Information on EC 2.7.7.18 - nicotinate-nucleotide adenylyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.7.7.18
-
RECOMMENDED NAME
GeneOntology No.
nicotinate-nucleotide adenylyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + beta-nicotinate D-ribonucleotide = diphosphate + deamido-NAD+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NAD biosynthesis from 2-amino-3-carboxymuconate semialdehyde
-
-
NAD biosynthesis I (from aspartate)
-
-
NAD salvage pathway I
-
-
pyridine nucleotide cycling (plants)
-
-
NAD metabolism
-
-
Nicotinate and nicotinamide metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:nicotinate-ribonucleotide adenylyltransferase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
adenylyltransferase, nicotinate mononucleotide
-
-
-
-
Arabidopsis thaliana nicotinate/nicotinamide mononucleotide adenyltransferase
-
-
deamido-NAD+ pyrophosphorylase
-
-
-
-
deamidonicotinamide adenine dinucleotide pyrophosphorylase
-
-
-
-
M6_Spy0291
locus name
M6_Spy0291
Streptococcus pyogenes ATCC BAA-946
locus name
-
nadD
-
gene name
NaMN AT
-
-
-
-
NaMN-ATase
-
-
-
-
NaMNAT
Methanothermobacter thermautotrophicum, Staphylococcus aureus
-
-
nicotinamide/nicotinic acid mononucleotide adenylyltransferase
-
-
nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
-
-
nicotinate/nicotinamide mononucleotide adenyltransferase
-
-
nicotinic acid mononucleotide adenylyltransferase
-
-
-
-
nicotinic acid mononucleotide adenylyltransferase
-
nicotinic acid mononucleotide adenylyltransferase
Bacillus subtilis, Methanothermobacter thermautotrophicum
-
-
nicotinic acid mononucleotide adenylyltransferase
-
-
nicotinic acid mononucleotide adenylyltransferase
-
-
NMN/NaMN adenylyltransferase
-
-
NMN/NaMN adenylyltransferase
gene nadD
NMN/NaMN adenylyltransferase 2
-
NMN/NaMN adenylyltransferase 3
-
sp.NadD
Streptococcus pyogenes ATCC BAA-946
gene name
-
CAS REGISTRY NUMBER
COMMENTARY
9026-98-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene nadD
UniProt
Manually annotated by BRENDA team
probable
UniProt
Manually annotated by BRENDA team
Bacillus anthracis CDC 684
probable
UniProt
Manually annotated by BRENDA team
strains K-12 or B <3>
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
isoform NMNAT1
SwissProt
Manually annotated by BRENDA team
isoform NMNAT2
SwissProt
Manually annotated by BRENDA team
isoform NMNAT3
SwissProt
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicum
-
-
-
Manually annotated by BRENDA team
tobacco, cv. Samsun or cv. Xanthi
-
-
Manually annotated by BRENDA team
brewer's yeast
-
-
Manually annotated by BRENDA team
serotype M6
UniProt
Manually annotated by BRENDA team
Streptococcus pyogenes ATCC BAA-946
serotype M6
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 3-acetyl-pyridine-NAD+
?
show the reaction diagram
-
poor substrate
-
-
?
ATP + 3-acetyl-pyridine-NAD+
?
show the reaction diagram
-
reaction at 76% the rate of nicotinamide ribonucleotide
-
-
?
ATP + 3-pyridinealdehyde-NAD+
?
show the reaction diagram
-
poor substrate
-
-
?
ATP + 3-pyridinealdehyde-NAD+
?
show the reaction diagram
-
reaction at 28% the rate of nicotinamide ribonucleotide
-
-
?
ATP + beta-nicotinate D-ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes ATCC BAA-946
-
-
?
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
-
-
-
r
ATP + nicotinamide ribonucleotide
diphosphate + NAD+
show the reaction diagram
-
i.e. NMN or nicotinamide mononucleotide, reverse reaction at 17% the rate of deamido-NAD+-synthesis
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
-
?
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
best substrate
i.e. nicotinic acid adenine dinucleotide
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
i.e. nicotinate mononucleotide
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
i.e. nicotinate mononucleotide
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
i.e. nicotinate mononucleotide
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
i.e. nicotinate mononucleotide
i.e. nicotinic acid adenine dinucleotide
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
i.e. nicotinate mononucleotide
i.e. nicotinic acid adenine dinucleotide
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
i.e. nicotinate mononucleotide
i.e. nicotinic acid adenine dinucleotide
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
reaction at 77% the rate of nicotinamide ribonucleotide
i.e. nicotinic acid adenine dinucleotide
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
NaMNAT is the penultimate enzyme in the biosynthesis of NAD+ and catalyzes the adenylation of nicotinic acid mononucleotide by ATP to form nicotinic acid adenine dinucleotide
-
?
ATP + nicotinic acid mononucleotide
nicotinic acid adenine dinucleotide + diphosphate
show the reaction diagram
-
-
-
r
ATP + NMN
diphosphate + NAD+
show the reaction diagram
-
-
-
r
deoxy-ATP + nicotinamide ribonucleotide
?
show the reaction diagram
-
-
-
-
?
deoxy-ATP + nicotinate ribonucleotide
?
show the reaction diagram
-
-
-
-
?
nicotinate mononucleotide + ATP
nicotinate adenine dinucleotide + diphosphate
show the reaction diagram
-
PreissHandler-dependent pathway
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
show the reaction diagram
-
-
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
show the reaction diagram
activity observed with dATP, ITP
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid adenine dinucleotide + diphosphate
show the reaction diagram
activity observed with GTP, ITP
-
r
nicotinic acid mononucleotide + ATP
nicotinic acid dinucleotide + diphosphate
show the reaction diagram
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid dinucleotide + diphosphate
show the reaction diagram
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid dinucleotide + diphosphate
show the reaction diagram
Methanothermobacter thermautotrophicum
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + beta-nicotinate D-ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
Streptococcus pyogenes, Streptococcus pyogenes ATCC BAA-946
Q5XDT7
-
-
?
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
-
-
-
r
ATP + nicotinate ribonucleotide
diphosphate + deamido-NAD+
show the reaction diagram
Q6HT60
NaMNAT is the penultimate enzyme in the biosynthesis of NAD+ and catalyzes the adenylation of nicotinic acid mononucleotide by ATP to form nicotinic acid adenine dinucleotide
-
?
nicotinate mononucleotide + ATP
nicotinate adenine dinucleotide + diphosphate
show the reaction diagram
-
PreissHandler-dependent pathway
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid dinucleotide + diphosphate
show the reaction diagram
Q5HFG7
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid dinucleotide + diphosphate
show the reaction diagram
P54455
-
-
?
nicotinic acid mononucleotide + ATP
nicotinic acid dinucleotide + diphosphate
show the reaction diagram
Methanothermobacter thermautotrophicum
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
-
activation, 25 mM, NAD+-synthesis, not deamido-NAD+-synthesis
Mg2+
-
requirement
Mg2+
-
requirement
Mg2+
-
requirement
NH4Cl
-
activation, can substitute for KCl
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4,4'-[cyclohexa-2,5-diene-1,4-diylidenebis[(E)methylylidene(E)diazene-2,1-diyl]]bis[N-(2-chlorophenyl)-4-oxobutanamide]
-
4-[2-(anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide
-
NAD+
-
deamido-NAD+ as substrate
NAD+
product inhibition
nicotinic acid adenine dinucleotide
product inhibition
[(2E)-1-[4-[(2-chlorophenyl)amino]-4-oxobutanoyl]-2-(naphthalen-1-ylmethylidene)hydrazino]acetic acid
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.27
3-acetylpyridine-NAD+
-
37C, pH 7.5
0.74
3-pyridinealdehyde-NAD+
-
37C, pH 7.5
0.0017
ATP
-
-
0.044
ATP
pH 7.5, recombinant enzyme
0.06
ATP
-
37C, pH 7.5, + nicotinate ribonucleotide
0.135
ATP
-
37C, pH 7.4
0.5
ATP
-
37C, pH 7.5
4
ATP
-
30C, pH 7.5
0.0045
deamido-NAD+
-
37C, pH 7.5
0.0068
deamido-NAD+
-
37C, pH 7.4
0.029
deamido-NAD+
-
37C, pH 7.5
0.083
diphosphate
-
0.65
diphosphate
-
37C, pH 7.5
1.1
diphosphate
-
37C, pH 7.5
1.119
diphosphate
-
4.2
diphosphate
-
37C, pH 7.4
0.069
NAD+
-
37C, pH 7.5
0.07
NAD+
-
0.37
NAD+
-
37C, pH 7.5
1.7
NAD+
-
37C, pH 7.4
0.021
nicotinamide mononucleotide
range 0.021-0.032 mM
0.17
nicotinamide mononucleotide
-
0.7
nicotinamide mononucleotide
-
-
0.043
nicotinamide ribonucleotide
-
37C, pH 7.4
0.2
nicotinamide ribonucleotide
-
37C, pH 7.5
0.4
nicotinamide ribonucleotide
-
37C, pH 7.5
0.025
nicotinate ribonucleotide
pH 7.5, recombinant enzyme
0.03
nicotinate ribonucleotide
-
37C, pH 7.5
0.08
nicotinate ribonucleotide
-
37C, pH 7.5
0.13
nicotinate ribonucleotide
-
37C, pH 7.5
1.3
nicotinate ribonucleotide
-
30C, pH 7.5
0.015
nicotinic acid mononucleotide
-
2.3
NMN
-
37C, pH 7.4
0.0304
reduced nicotinamide mononucleotide
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0079
K891-0166
pH 7.5, 37C
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
4,4'-[cyclohexa-2,5-diene-1,4-diylidenebis[(E)methylylidene(E)diazene-2,1-diyl]]bis[N-(2-chlorophenyl)-4-oxobutanamide]
Bacillus anthracis
C3L5T6
pH 7.5, 22C
0.025
4-[2-(anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide
Bacillus anthracis
C3L5T6
pH 7.5, 22C
0.015
K891-0166
Streptococcus pyogenes
Q5XDT7
pH 7.5, 37C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0003
-
3-acetyl-pyridine-NAD+ as substrate
0.0008
-
3-pyridinealdehyde-NAD+ as substrate
0.00133
-
Xanthi, callus culture
0.00269
-
Samsun, callus culture
0.00358
-
Samsun, root
0.004
-
NAD+ as substrate
0.024
-
deamido-NAD+ as substrate
0.054
-
NMN as substrate
0.34
-
NAD+ as substrate
1.42
-
3-pyridinealdehyde-NAD+ as substrate
2.8
-
deamido-NAD+ as substrate
3.82
-
3-acetyl-pyridine-NAD+ as substrate
3.85
-
deamido-NAD+ as substrate
5
-
NAD+ as substrate
10.1
-
ATP as substrate
11.1
-
nicotinate ribonucleotide as substrate
11.5
-
diphosphate as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
isoform NMNAT2 localizes to the cis-Golgi and endoplasmic reticulum-Golgi intermediate compartment. It is palmitoylated at two adjacent cysteine residues of its isoform-specific domain and thereby anchored at the cytoplasmic surface
Manually annotated by BRENDA team
sequence of isoform NMNAT1 contains a predicted nuclear localization signal
Manually annotated by BRENDA team
isoform NMNAT3 is targeted to mitochondria by its N-terminus
Manually annotated by BRENDA team
additional information
the three human isoforms NMNAT1-3 are localized to the nucleus, the Golgi complex, and mitochondria. Their genes contain unique exons that encode isoform-specific domains to mediate subcellular targeting and post-translational modifications. These domains are dispensable for catalytic activity; the three human isoforms NMNAT1-3 are localized to the nucleus, the Golgi complex, and mitochondria. Their genes contain unique exons that encode isoform-specific domains to mediate subcellular targeting and post-translational modifications. These domains are dispensable for catalytic activity; the three human isoforms NMNAT1-3 are localized to the nucleus, the Golgi complex, and mitochondria. Their genes contain unique exons that encode isoform-specific domains to mediate subcellular targeting and post-translational modifications. These domains are dispensable for catalytic activity
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus anthracis (strain CDC 684 / NRRL 3495)
Bacillus anthracis (strain CDC 684 / NRRL 3495)
Bacillus anthracis (strain CDC 684 / NRRL 3495)
Bacillus anthracis (strain CDC 684 / NRRL 3495)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Staphylococcus aureus (strain COL)
Staphylococcus aureus (strain COL)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24350
calculated from amino acid sequence
727776
36370 - 49140
-
gel filtration, sedimentation equlibrium centrifugation
642935
44000
by gel filtration
675394
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 23347, sequence calculation
?
-
x * 24500, calculated: 24528
dimer
-
crystallization studies
hexamer
Methanothermobacter thermautotrophicum
-
-
homohexamer
-
-
homotetramer
4 * 34439, calculated
homotetramer
4 * 48000, calculated: 45859
additional information
presence of considerable conformational heterogeneity and flexibility in three loops surrounding the substrate-binding area, analysis of protein aggregation during purification by self-interaction chromatography
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitors 4-[2-(anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide, 4,4'-[cyclohexa-2,5-diene-1,4-diylidenebis[(E)methylylidene(E)diazene-2,1-diyl]]bis[N-(2-chlorophenyl)-4-oxobutanamide], and [(2E)-1-[4-[(2-chlorophenyl)amino]-4-oxobutanoyl]-2-(naphthalen-1-ylmethylidene)hydrazino]acetic acid. 4-[2-(Anthracen-9-ylmethylidene)hydrazino]-N-(3-chlorophenyl)-4-oxobutanamide binds at an enzyme monomer-monomer interface formed in the crystal of the complex, it sits at a central cleft between strands beta1 and beta4 of the beta sheet, which is the catalytic and substrate binding sites of the enzyme. The structures reveal a common binding site near residues Trp117, Try112, and Met109. This site overlaps but is distinct from the substrate-binding pocket
sitting drop and hanging drop vapour diffusion method, mixing 0.001 ml of 4 mg/ml protein in 50 mM Tris, pH 7.0, 100 mM NaCl, 100 mM Arg, 100 mM Glu, 1% glycerol, 1 mM DTT, and containing 200 mM trehalose, with 0.001 ml of reservoir solution containing 2.1 M ammonium sulfate, 100 mM HEPES pH 7.0, 2% PEG 400 and 10 mM MgCl2, cryoprotection by 25% glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution, usage molecular replacement and of self-interaction chromatography for process optimization
crystals of the apo-enzyme belong to space group: P21 with 58.5% solvent and contain four molecules of NaMN AT in the asymmetric subunit, crystals in complex with deamido-NAD+ belong to space group: P212121 with 55.6% solvent and contain six molecules of NaMN AT in the asymmetric subunit, conditions: polyethylene glycol 3350 and 100 mM MgCl2
-
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 20C in 100 mM Tris, pH 7, 200 mM NaCl and 800 mM sodium citrate
-
crystal structure of NaMN-bound form at 1.7 A, ATP-bound form at 2.0 A, apo-form at 2.0 A. The substrate-unbound and substrate-complexed structures are all in the fully open conformation. There is little conformational change upon binding each of the substrates. A conformational change is necessary to bring the two substrates closer together for initiating the catalysis. The authors suggest that such a conformational change likely occurs only after both substrates are simultaneously bound in the active site
Crystals of saNaMNAT were initially obtained at 22C from polyethylene glycol 3000 and phosphatecitrate buffer.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
5 min 54% loss of activity
642778
60
-
5 min 95% loss of activity
642778
60
-
5 min 39% loss of activity
642778
65
-
5 min 65% loss of activity
642778
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
phosphate buffer, 0.08 M, pH 7.5, stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-3C, 31 days stable
-
frozen 24 h
-
0-3C, 22% loss of activity within 31 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration to homogeneity
recombinant enzyme
-
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene nadD, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
overexpression in Escherichia coli BL21 with a His-tag
-
expression in Escherichia coli NZN111 with IdhA and pflB genes inactivated for the production of succinic acid
-
overexpression in Escherichia coli BL21 with a 6 x His-tag
-
expression in HeLa S3 cells; expression in HeLa S3 cells; expression in HeLa S3 cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
mutation in the nadD gene, renamed nadD72, leads to a temparature-sensitive strain which cannot grow on minimal medium
additional information
generation of mutants lacking residues Glu107-Lys146. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoforms NMNAT1 are distributed throughout the cytoplasm; generation of mutants lacking residues Leu105-Ala125 of isoform NMNAT3. Overexpression of the construct results in a strong increase in overall enzymic activity compared with non-transfected cells; generation of mutants lacking residues Val109-Leu192. Overexpression of the constructs results in a strong increase in overall enzymic activity compared with non-transfected cells. The deletion mutants of isoform NMNAT2 are distributed throughout the cytoplasm
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
the enzyme is a target for inhibitor development
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