgucose and produce 6.23 g/l of succinic acid
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Imsande, J.
Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia coli
J. Biol. Chem.
236
1494-1497
1961
Escherichia coli
Manually annotated by BRENDA team
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, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Zhang, H.; Zhou, T.; Kurnasov, O.; Cheek, S.; Grishin, N.V.; Osterman, A.
Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD
Structure
10
69-79
2002
Escherichia coli (P0A752), Escherichia coli
Manually annotated by BRENDA team
Stancek, M.; Isaksson, L.A.; Ryden-Aulin, M.
fusB is an allele of nadD, encoding nicotinate mononucleotide adenylyltransferase in Escherichia coli
Microbiology
149
2427-2433
2003
Escherichia coli
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
Bacillus anthracis, Escherichia coli, Homo sapiens, Pseudomonas aeruginosa
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), Homo sapiens (Q96T66), Saccharomyces cerevisiae (P53204)
Manually annotated by BRENDA team
Gou, D.; Liang, L.; Liu, R.; Zhang, C.; Wu, M.; Ma, J.; Chen, K.; Zhu, J.; Jiang, M.
Effect of overexpression of nicotinic acid mononucleotide adenylyltransferase on succinic acid production in Escherichia coli NZN111
Chin. J. Biotechnol.
28
1059-1069
2012
Escherichia coli
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, Escherichia coli BL21-DE3 (A0A140NE60)
Manually annotated by BRENDA team