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beta-nicotinamide D-ribonucleoside + H2O
beta-nicotinate D-ribonucleoside + NH3
-
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
nicotinamide riboside + H2O
nicotinate riboside + NH3
-
-
-
-
?
additional information
?
-
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
ir
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
involvement in NAD metabolism
-
ir
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
contribution to the recycling pathway of NAD+
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
contribution to the recycling pathway of NAD+
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
absolute specific for
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
absolute specific for
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
contribution to the recycling pathway of NAD+
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
highly specific, involvement in B12 synthesis and bacterial DNA ligase reaction
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
integral component of the four-membered pyridine nucleotide cycle
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
contribution to the recycling pathway of NAD+
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
involvement in NAD metabolism
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
-
-
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
NaMN binding site, structure, overview
-
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
-
-
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
NaMN binding site, structure, overview
-
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
-
-
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
NaMN binding site, structure, overview
-
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
-
-
-
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
-
-
-
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
-
-
-
-
ir
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
-
-
-
-
ir
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
14% activity compared to nicotinamide D-ribonucleotide
-
ir
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
additional information
?
-
-
NMN deamidase lacks intrinsic NAD synthesis activity
-
-
?
additional information
?
-
-
the enzyme has no detectable deamidase activity toward NAD, NADP+, nicotinamide, and nicotinamide riboside
-
-
?
additional information
?
-
CinA is a bifunctional enzyme exhibiting both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities, ligand binding structures and catalytic mechanism analysis for both activities, overview
-
-
?
additional information
?
-
-
CinA is a bifunctional enzyme exhibiting both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities, ligand binding structures and catalytic mechanism analysis for both activities, overview
-
-
?
additional information
?
-
-
CinA is a bifunctional enzyme exhibiting both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities, ligand binding structures and catalytic mechanism analysis for both activities, overview
-
-
?
additional information
?
-
CinA is a bifunctional enzyme exhibiting both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities, ligand binding structures and catalytic mechanism analysis for both activities, overview
-
-
?
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beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
additional information
?
-
-
the enzyme has no detectable deamidase activity toward NAD, NADP+, nicotinamide, and nicotinamide riboside
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
involvement in NAD metabolism
-
ir
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
contribution to the recycling pathway of NAD+
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
contribution to the recycling pathway of NAD+
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
absolute specific for
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
absolute specific for
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
contribution to the recycling pathway of NAD+
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
highly specific, involvement in B12 synthesis and bacterial DNA ligase reaction
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
integral component of the four-membered pyridine nucleotide cycle
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
contribution to the recycling pathway of NAD+
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
-
-
?
beta-nicotinamide D-ribonucleotide + H2O
beta-nicotinate D-ribonucleotide + NH3
-
involvement in NAD metabolism
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
-
-
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
-
-
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
-
-
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
-
-
-
-
?
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
-
-
-
-
ir
nicotinamide mononucleotide + H2O
nicotinate mononucleotide + NH3
-
-
-
-
ir
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
14% activity compared to nicotinamide D-ribonucleotide
-
ir
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
nicotinamide ribonucleoside + H2O
nicotinic acid ribonucleoside + NH3
-
highly specific
-
?
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3.6
beta-nicotinamide D-ribonucleoside
-
-
0.007 - 1.05
beta-nicotinamide D-ribonucleotide
0.006 - 1.93
nicotinamide mononucleotide
additional information
additional information
-
0.007
beta-nicotinamide D-ribonucleotide
-
recombinant wild-type enzyme, pH 7.5, 37°C
0.012
beta-nicotinamide D-ribonucleotide
-
recombinant mutant S103A, pH 7.5, 37°C
0.014
beta-nicotinamide D-ribonucleotide
-
-
0.027
beta-nicotinamide D-ribonucleotide
-
recombinant mutant T31A, pH 7.5, 37°C
0.07
beta-nicotinamide D-ribonucleotide
-
-
0.18
beta-nicotinamide D-ribonucleotide
recombinant enzyme, pH 7.4, 37°C
0.272
beta-nicotinamide D-ribonucleotide
-
recombinant mutant E28A, pH 7.5, 37°C
1.05
beta-nicotinamide D-ribonucleotide
-
-
0.006
nicotinamide mononucleotide
-
in 100 mM potassium phosphate, pH 8.0, 10 mM sodium fluoride, 10 mM EDTA, at 37°C
0.006
nicotinamide mononucleotide
-
in 100 mM potassium phosphate, pH 8.0, 10 mM sodium fluoride, 10 mM EDTA, at 37°C
0.024
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant wild-type enzyme
0.028
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant mutant C32A
0.051
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant mutant S48A
0.158
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant mutant T105A
1.93
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant mutant Y58F
additional information
additional information
-
beta-nicotinamide D-ribonucleotide, sigmoidal shape of substrate concentration shows a form of allosteric control
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetic at pH 7.5 and 37°C
-
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0.38 - 4.1
beta-nicotinamide D-ribonucleotide
1.5 - 8.7
nicotinamide mononucleotide
0.38
beta-nicotinamide D-ribonucleotide
recombinant enzyme, pH 7.4, 37°C
1.1
beta-nicotinamide D-ribonucleotide
-
recombinant mutant S103A, pH 7.5, 37°C
3.2
beta-nicotinamide D-ribonucleotide
-
recombinant mutant T31A, pH 7.5, 37°C
3.9
beta-nicotinamide D-ribonucleotide
-
recombinant mutant E28A, pH 7.5, 37°C
4.1
beta-nicotinamide D-ribonucleotide
-
recombinant wild-type enzyme, pH 7.5, 37°C
1.5
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant mutant Y58F
3.3
nicotinamide mononucleotide
-
in 100 mM potassium phosphate, pH 8.0, 10 mM sodium fluoride, 10 mM EDTA, at 37°C
3.3
nicotinamide mononucleotide
-
in 100 mM potassium phosphate, pH 8.0, 10 mM sodium fluoride, 10 mM EDTA, at 37°C
3.5
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant mutant T105A
7.3
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant mutant C32A
8.7
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant wild-type enzyme
8.7
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant mutant S48A
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2.1 - 590
beta-nicotinamide D-ribonucleotide
0.777 - 362.5
nicotinamide mononucleotide
2.1
beta-nicotinamide D-ribonucleotide
recombinant enzyme, pH 7.4, 37°C
10
beta-nicotinamide D-ribonucleotide
-
recombinant mutant E28A, pH 7.5, 37°C
90
beta-nicotinamide D-ribonucleotide
-
recombinant mutant S103A, pH 7.5, 37°C
120
beta-nicotinamide D-ribonucleotide
-
recombinant mutant T31A, pH 7.5, 37°C
590
beta-nicotinamide D-ribonucleotide
-
recombinant wild-type enzyme, pH 7.5, 37°C
0.777
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant mutant Y58F
22.15
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant mutant T105A
170.6
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant mutant S48A
260.7
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant mutant C32A
362.5
nicotinamide mononucleotide
pH 7.5, 37°C, recombinant wild-type enzyme
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physiological function
-
recombinant NMN deamidase delays Wallerian degeneration and rescues axonal defects caused by NMNAT2 deficiency in vivo. NMN-consuming activity with axonal NAD-synthesizing enzyme NMNAT2, but not NAD-synthesizing activity, and it delays axon degeneration in primary neuronal cultures. Transgenic NMN deamidase protection is neuron specific and effective against various toxic insults. NMN deamidase prevents NMN accumulation in injured sciatic nerves
evolution
-
the enzyme belongs to the PncC superfamily, active site configuration, structure comparisons, overview
evolution
the enzyme's N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose pyrophosphatase activity
evolution
the enzyme belongs to the NMN deamidase family
evolution
-
the enzyme belongs to the NMN deamidase family
-
evolution
-
the enzyme's N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose pyrophosphatase activity
-
evolution
-
the enzyme belongs to the NMN deamidase family
-
evolution
-
the enzyme's N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose pyrophosphatase activity
-
metabolism
-
the only possible way of nicotinamide salvage in Shewanella oneidensis
metabolism
nicotinamide mononucleotide (NMN) deamidase is one of the key enzymes of the bacterial pyridine nucleotide cycle, PNC
metabolism
the enzyme is associated with natural competence and is proposed to have a function as an enzyme participating in the pyridine nucleotide cycle, which recycles products formed by non-redox uses of NAD+
metabolism
the hyperthermophilic archaeon Thermococcus kodakarensis utilizes a four-step pathway for NAD+ salvage through nicotinamide deamination
metabolism
-
the hyperthermophilic archaeon Thermococcus kodakarensis utilizes a four-step pathway for NAD+ salvage through nicotinamide deamination
-
metabolism
-
nicotinamide mononucleotide (NMN) deamidase is one of the key enzymes of the bacterial pyridine nucleotide cycle, PNC
-
metabolism
-
the enzyme is associated with natural competence and is proposed to have a function as an enzyme participating in the pyridine nucleotide cycle, which recycles products formed by non-redox uses of NAD+
-
metabolism
-
the hyperthermophilic archaeon Thermococcus kodakarensis utilizes a four-step pathway for NAD+ salvage through nicotinamide deamination
-
metabolism
-
the enzyme is associated with natural competence and is proposed to have a function as an enzyme participating in the pyridine nucleotide cycle, which recycles products formed by non-redox uses of NAD+
-
additional information
-
enzyme surface charge analysis and substrate docking performed on the enzyme structure from Agrobacterium tumefaciens, PDB code 2A9S, overview
additional information
mutational analysis of AtCinA supports the Ser/Lys catalytic dyad mechanism, overview
additional information
-
mutational analysis of AtCinA supports the Ser/Lys catalytic dyad mechanism, overview
-
additional information
-
mutational analysis of AtCinA supports the Ser/Lys catalytic dyad mechanism, overview
-
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oligomer
-
heat-stable and heat-sensitive subunits
additional information
-
enzyme structure comparisons
dimer
an unusual asymmetric dimer, with three domains for each chain, the C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The asymmetry in the CinA dimer arises from two alternative orientations of the N-terminal COG1058 domains, only one of which forms a contact with the KH-type domain from the other chain, effectively closing the active site into, we propose, a catalytically competent state
dimer
-
an unusual asymmetric dimer, with three domains for each chain, the C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The asymmetry in the CinA dimer arises from two alternative orientations of the N-terminal COG1058 domains, only one of which forms a contact with the KH-type domain from the other chain, effectively closing the active site into, we propose, a catalytically competent state
-
dimer
-
an unusual asymmetric dimer, with three domains for each chain, the C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The asymmetry in the CinA dimer arises from two alternative orientations of the N-terminal COG1058 domains, only one of which forms a contact with the KH-type domain from the other chain, effectively closing the active site into, we propose, a catalytically competent state
-
homodimer
2 * 19000, recombinant enzyme, SDS-PAGE
homodimer
-
2 * 19000, recombinant enzyme, SDS-PAGE
-
homodimer
-
2 * 19000, recombinant enzyme, SDS-PAGE
-
homodimer
-
2 * about 20000, SDS-PAGE
homodimer
2 * 47320, recombinant His6-tagged enzyme, mass spectrometry
homodimer
-
2 * 47320, recombinant His6-tagged enzyme, mass spectrometry
-
homodimer
-
2 * 47000, SDS-PAGE
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C32A
site-directed mutagenesis, the mutant shows 28% reduced activity compared to the wild-type enzyme
K638A
site-directed mutagenesis, inactive mutant
R145A
site-directed mutagenesis, inactive mutant
S31A
site-directed mutagenesis, inactive mutant
S48A
site-directed mutagenesis, the mutant shows 47% reduced activity compared to the wild-type enzyme
T105A
site-directed mutagenesis, the mutant shows 94% reduced activity compared to the wild-type enzyme
Y58A
site-directed mutagenesis, inactive mutant
Y58F
site-directed mutagenesis, almost inactive mutant
R145A
-
site-directed mutagenesis, inactive mutant
-
S31A
-
site-directed mutagenesis, inactive mutant
-
T105A
-
site-directed mutagenesis, the mutant shows 94% reduced activity compared to the wild-type enzyme
-
Y58A
-
site-directed mutagenesis, inactive mutant
-
Y58F
-
site-directed mutagenesis, almost inactive mutant
-
R145A
-
site-directed mutagenesis, inactive mutant
-
S31A
-
site-directed mutagenesis, inactive mutant
-
T105A
-
site-directed mutagenesis, the mutant shows 94% reduced activity compared to the wild-type enzyme
-
Y58A
-
site-directed mutagenesis, inactive mutant
-
Y58F
-
site-directed mutagenesis, almost inactive mutant
-
E28A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K61Q
-
site-directed mutagenesis, inactive mutant
R142A
-
site-directed mutagenesis, inactive mutant
S103A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S29A
-
site-directed mutagenesis, inactive mutant
T31A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y56A
-
site-directed mutagenesis, inactive mutant
additional information
-
NMN deamidase blocks Wallerian degeneration in transgenic zebrafish larvae. NMN deamidase also rescues axonal outgrowth and perinatal lethality in a dose-dependent manner in mice lacking NMNAT2. Recombinant NMN deamidase delays Wallerian degeneration and rescues axonal defects caused by NMNAT2 deficiency in vivo. NMN deamidase protection is neuron specific and effective against various toxic insults. NMN deamidase expression confers morphological and functional preservation of transected axons
additional information
construction of a TK1650 knockout mutant strain
additional information
-
construction of a TK1650 knockout mutant strain
-
additional information
-
construction of a TK1650 knockout mutant strain
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Foster, J.W.
Pyridine nucleotide cycle of Salmonella typhimurium: in vitro demonstration of nicotinamide adenine dinucleotide glycohydrolase, nicotinamide mononucleotide glycohydrolase, and nicotinamide adenine dinucleotide pyrophosphatase activities
J. Bacteriol.
145
1002-1009
1981
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Cheng, W.; Roth, J.
Isolation of NAD cycle mutants defective in nicotinamide mononucleotide deamidase in Salmonella typhimurium
J. Bacteriol.
177
6711-6717
1995
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kuwahara, M.; Ishida, Y.; Okatani, M.
Nicotinamide nucleoside amidase activity, a novel deamidating reaction in NAD metabolism, in Aspergillus fungi
J. Ferment. Technol.
61
61-66
1983
Aspergillus awamori, Aspergillus flavus, Aspergillus niger, Aspergillus oryzae, Aspergillus usamii, Athelia rolfsii, Fusarium oxysporum, Trichoderma deliquescens, Rhizopus arrhizus
-
brenda
Foster, J.W.; Brestel, C.
NAD metabolism in Vibrio cholerae
J. Bacteriol.
149
368-371
1982
Vibrio cholerae serotype O1
brenda
Hillyard, D.; Rechsteiner, M.; Manlapaz-Ramos, P.; Imperial, J.S.; Cruz, L.J.; Olivera, B.M.
The pyridine nucleotide cycle. Studies in Escherichia coli and the human cell line D98/AH2
J. Biol. Chem.
256
8491-8497
1981
Escherichia coli, Homo sapiens
brenda
Kinney, D.M.; Foster, J.W.; Moat, A.G.
Pyridine nucleotide cycle of Samonella typhimurium: In vitro demonstration of nicotinamide mononucleotide deamidase and characterization of pnuA mutants defective in nicotinamide mononucleotide transport
J. Bacteriol.
140
607-611
1979
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Friedmann, H.C.; Garstki, C.
The pyridine nucleotide cycle: Presence of a nicotinamide mononucleotide-specific amidohydrolase in Propionibacterium shermanii
Biochem. Biophys. Res. Commun.
50
54-58
1973
Propionibacterium freudenreichii subsp. shermanii
brenda
Imai, T.
Purification and properties of nicotinamide mononucleotide amidohydrolase from Azotobacter vinelandii
J. Biochem.
73
139-153
1973
Azotobacter vinelandii, Escherichia coli, no activity in Saccharomyces cerevisiae, no activity in Oryctolagus cuniculus
brenda
Friedmann, H.C.
Preparation of nicotinic acid mononucleotide from nicotinamide mononucleotide by enzymatic deamidation
Methods Enzymol.
18
192-197
1971
Propionibacterium freudenreichii subsp. shermanii
-
brenda
Elzainy, T.A.; Ali, T.H.
NAD deamidation a new reaction by an enzyme from Aspergillus terreus DSM 826
Antonie van Leeuwenhoek
87
119-129
2005
Aspergillus terreus
brenda
Galeazzi, L.; Bocci, P.; Amici, A.; Brunetti, L.; Ruggieri, S.; Romine, M.; Reed, S.; Osterman, A.L.; Rodionov, D.A.; Sorci, L.; Raffaelli, N.
Identification of nicotinamide mononucleotide deamidase of the bacterial pyridine nucleotide cycle reveals a novel broadly conserved amidohydrolase family
J. Biol. Chem.
286
40365-40375
2011
Escherichia coli, Shewanella oneidensis
brenda
Sorci, L.; Brunetti, L.; Cialabrini, L.; Mazzola, F.; Kazanov, M.D.; DAuria, S.; Ruggieri, S.; Raffaelli, N.
Characterization of bacterial NMN deamidase as a Ser/Lys hydrolase expands diversity of serine amidohydrolases
FEBS Lett.
588
1016-1023
2014
Escherichia coli
brenda
Karuppiah, V.; Thistlethwaite, A.; Dajani, R.; Warwicker, J.; Derrick, J.P.
Structure and mechanism of the bifunctional CinA enzyme from Thermus thermophilus
J. Biol. Chem.
289
33187-33197
2014
Thermus thermophilus (Q5SHB0), Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SHB0)
brenda
Sanchez-Carron, G.; Martinez-Monino, A.B.; Sola-Carvajal, A.; Takami, H.; Garcia-Carmona, F.; Sanchez-Ferrer, A.
New insights into the phylogeny and molecular classification of nicotinamide mononucleotide deamidases
PLoS ONE
8
e82705
2013
Oceanobacillus iheyensis (Q8EQR8), Oceanobacillus iheyensis, Oceanobacillus iheyensis HTE831 (Q8EQR8)
brenda
Di Stefano, M.; Loreto, A.; Orsomando, G.; Mori, V.; Zamporlini, F.; Hulse, R.P.; Webster, J.; Donaldson, L.F.; Gering, M.; Raffaelli, N.; Coleman, M.P.; Gilley, J.; Conforti, L.
NMN deamidase delays Wallerian degeneration and rescues axonal defects caused by NMNAT2 deficiency in vivo
Curr. Biol.
27
784-794
2017
Escherichia coli
brenda
Hachisuka, S.I.; Sato, T.; Atomi, H.
Hyperthermophilic archaeon Thermococcus kodakarensis utilizes a four-step pathway for NAD+ salvage through nicotinamide deamination
J. Bacteriol.
200
e00785-17
2018
Thermococcus kodakarensis (Q5JIT6), Thermococcus kodakarensis JCM 12380 (Q5JIT6), Thermococcus kodakarensis ATCC BAA-918 (Q5JIT6)
brenda
Martinez-Monino, A.B.; Zapata-Perez, R.; Garcia-Saura, A.G.; Gil-Ortiz, F.; Perez-Gilabert, M.; Sanchez-Ferrer, A.
Characterization and mutational analysis of a nicotinamide mononucleotide deamidase from Agrobacterium tumefaciens showing high thermal stability and catalytic efficiency
PLoS ONE
12
e0174759
2017
Agrobacterium fabrum (A9CJ26), Agrobacterium fabrum C58 (A9CJ26), Agrobacterium fabrum ATCC 33970 (A9CJ26)
brenda