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show all sequences of 3.5.1.19

Structural and kinetic isotope effect studies of nicotinamidase (Pnc1) from Saccharomyces cerevisiae

Smith, B.C.; Anderson, M.A.; Hoadley, K.A.; Keck, J.L.; Cleland, W.W.; Denu, J.M.; Biochemistry 51, 243-256 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Saccharomyces cerevisiae
Crystallization (Commentary)
Crystallization
Organism
in complex with nicotinaldehyde, hanging drop vapor diffusion method, using 1.6 M NaOAc, 10% (w/v) ethylene glycol, and 0.1 M HEPES (pH 7.4)
Saccharomyces cerevisiae
Engineering
Amino acid exchange
Commentary
Organism
C167A
the mutant shows most strongly decreased kcat value compared to the wild type enzyme (below the assay detection limit)
Saccharomyces cerevisiae
D51A
the zinc-binding mutant shows decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
D51N
the zinc-binding mutant shows decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
D8A
the mutant shows 770fold decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
D8E
the mutant shows 100fold decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
D8N
the mutant shows 1000fold decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
H53A
the zinc-binding mutant shows decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
H94A
the zinc-binding mutant shows decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
K122A
the mutant shows 16fold decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
K122R
the mutant shows 770fold decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
Inhibitors
Inhibitors
Commentary
Organism
Structure
3-acetylpyridine
competitive inhibition
Saccharomyces cerevisiae
benzaldehyde
competitive inhibition
Saccharomyces cerevisiae
additional information
not inhibited by 10 mM EDTA
Saccharomyces cerevisiae
nicotinaldehyde
most potent inhibitor
Saccharomyces cerevisiae
nicotinic acid
competitive inhibition
Saccharomyces cerevisiae
pyrazinoic acid
competitive inhibition
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0018
-
nicotinamide
Km below 0.0018 mM, mutant enzyme D51N, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0024
-
nicotinamide
Km below 0.0024 mM, mutant enzyme D51A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0027
-
nicotinamide
Km below 0.0027 mM, mutant enzyme H94A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0065
-
nicotinamide
Km below 0.0065 mM, mutant enzyme K122A, in 50 mM sodium phosphate (pH 7.5), at 25°C; mutant enzyme H53A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0096
-
nicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.025
-
Benzamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.061
-
5-Methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.157
-
Pyrazinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
contains tightly bound zinc. Addition of 2 mM ZnCl2 fails to increase the activity of the wild type enzyme
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
nicotinamide + H2O
Saccharomyces cerevisiae
best substrate
nicotinate + NH3
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
P53184
-
-
Purification (Commentary)
Commentary
Organism
Ni-NTA column chromatography and Sephacryl S-300 gel filtration
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-methylnicotinamide + H2O
-
718924
Saccharomyces cerevisiae
1-methylnicotinate + NH3
-
-
-
?
5-methylnicotinamide + H2O
-
718924
Saccharomyces cerevisiae
5-methylnicotinate + NH3
-
-
-
?
benzamide + H2O
-
718924
Saccharomyces cerevisiae
benzoate + NH3
-
-
-
?
additional information
no activity with nicotinamide mononucleotide and NAD+
718924
Saccharomyces cerevisiae
?
-
-
-
-
nicotinamide + H2O
best substrate
718924
Saccharomyces cerevisiae
nicotinate + NH3
-
-
-
?
pyrazinamide + H2O
-
718924
Saccharomyces cerevisiae
pyrazine-2-carboxylic acid + NH3
-
-
-
?
thionicotinamide + H2O
-
718924
Saccharomyces cerevisiae
pyridine-3-carbothioic O-acid
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0005
-
nicotinamide
kcat below 0.0005 s-1, mutant enzyme C167A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0006
-
nicotinamide
mutant enzyme D8E, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0009
-
nicotinamide
mutant enzyme D8A, in 50 mM sodium phosphate (pH 7.5), at 25°C; mutant enzyme D8N, in 50 mM sodium phosphate (pH 7.5), at 25°C; mutant enzyme K122R, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.007
-
nicotinamide
mutant enzyme D51A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0088
-
Benzamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.014
-
nicotinamide
mutant enzyme H53A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.02
-
nicotinamide
mutant enzyme H94A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.044
-
nicotinamide
mutant enzyme K122A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.064
-
nicotinamide
mutant enzyme D51N, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.69
-
nicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
1.75
-
5-Methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
2.56
-
Pyrazinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8
-
Saccharomyces cerevisiae
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.00094
-
nicotinaldehyde
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0206
-
benzaldehyde
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.12
-
nicotinic acid
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.316
-
3-acetylpyridine
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
6.7
-
pyrazinoic acid
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Saccharomyces cerevisiae
Crystallization (Commentary) (protein specific)
Crystallization
Organism
in complex with nicotinaldehyde, hanging drop vapor diffusion method, using 1.6 M NaOAc, 10% (w/v) ethylene glycol, and 0.1 M HEPES (pH 7.4)
Saccharomyces cerevisiae
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C167A
the mutant shows most strongly decreased kcat value compared to the wild type enzyme (below the assay detection limit)
Saccharomyces cerevisiae
D51A
the zinc-binding mutant shows decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
D51N
the zinc-binding mutant shows decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
D8A
the mutant shows 770fold decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
D8E
the mutant shows 100fold decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
D8N
the mutant shows 1000fold decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
H53A
the zinc-binding mutant shows decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
H94A
the zinc-binding mutant shows decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
K122A
the mutant shows 16fold decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
K122R
the mutant shows 770fold decreased kcat value compared to the wild type enzyme
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
3-acetylpyridine
competitive inhibition
Saccharomyces cerevisiae
benzaldehyde
competitive inhibition
Saccharomyces cerevisiae
additional information
not inhibited by 10 mM EDTA
Saccharomyces cerevisiae
nicotinaldehyde
most potent inhibitor
Saccharomyces cerevisiae
nicotinic acid
competitive inhibition
Saccharomyces cerevisiae
pyrazinoic acid
competitive inhibition
Saccharomyces cerevisiae
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.00094
-
nicotinaldehyde
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0206
-
benzaldehyde
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.12
-
nicotinic acid
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.316
-
3-acetylpyridine
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
6.7
-
pyrazinoic acid
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0018
-
nicotinamide
Km below 0.0018 mM, mutant enzyme D51N, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0024
-
nicotinamide
Km below 0.0024 mM, mutant enzyme D51A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0027
-
nicotinamide
Km below 0.0027 mM, mutant enzyme H94A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0065
-
nicotinamide
Km below 0.0065 mM, mutant enzyme K122A, in 50 mM sodium phosphate (pH 7.5), at 25°C; mutant enzyme H53A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0096
-
nicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.025
-
Benzamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.061
-
5-Methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.157
-
Pyrazinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
contains tightly bound zinc. Addition of 2 mM ZnCl2 fails to increase the activity of the wild type enzyme
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
nicotinamide + H2O
Saccharomyces cerevisiae
best substrate
nicotinate + NH3
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
Ni-NTA column chromatography and Sephacryl S-300 gel filtration
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-methylnicotinamide + H2O
-
718924
Saccharomyces cerevisiae
1-methylnicotinate + NH3
-
-
-
?
5-methylnicotinamide + H2O
-
718924
Saccharomyces cerevisiae
5-methylnicotinate + NH3
-
-
-
?
benzamide + H2O
-
718924
Saccharomyces cerevisiae
benzoate + NH3
-
-
-
?
additional information
no activity with nicotinamide mononucleotide and NAD+
718924
Saccharomyces cerevisiae
?
-
-
-
-
nicotinamide + H2O
best substrate
718924
Saccharomyces cerevisiae
nicotinate + NH3
-
-
-
?
pyrazinamide + H2O
-
718924
Saccharomyces cerevisiae
pyrazine-2-carboxylic acid + NH3
-
-
-
?
thionicotinamide + H2O
-
718924
Saccharomyces cerevisiae
pyridine-3-carbothioic O-acid
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0005
-
nicotinamide
kcat below 0.0005 s-1, mutant enzyme C167A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0006
-
nicotinamide
mutant enzyme D8E, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0009
-
nicotinamide
mutant enzyme D8A, in 50 mM sodium phosphate (pH 7.5), at 25°C; mutant enzyme D8N, in 50 mM sodium phosphate (pH 7.5), at 25°C; mutant enzyme K122R, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.007
-
nicotinamide
mutant enzyme D51A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0088
-
Benzamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.014
-
nicotinamide
mutant enzyme H53A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.02
-
nicotinamide
mutant enzyme H94A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.044
-
nicotinamide
mutant enzyme K122A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.064
-
nicotinamide
mutant enzyme D51N, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.69
-
nicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
1.75
-
5-Methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
2.56
-
Pyrazinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8
-
Saccharomyces cerevisiae
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0086
-
1-methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0096
-
nicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.025
-
Benzamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.05
-
Thionicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.061
-
5-Methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.157
-
Pyrazinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.35
-
Benzamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
2.2
-
nicotinamide
mutant enzyme H53A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
6.7
-
nicotinamide
kcat/Km above 6.7 (1/sec*mM), mutant enzyme K122A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
7.4
-
nicotinamide
kcat/Km above 7.4 (1/sec*mM), mutant enzyme H94A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
8.3
-
nicotinamide
kcat/Km above 8.3 (1/sec*mM), mutant enzyme D51A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
16
-
Pyrazinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
29
-
5-Methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
35
-
nicotinamide
kcat/Km above 35 (1/sec*mM), mutant enzyme D51N, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
72
-
nicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.0086
-
1-methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.0096
-
nicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.025
-
Benzamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.05
-
Thionicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.061
-
5-Methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.157
-
Pyrazinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
0.35
-
Benzamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
2.2
-
nicotinamide
mutant enzyme H53A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
6.7
-
nicotinamide
kcat/Km above 6.7 (1/sec*mM), mutant enzyme K122A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
7.4
-
nicotinamide
kcat/Km above 7.4 (1/sec*mM), mutant enzyme H94A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
8.3
-
nicotinamide
kcat/Km above 8.3 (1/sec*mM), mutant enzyme D51A, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
16
-
Pyrazinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
29
-
5-Methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
35
-
nicotinamide
kcat/Km above 35 (1/sec*mM), mutant enzyme D51N, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
72
-
nicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
Saccharomyces cerevisiae
Other publictions for EC 3.5.1.19
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
727053
Stekhanova
Nicotinamidase from the thermo ...
Acidilobus saccharovorans, Acidilobus saccharovorans DSM 16705
Biochemistry
79
54-61
2014
2
-
1
-
-
-
4
1
-
1
1
-
-
7
-
-
-
-
-
-
-
-
2
1
1
1
2
1
1
-
-
-
-
-
-
2
-
1
-
-
-
-
-
4
-
1
-
1
1
-
-
-
-
-
-
-
-
-
2
1
1
1
2
1
1
-
-
-
-
1
1
-
1
1
729184
Stekhanova
Nicotinamidase from the thermo ...
Acidilobus saccharovorans, Acidilobus saccharovorans DSM 16705
Biochemistry (Moscow)
79
54-61
2014
3
-
1
-
-
-
3
2
-
1
1
-
-
7
-
-
-
-
-
-
-
-
6
1
1
1
2
2
1
1
-
-
-
-
-
3
-
1
-
-
-
-
-
3
-
2
-
1
1
-
-
-
-
-
-
-
-
-
6
1
1
1
2
2
1
1
-
-
-
-
-
-
2
2
734741
Ion
A multi-scale computational st ...
Streptococcus pneumoniae
Molecules
19
15735-15753
2014
-
1
-
-
-
-
-
-
-
1
-
1
-
2
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
735324
Rueda
Nicotinamidase/pyrazinamidase ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Tuberculosis
94
644-648
2014
-
-
1
-
-
-
-
-
-
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Wintzerith
Purification and characterizat ...
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Fuller
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Determination of nicotinamide ...
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Tanigawa
Nicotinamide deamidase from Fl ...
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Foster
Pyridine nucleotide cycle of S ...
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Kinetic studies of nicotinamid ...
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Johnson
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Inhibition of nicotinamide dea ...
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Gillam
Nicotinamide deamidase from ra ...
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246570
Albizati
Active-site studies on rabbit ...
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Tanigawa
Purification and properties of ...
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Pardee
Hyperproduction and purificati ...
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Petrack
Nicotinamide deaminase from ma ...
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246567
Sarma
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Studies on the enzymes involve ...
Aspergillus niger
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311-322
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