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1-methylnicotinamide + H2O
1-methylnicotinate + NH3
-
-
-
?
4-methoxypyridine-3-carboxamide + H2O
?
5-methoxypyridine-3-carboxamide + H2O
?
5-methyl nicotinamide + H2O
5-methyl nicotinate + NH3
5-methylnicotinamide + H2O
5-methylnicotinate + NH3
5-methylnicotinamide + H2O
5-methylnicotinic acid + NH3
-
-
-
-
r
5-methylpyridine-3-carboxamide + H2O
?
6-aminopyridine-3-carboxamide + H2O
?
6-chloropyridine-3-carboxamide + H2O
?
6-methylpyridine-3-carboxamide + H2O
?
benzamide + H2O
benzoate + NH3
-
-
-
?
ethyl nicotinate + H2O
nicotinate + ethanol
-
-
-
?
ethyl pyridine-3-carboxylate + H2O
?
ethylnicotinate + H2O
nicotinate + ethanol
ethylnicotinate + H2O
nicotinic acid + ethanol
-
-
-
-
r
methyl nicotinate + H2O
nicotinate + methanol
-
-
-
?
methyl pyridine-3-carboxylate + H2O
?
methylnicotinate + H2O
nicotinate + methanol
nicotinamide + H2O
NH3 + nicotinic acid
nicotinamide + H2O
nicotinate + NH3
nicotinamide + H2O
nicotinic acid + NH3
p-nitrophenol + H2O
phenol + NH3
-
-
-
-
?
p-nitrophenyl nicotinate + H2O
?
-
-
-
-
?
phenyl pyridine-3-carboxylate + H2O
?
pyrazinamide + H2O
NH3 + pyrazinoic acid
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
pyrazinamide + H2O
pyrazinoic acid + NH3
pyridine-3-carbothioamide + H2O
?
-
44% activity compared to nicotinamide
-
-
?
thionicotinamide + H2O
pyridine-3-carbothioic O-acid
-
-
-
?
additional information
?
-
4-methoxypyridine-3-carboxamide + H2O
?
-
20% activity compared to nicotinamide
-
-
?
4-methoxypyridine-3-carboxamide + H2O
?
-
12% activity compared to nicotinamide
-
-
?
4-methoxypyridine-3-carboxamide + H2O
?
-
5% activity compared to nicotinamide
-
-
?
4-methoxypyridine-3-carboxamide + H2O
?
-
6.5% activity compared to nicotinamide
-
-
?
5-methoxypyridine-3-carboxamide + H2O
?
-
221% activity compared to nicotinamide
-
-
?
5-methoxypyridine-3-carboxamide + H2O
?
-
646% activity compared to nicotinamide
-
-
?
5-methoxypyridine-3-carboxamide + H2O
?
-
206% activity compared to nicotinamide
-
-
?
5-methoxypyridine-3-carboxamide + H2O
?
-
137% activity compared to nicotinamide
-
-
?
5-methyl nicotinamide + H2O
5-methyl nicotinate + NH3
-
-
-
?
5-methyl nicotinamide + H2O
5-methyl nicotinate + NH3
-
-
-
?
5-methylnicotinamide + H2O
5-methylnicotinate + NH3
-
-
-
-
?
5-methylnicotinamide + H2O
5-methylnicotinate + NH3
-
-
-
?
5-methylnicotinamide + H2O
5-methylnicotinate + NH3
-
-
-
?
5-methylnicotinamide + H2O
5-methylnicotinate + NH3
-
-
-
-
?
5-methylpyridine-3-carboxamide + H2O
?
-
51% activity compared to nicotinamide
-
-
?
5-methylpyridine-3-carboxamide + H2O
?
-
330% activity compared to nicotinamide
-
-
?
5-methylpyridine-3-carboxamide + H2O
?
-
80% activity compared to nicotinamide
-
-
?
5-methylpyridine-3-carboxamide + H2O
?
-
163% activity compared to nicotinamide
-
-
?
6-aminopyridine-3-carboxamide + H2O
?
-
45% activity compared to nicotinamide
-
-
?
6-aminopyridine-3-carboxamide + H2O
?
-
20% activity compared to nicotinamide
-
-
?
6-aminopyridine-3-carboxamide + H2O
?
-
36% activity compared to nicotinamide
-
-
?
6-chloropyridine-3-carboxamide + H2O
?
-
17% activity compared to nicotinamide
-
-
?
6-chloropyridine-3-carboxamide + H2O
?
-
1.8% activity compared to nicotinamide
-
-
?
6-methylpyridine-3-carboxamide + H2O
?
-
45% activity compared to nicotinamide
-
-
?
6-methylpyridine-3-carboxamide + H2O
?
-
40% activity compared to nicotinamide
-
-
?
6-methylpyridine-3-carboxamide + H2O
?
-
11% activity compared to nicotinamide
-
-
?
ethyl pyridine-3-carboxylate + H2O
?
-
2.3% activity compared to nicotinamide
-
-
?
ethyl pyridine-3-carboxylate + H2O
?
-
4.4% activity compared to nicotinamide
-
-
?
ethyl pyridine-3-carboxylate + H2O
?
-
0.86% activity compared to nicotinamide
-
-
?
ethylnicotinate + H2O
nicotinate + ethanol
-
-
-
?
ethylnicotinate + H2O
nicotinate + ethanol
-
-
-
-
?
methyl pyridine-3-carboxylate + H2O
?
-
6500% activity compared to nicotinamide
-
-
?
methyl pyridine-3-carboxylate + H2O
?
-
15% activity compared to nicotinamide
-
-
?
methyl pyridine-3-carboxylate + H2O
?
-
3.5% activity compared to nicotinamide
-
-
?
methylnicotinate + H2O
nicotinate + methanol
-
-
-
?
methylnicotinate + H2O
nicotinate + methanol
-
-
-
-
?
nicotinamide + H2O
NH3 + nicotinic acid
-
-
-
-
?
nicotinamide + H2O
NH3 + nicotinic acid
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
the enzyme also catalyzes the hydrolysis of pyrazinamide
-
-
?
nicotinamide + H2O
nicotinate + NH3
the enzyme also catalyzes the hydrolysis of pyrazinamide
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
active site structure, overview
-
-
?
nicotinamide + H2O
nicotinate + NH3
binding structure involving residues A155, C159, and Ile154, and unbinding mechanism, modeling, overview
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
the enzyme is involved in degradation of nicotinamide
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
100% activity
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
contributes to the intracellular replication and infectivity of Brucella abortus in mice
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
contributes to the intracellular replication and infectivity of Brucella abortus in mice
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
100% activity
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
Flavobacterium peregrinum
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
enzyme is induced at high nicotinamide concentrations
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
preferred substrate
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
preferred substrate
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
100% activity
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
enzyme is involved in NAD+ biosynthesis
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
59.5% of the activity with pyrazinamide
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
59.5% of the activity with pyrazinamide
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
nicotinamidase is a key enzyme in the NAD+ salvage pathway
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
nicotinamidase is a key enzyme in the NAD+ salvage pathway
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
ir
nicotinamide + H2O
nicotinate + NH3
best substrate
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
100% activity
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
nicotinamide is a by-product of the Sir2 deacetylase reaction and is a natural Sir2 inhibitor, Pnc1, therefore, positively regulates Sir2-mediated silencing and longevity by preventing the accumulation of intracellular nicotinamide during times of stress, PNC1 specifically prevents nicotinamide-induced inhibition of telomeric and rDNA silencing in vivo, overview, the enzyme is involved in the NAD+ biosynthesis and salvage, pathway overview
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
Pnc1 stimulates Sir2, an NAD+-dependent histone deacetylase, and prevents the accumulation of nicotinamide
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
the enzyme of the pyridine nucleotide cycle is not controlled by end-product repression
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
100% activity
-
-
?
nicotinamide + H2O
nicotinate + NH3
binding structure and unbinding mechanism, modeling, overview
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
key enzyme of the NAD+ salvage pathway
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
the enzyme is an essential component of the NAD+ salvage pathway
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
enzyme is involved in the pyridine nucleotide cycle
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
the enzyme is involved in the trigonelline biosynthesis
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
assay with radiolabeled substrate
-
-
?
nicotinamide + H2O
nicotinic acid + NH3
-
as nicotinamide is an inhibitor of Arabidopsis seed germination, enzyme activity is important for germination
-
-
?
nicotinamide + H2O
nicotinic acid + NH3
-
enzyme involved in the NAD salvage pathway
-
-
?
nicotinamide + H2O
nicotinic acid + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinic acid + NH3
-
-
-
-
r
phenyl pyridine-3-carboxylate + H2O
?
-
13% activity compared to nicotinamide
-
-
?
phenyl pyridine-3-carboxylate + H2O
?
-
3.1% activity compared to nicotinamide
-
-
?
phenyl pyridine-3-carboxylate + H2O
?
-
3.1% activity compared to nicotinamide
-
-
?
pyrazinamide + H2O
NH3 + pyrazinoic acid
-
-
-
-
?
pyrazinamide + H2O
NH3 + pyrazinoic acid
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
a nicotinamide prodrug. In Mycobacterium tuberculosis the enzyme converts the nicotinamide analogue prodrug pyrazinamide into the bacteriostatic pyrazinoic acid, hence the alternative name, pyrazinamidase, PncA
a bacteriostatic drug
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
the natural resistance of Mycobacterium kansasii to pyrazinamide is due to a deficient pyrazinamidase activity of nicotinamidase
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
residues Cys133 and Phe68 are critical for the pyraminidase activity
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
residues Cys133 and Phe68 are critical for the pyraminidase activity
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
-
?
additional information
?
-
no activity with N-carbamoylsarcosine, hydantoic acid, acrylamide, D- and L-asparagine, D- and L-glutamine
-
-
?
additional information
?
-
-
no activity with N-carbamoylsarcosine, hydantoic acid, acrylamide, D- and L-asparagine, D- and L-glutamine
-
-
?
additional information
?
-
no activity with N-carbamoylsarcosine, hydantoic acid, acrylamide, D- and L-asparagine, D- and L-glutamine
-
-
?
additional information
?
-
-
nicotinamidase cannot hydrolyze 1-methyl isonicotinamide
-
-
?
additional information
?
-
-
nicotinamidase cannot hydrolyze 1-methylisonicotinamide
-
-
?
additional information
?
-
-
nicotinamidase cannot hydrolyze 1-methyl isonicotinamide
-
-
?
additional information
?
-
-
nicotinamidase cannot hydrolyze 1-methyl isonicotinamide
-
-
?
additional information
?
-
no activity with nicotinamide mononucleotide and NAD+
-
-
?
additional information
?
-
-
no activity with nicotinamide mononucleotide and NAD+
-
-
?
additional information
?
-
-
nicotinamidase cannot hydrolyze 1-methylisonicotinamide
-
-
?
additional information
?
-
-
changes in trigonelline content and nicotinic acid metabolism during germination, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-methoxypyridine-3-carboxamide + H2O
?
5-methoxypyridine-3-carboxamide + H2O
?
5-methylpyridine-3-carboxamide + H2O
?
6-aminopyridine-3-carboxamide + H2O
?
6-chloropyridine-3-carboxamide + H2O
?
6-methylpyridine-3-carboxamide + H2O
?
ethyl pyridine-3-carboxylate + H2O
?
methyl pyridine-3-carboxylate + H2O
?
nicotinamide + H2O
NH3 + nicotinic acid
nicotinamide + H2O
nicotinate + NH3
nicotinamide + H2O
nicotinic acid + NH3
phenyl pyridine-3-carboxylate + H2O
?
pyrazinamide + H2O
NH3 + pyrazinoic acid
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
pyrazinamide + H2O
pyrazinoic acid + NH3
pyridine-3-carbothioamide + H2O
?
-
44% activity compared to nicotinamide
-
-
?
additional information
?
-
4-methoxypyridine-3-carboxamide + H2O
?
-
20% activity compared to nicotinamide
-
-
?
4-methoxypyridine-3-carboxamide + H2O
?
-
12% activity compared to nicotinamide
-
-
?
4-methoxypyridine-3-carboxamide + H2O
?
-
5% activity compared to nicotinamide
-
-
?
4-methoxypyridine-3-carboxamide + H2O
?
-
6.5% activity compared to nicotinamide
-
-
?
5-methoxypyridine-3-carboxamide + H2O
?
-
221% activity compared to nicotinamide
-
-
?
5-methoxypyridine-3-carboxamide + H2O
?
-
646% activity compared to nicotinamide
-
-
?
5-methoxypyridine-3-carboxamide + H2O
?
-
206% activity compared to nicotinamide
-
-
?
5-methoxypyridine-3-carboxamide + H2O
?
-
137% activity compared to nicotinamide
-
-
?
5-methylpyridine-3-carboxamide + H2O
?
-
51% activity compared to nicotinamide
-
-
?
5-methylpyridine-3-carboxamide + H2O
?
-
330% activity compared to nicotinamide
-
-
?
5-methylpyridine-3-carboxamide + H2O
?
-
80% activity compared to nicotinamide
-
-
?
5-methylpyridine-3-carboxamide + H2O
?
-
163% activity compared to nicotinamide
-
-
?
6-aminopyridine-3-carboxamide + H2O
?
-
45% activity compared to nicotinamide
-
-
?
6-aminopyridine-3-carboxamide + H2O
?
-
20% activity compared to nicotinamide
-
-
?
6-aminopyridine-3-carboxamide + H2O
?
-
36% activity compared to nicotinamide
-
-
?
6-chloropyridine-3-carboxamide + H2O
?
-
17% activity compared to nicotinamide
-
-
?
6-chloropyridine-3-carboxamide + H2O
?
-
1.8% activity compared to nicotinamide
-
-
?
6-methylpyridine-3-carboxamide + H2O
?
-
45% activity compared to nicotinamide
-
-
?
6-methylpyridine-3-carboxamide + H2O
?
-
40% activity compared to nicotinamide
-
-
?
6-methylpyridine-3-carboxamide + H2O
?
-
11% activity compared to nicotinamide
-
-
?
ethyl pyridine-3-carboxylate + H2O
?
-
2.3% activity compared to nicotinamide
-
-
?
ethyl pyridine-3-carboxylate + H2O
?
-
4.4% activity compared to nicotinamide
-
-
?
ethyl pyridine-3-carboxylate + H2O
?
-
0.86% activity compared to nicotinamide
-
-
?
methyl pyridine-3-carboxylate + H2O
?
-
6500% activity compared to nicotinamide
-
-
?
methyl pyridine-3-carboxylate + H2O
?
-
15% activity compared to nicotinamide
-
-
?
methyl pyridine-3-carboxylate + H2O
?
-
3.5% activity compared to nicotinamide
-
-
?
nicotinamide + H2O
NH3 + nicotinic acid
-
-
-
-
?
nicotinamide + H2O
NH3 + nicotinic acid
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
the enzyme is involved in degradation of nicotinamide
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
100% activity
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
contributes to the intracellular replication and infectivity of Brucella abortus in mice
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
contributes to the intracellular replication and infectivity of Brucella abortus in mice
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
100% activity
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
enzyme is induced at high nicotinamide concentrations
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
100% activity
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
enzyme is involved in NAD+ biosynthesis
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
nicotinamidase is a key enzyme in the NAD+ salvage pathway
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
nicotinamidase is a key enzyme in the NAD+ salvage pathway
-
-
?
nicotinamide + H2O
nicotinate + NH3
best substrate
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
100% activity
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
nicotinamide is a by-product of the Sir2 deacetylase reaction and is a natural Sir2 inhibitor, Pnc1, therefore, positively regulates Sir2-mediated silencing and longevity by preventing the accumulation of intracellular nicotinamide during times of stress, PNC1 specifically prevents nicotinamide-induced inhibition of telomeric and rDNA silencing in vivo, overview, the enzyme is involved in the NAD+ biosynthesis and salvage, pathway overview
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
the enzyme of the pyridine nucleotide cycle is not controlled by end-product repression
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
100% activity
-
-
?
nicotinamide + H2O
nicotinate + NH3
key enzyme of the NAD+ salvage pathway
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
the enzyme is an essential component of the NAD+ salvage pathway
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
enzyme is involved in the pyridine nucleotide cycle
-
-
?
nicotinamide + H2O
nicotinate + NH3
-
the enzyme is involved in the trigonelline biosynthesis
-
-
?
nicotinamide + H2O
nicotinic acid + NH3
-
as nicotinamide is an inhibitor of Arabidopsis seed germination, enzyme activity is important for germination
-
-
?
nicotinamide + H2O
nicotinic acid + NH3
-
enzyme involved in the NAD salvage pathway
-
-
?
nicotinamide + H2O
nicotinic acid + NH3
-
-
-
-
?
nicotinamide + H2O
nicotinic acid + NH3
-
-
-
-
r
phenyl pyridine-3-carboxylate + H2O
?
-
13% activity compared to nicotinamide
-
-
?
phenyl pyridine-3-carboxylate + H2O
?
-
3.1% activity compared to nicotinamide
-
-
?
phenyl pyridine-3-carboxylate + H2O
?
-
3.1% activity compared to nicotinamide
-
-
?
pyrazinamide + H2O
NH3 + pyrazinoic acid
-
-
-
-
?
pyrazinamide + H2O
NH3 + pyrazinoic acid
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazine-2-carboxylic acid + NH3
-
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
a nicotinamide prodrug. In Mycobacterium tuberculosis the enzyme converts the nicotinamide analogue prodrug pyrazinamide into the bacteriostatic pyrazinoic acid, hence the alternative name, pyrazinamidase, PncA
a bacteriostatic drug
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
-
-
?
additional information
?
-
-
nicotinamidase cannot hydrolyze 1-methyl isonicotinamide
-
-
?
additional information
?
-
-
nicotinamidase cannot hydrolyze 1-methylisonicotinamide
-
-
?
additional information
?
-
-
nicotinamidase cannot hydrolyze 1-methyl isonicotinamide
-
-
?
additional information
?
-
-
nicotinamidase cannot hydrolyze 1-methyl isonicotinamide
-
-
?
additional information
?
-
-
nicotinamidase cannot hydrolyze 1-methylisonicotinamide
-
-
?
additional information
?
-
-
changes in trigonelline content and nicotinic acid metabolism during germination, overview
-
-
?
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Bacteremia
Intranasal immunization with pneumococcal polysaccharide conjugate vaccines with nontoxic mutants of Escherichia coli heat-labile enterotoxins as adjuvants protects mice against invasive pneumococcal infections.
Cysts
The NAD+ Responsive Transcription Factor ERM-BP Functions Downstream of Cellular Aggregation and Is an Early Regulator of Development and Heat Shock Response in Entamoeba.
Infections
A plasmid-encoded nicotinamidase (PncA) is essential for infectivity of Borrelia burgdorferi in a mammalian host.
Infections
Defining plasmids required by Borrelia burgdorferi for colonization of tick vector Ixodes scapularis (Acari: Ixodidae).
Leishmaniasis
In silico pharmacophore modeling and simulation studies for searching potent antileishmanials targeted against Leishmania donovani nicotinamidase.
Leprosy
Identification of cat leprosy bacillus grown in mice.
Neoplasms
Early effects of nicotinamide, 2,4-dichloro-phenoxy acetic acid & actinomycin-D on the synthesis of nicotinamide amidohydrolase in rumex acetosa tumour tissue.
Neuroblastoma
Purification and characterization of a nicotinamide deamidase released into the growth medium of neuroblastoma in vitro.
Photophobia
[Nicotinamidase and the so-called pyrazinamidase in mycobacteria; the simultaneous occurrence of both activites (author's transl)]
Pneumonia
Multiscale Computational Study on the Catalytic Mechanism of the Nonmetallo Amidase Maleamate Amidohydrolase (NicF).
Tuberculosis
A Multinational Analysis of Mutations and Heterogeneity in PZase, RpsA, and PanD Associated with Pyrazinamide Resistance in M/XDR Mycobacterium tuberculosis.
Tuberculosis
An assessment of a multiplex PCR assay for differentiating clinically important mycobacteria based on pncA gene variation.
Tuberculosis
Biochemical Characterization and Computational Identification of Mycobacterium tuberculosis Pyrazinamidase in Some Pyrazinamide-Resistant Isolates of Iran.
Tuberculosis
Characterization of Mycobacterium tuberculosis nicotinamidase/pyrazinamidase.
Tuberculosis
Characterization of pncA mutations in pyrazinamide-resistant Mycobacterium tuberculosis.
Tuberculosis
Characterization of pncA mutations of pyrazinamide-resistant Mycobacterium tuberculosis in Turkey.
Tuberculosis
Comparison of MGIT 960 & pyrazinamidase activity assay for pyrazinamide susceptibility testing of Mycobacterium tuberculosis.
Tuberculosis
Crystal structure and mechanism of catalysis of a pyrazinamidase from Pyrococcus horikoshii.
Tuberculosis
Crystal structure of the yeast nicotinamidase Pnc1p.
Tuberculosis
Cytochemical and biological properties of Mycobacterium bovis BCG.
Tuberculosis
Detection of Novel Gene Mutations Associated with Pyrazinamide Resistance in Multidrug-Resistant Mycobacterium tuberculosis Clinical Isolates in Southern China.
Tuberculosis
Direct Detection of Pyrazinamide Resistance in Mycobacterium tuberculosis by Use of pncA PCR Sequencing.
Tuberculosis
Effects of sorbitol and glycerol on the structure, dynamics, and stability of Mycobacterium tuberculosis pyrazinamidase.
Tuberculosis
Estimation of pyrazinamidase activity using a cell-free
Tuberculosis
Evaluation of drug susceptibility testing methods of clinical Mycobacterium tuberculosis isolates to pyrazinamide.
Tuberculosis
Extracellular enzyme activities potentially involved in the pathogenicity of Mycobacterium tuberculosis.
Tuberculosis
Identification, cloning, and expression of the Escherichia coli pyrazinamidase and nicotinamidase gene, pncA.
Tuberculosis
Insight to pyrazinamide resistance in Mycobacterium tuberculosis by molecular docking.
Tuberculosis
Kinetics and Inhibition of Nicotinamidase from Mycobacterium tuberculosis.
Tuberculosis
Mechanisms of pyrazinamide resistance in mycobacteria: importance of lack of uptake in addition to lack of pyrazinamidase activity.
Tuberculosis
Molecular characterization of pncA gene mutations in Mycobacterium tuberculosis clinical isolates from China.
Tuberculosis
Mutation in pncA is a major mechanism of pyrazinamide resistance in Mycobacterium tuberculosis.
Tuberculosis
Mutations in pncA, a gene encoding pyrazinamidase/nicotinamidase, cause resistance to the antituberculous drug pyrazinamide in tubercle bacillus.
Tuberculosis
Mycobacterium tuberculosis isolates from Rio de Janeiro reveal unusually low correlation between pyrazinamide resistance and mutations in the pncA gene.
Tuberculosis
Nicotinamidase/pyrazinamidase of Mycobacterium tuberculosis forms homo-dimers stabilized by disulfide bonds.
Tuberculosis
pncA mutations as a major mechanism of pyrazinamide resistance in Mycobacterium tuberculosis: spread of a monoresistant strain in Quebec, Canada.
Tuberculosis
pncA mutations in clinical Mycobacterium tuberculosis isolates from Korea.
Tuberculosis
Purification, gene cloning, targeted knockout, overexpression, and biochemical characterization of the major pyrazinamidase from Mycobacterium smegmatis.
Tuberculosis
Rapid colorimetric testing for pyrazinamide susceptibility of M. tuberculosis by a PCR-based in-vitro synthesized pyrazinamidase method.
Tuberculosis
Rapid detection of Mycobacterium tuberculosis and pyrazinamide susceptibility related to pncA mutations in sputum specimens through an integrated gene-to-protein function approach.
Tuberculosis
Rapid differentiation of bovine and human tubercle bacilli based on a characteristic mutation in the bovine pyrazinamidase gene.
Tuberculosis
Reduced pyrazinamidase activity and the natural resistance of Mycobacterium kansasii to the antituberculosis drug pyrazinamide.
Tuberculosis
Revelation of enzyme activity of mutant pyrazinamidases from Mycobacterium tuberculosis upon binding with various metals using quantum mechanical approach.
Tuberculosis
Specificity and Mechanism of Acinetobacter baumanii Nicotinamidase: Implications for Activation of the Front-Line Tuberculosis Drug Pyrazinamide.
Tuberculosis
Structural dynamics behind variants in pyrazinamidase and pyrazinamide resistance.
Tuberculosis
The curious characteristics of pyrazinamide: a review.
Tuberculosis
The paradox of pyrazinamide: an update on the molecular mechanisms of pyrazinamide resistance in Mycobacteria.
Tuberculosis
The pncA gene from naturally pyrazinamide-resistant Mycobacterium avium encodes pyrazinamidase and confers pyrazinamide susceptibility to resistant M. tuberculosis complex organisms.
Tuberculosis
[Type differentiation of tuberculosis bacteria with the aid of the nicotinamidase test.]
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0.36
5'-methylnicotinamide
-
-
0.55 - 0.68
5-methyl nicotinamide
0.061 - 1.09
5-Methylnicotinamide
0.025
Benzamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.34 - 1.43
ethyl nicotinate
0.46 - 3.84
ethylnicotinate
0.44 - 1.03
methyl nicotinate
0.21 - 3.59
methylnicotinate
0.016 - 2.89
Pyrazinamide
additional information
additional information
-
0.55
5-methyl nicotinamide
recombinant mutant Q96A, pH 7.3, 37°C
0.62
5-methyl nicotinamide
recombinant mutant Q96K, pH 7.3, 37°C
0.64
5-methyl nicotinamide
recombinant mutant C133A, pH 7.3, 37°C
0.68
5-methyl nicotinamide
recombinant wild-type enzyme, pH 7.3, 37°C
0.061
5-Methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.14
5-Methylnicotinamide
37°C, pH 7.3, mutant enzyme H75E
0.21
5-Methylnicotinamide
37°C, pH 7.3, mutant enzyme A151C
0.23
5-Methylnicotinamide
37°C, pH 7.3, mutant enzyme H75S
0.435
5-Methylnicotinamide
-
pH 7.3, temperature not specified in the publication
0.74
5-Methylnicotinamide
37°C, pH 7.3, mutant enzyme W83F
1.09
5-Methylnicotinamide
37°C, pH 7.3, wild-type enzyme
0.34
ethyl nicotinate
recombinant mutant C133A, pH 7.3, 37°C
1.02
ethyl nicotinate
recombinant wild-type enzyme, pH 7.3, 37°C
1.11
ethyl nicotinate
recombinant mutant Q96K, pH 7.3, 37°C
1.43
ethyl nicotinate
recombinant mutant Q96A, pH 7.3, 37°C
0.46
ethylnicotinate
37°C, pH 7.3, mutant enzyme H75E
0.89
ethylnicotinate
37°C, pH 7.3, mutant enzyme A151C
1.092
ethylnicotinate
-
pH 7.3, temperature not specified in the publication
1.21
ethylnicotinate
37°C, pH 7.3, mutant enzyme H75S
1.31
ethylnicotinate
37°C, pH 7.3, wild-type enzyme
3.84
ethylnicotinate
37°C, pH 7.3, mutant enzyme W83F
0.44
methyl nicotinate
recombinant mutant Q96K, pH 7.3, 37°C
0.56
methyl nicotinate
recombinant mutant Q96A, pH 7.3, 37°C
0.89
methyl nicotinate
recombinant mutant C133A, pH 7.3, 37°C
1.03
methyl nicotinate
recombinant wild-type enzyme, pH 7.3, 37°C
0.21
methylnicotinate
37°C, pH 7.3, mutant enzyme A151C
0.355
methylnicotinate
-
pH 7.3, temperature not specified in the publication
0.41
methylnicotinate
37°C, pH 7.3, mutant enzyme H75E
0.68
methylnicotinate
37°C, pH 7.3, mutant enzyme H75S
1.08
methylnicotinate
37°C, pH 7.3, wild-type enzyme
3.59
methylnicotinate
37°C, pH 7.3, mutant enzyme W83F
0.0002
nicotinamide
Flavobacterium peregrinum
-
-
0.0018
nicotinamide
Km below 0.0018 mM, mutant enzyme D51N, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.0024
nicotinamide
Km below 0.0024 mM, mutant enzyme D51A, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.0027
nicotinamide
Km below 0.0027 mM, mutant enzyme H94A, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.0027
nicotinamide
-
wild type enzyme, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.003
nicotinamide
-
wild type enzyme, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.0065
nicotinamide
Km below 0.0065 mM, mutant enzyme K122A, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.0065
nicotinamide
mutant enzyme H53A, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.0096
nicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.0106
nicotinamide
-
wild type enzyme, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.013
nicotinamide
-
mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C
0.014
nicotinamide
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
0.017
nicotinamide
pH and temperature not specified in the publication
0.0367
nicotinamide
-
wild type enzyme, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.049
nicotinamide
-
pH 7.3, temperature not specified in the publication
0.076
nicotinamide
-
wild type enzyme isoform PNC2, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.1
nicotinamide
37°C, pH 7.3, mutant enzyme A151C
0.113
nicotinamide
-
wild type enzyme isoform PNC1, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.12
nicotinamide
37°C, pH 7.3, wild-type enzyme
0.13
nicotinamide
-
enzyme in crude lysates
0.13
nicotinamide
recombinant mutant E65H, pH 7.3, 37°C
0.15
nicotinamide
37°C, pH 7.3, mutant enzyme H75E
0.17
nicotinamide
recombinant mutant F68W, pH 7.3, 37°C
0.18
nicotinamide
pH 7.5, 60°C
0.18
nicotinamide
pH and temperature not specified in the publication
0.19
nicotinamide
recombinant mutant F68W/C133A, pH 7.3, 37°C
0.21
nicotinamide
about 3fold higher than with pyrazinamide as substrate
0.23
nicotinamide
37°C, pH 7.3, mutant enzyme H75S
0.26
nicotinamide
recombinant wild-type enzyme, pH 7.3, 37°C
0.36
nicotinamide
recombinant mutant Q96A, pH 7.3, 37°C
0.39
nicotinamide
37°C, pH 7.3, mutant enzyme W83F
0.4
nicotinamide
recombinant mutant C133A, pH 7.3, 37°C
0.57
nicotinamide
recombinant mutant Q96K, pH 7.3, 37°C
0.016
Pyrazinamide
-
mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C
0.103
Pyrazinamide
-
pH 7.3, temperature not specified in the publication
0.157
Pyrazinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.22
Pyrazinamide
37°C, pH 7.3, mutant enzyme A151C
0.3
Pyrazinamide
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
0.33
Pyrazinamide
37°C, pH 7.3, wild-type enzyme
0.36
Pyrazinamide
recombinant mutant C133A, pH 7.3, 37°C
0.41
Pyrazinamide
pH 7.5, 60°C
0.5
Pyrazinamide
recombinant mutant F68W, pH 7.3, 37°C
0.59
Pyrazinamide
37°C, pH 7.3, mutant enzyme H75S
0.67
Pyrazinamide
37°C, pH 7.3, mutant enzyme H75E
0.81
Pyrazinamide
recombinant wild-type enzyme, pH 7.3, 37°C
0.82
Pyrazinamide
recombinant mutant E65H, pH 7.3, 37°C
0.83
Pyrazinamide
recombinant mutant F68W/C133A, pH 7.3, 37°C
1.15
Pyrazinamide
recombinant mutant Q96K, pH 7.3, 37°C
1.2
Pyrazinamide
recombinant mutant Q96A, pH 7.3, 37°C
2.89
Pyrazinamide
37°C, pH 7.3, mutant enzyme W83F
additional information
additional information
-
-
-
additional information
additional information
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2.16 - 15.9
5-methyl nicotinamide
1.75 - 43.7
5-Methylnicotinamide
0.0088
Benzamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.05 - 0.19
ethyl nicotinate
0.1 - 3.7
ethylnicotinate
0.17 - 1.02
methyl nicotinate
1.9 - 54.5
methylnicotinate
0.0005 - 76.9
nicotinamide
2.16
5-methyl nicotinamide
recombinant mutant Q96K, pH 7.3, 37°C
5.1
5-methyl nicotinamide
recombinant wild-type enzyme, pH 7.3, 37°C
7.09
5-methyl nicotinamide
recombinant mutant C133A, pH 7.3, 37°C
15.9
5-methyl nicotinamide
recombinant mutant Q96A, pH 7.3, 37°C
1.75
5-Methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
4.9
5-Methylnicotinamide
37°C, pH 7.3, mutant enzyme H75E
8.2
5-Methylnicotinamide
-
pH 7.3, temperature not specified in the publication
9.6
5-Methylnicotinamide
37°C, pH 7.3, mutant enzyme A151C
12.4
5-Methylnicotinamide
37°C, pH 7.3, mutant enzyme H75S
13.7
5-Methylnicotinamide
37°C, pH 7.3, mutant enzyme W83F
43.7
5-Methylnicotinamide
37°C, pH 7.3, wild-type enzyme
0.05
ethyl nicotinate
recombinant mutant Q96K, pH 7.3, 37°C
0.1
ethyl nicotinate
recombinant wild-type enzyme, pH 7.3, 37°C
0.14
ethyl nicotinate
recombinant mutant C133A, pH 7.3, 37°C
0.19
ethyl nicotinate
recombinant mutant Q96A, pH 7.3, 37°C
0.1
ethylnicotinate
37°C, pH 7.3, mutant enzyme H75E
0.2
ethylnicotinate
37°C, pH 7.3, mutant enzyme H75S
0.2
ethylnicotinate
37°C, pH 7.3, mutant enzyme W83F
0.3
ethylnicotinate
37°C, pH 7.3, mutant enzyme A151C
1.1
ethylnicotinate
-
pH 7.3, temperature not specified in the publication
3.7
ethylnicotinate
37°C, pH 7.3, wild-type enzyme
0.17
methyl nicotinate
recombinant mutant Q96K, pH 7.3, 37°C
0.32
methyl nicotinate
recombinant wild-type enzyme, pH 7.3, 37°C
0.6
methyl nicotinate
recombinant mutant Q96A, pH 7.3, 37°C
1.02
methyl nicotinate
recombinant mutant C133A, pH 7.3, 37°C
1.9
methylnicotinate
37°C, pH 7.3, mutant enzyme H75S
4.3
methylnicotinate
37°C, pH 7.3, mutant enzyme A151C
4.9
methylnicotinate
37°C, pH 7.3, mutant enzyme W83F
5.8
methylnicotinate
37°C, pH 7.3, mutant enzyme H75E
7
methylnicotinate
-
pH 7.3, temperature not specified in the publication
54.5
methylnicotinate
37°C, pH 7.3, wild-type enzyme
0.0005
nicotinamide
kcat below 0.0005 s-1, mutant enzyme C167A, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.0006
nicotinamide
mutant enzyme D8E, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.0009
nicotinamide
mutant enzyme D8A, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.0009
nicotinamide
mutant enzyme D8N, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.0009
nicotinamide
mutant enzyme K122R, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.003
nicotinamide
-
wild type enzyme, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.007
nicotinamide
mutant enzyme D51A, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.014
nicotinamide
mutant enzyme H53A, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.02
nicotinamide
mutant enzyme H94A, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.044
nicotinamide
mutant enzyme K122A, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.064
nicotinamide
mutant enzyme D51N, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.28
nicotinamide
-
wild type enzyme isoform PNC2, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.3
nicotinamide
-
wild type enzyme, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.5
nicotinamide
-
mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C
0.69
nicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
2.1
nicotinamide
-
wild type enzyme, in 100 mM phosphate buffer, pH 7.3 at 25°C
2.37
nicotinamide
recombinant mutant Q96K, pH 7.3, 37°C
3.1
nicotinamide
-
wild type enzyme isoform PNC1, in 100 mM phosphate buffer, pH 7.3 at 25°C
3.1
nicotinamide
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
3.8
nicotinamide
-
wild type enzyme, in 100 mM phosphate buffer, pH 7.3 at 25°C
5
nicotinamide
-
pH 7.3, temperature not specified in the publication
5.1
nicotinamide
37°C, pH 7.3, mutant enzyme A151C
5.63
nicotinamide
recombinant mutant E65H, pH 7.3, 37°C
8.79
nicotinamide
recombinant mutant F68W, pH 7.3, 37°C
9.82
nicotinamide
recombinant mutant F68W/C133A, pH 7.3, 37°C
10.2
nicotinamide
37°C, pH 7.3, mutant enzyme H75E
11.65
nicotinamide
recombinant wild-type enzyme, pH 7.3, 37°C
12.5
nicotinamide
37°C, pH 7.3, mutant enzyme H75S
13.6
nicotinamide
recombinant mutant C133A, pH 7.3, 37°C
15.5
nicotinamide
37°C, pH 7.3, mutant enzyme W83F
16.05
nicotinamide
recombinant mutant Q96A, pH 7.3, 37°C
22.7
nicotinamide
37°C, pH 7.3, wild-type enzyme
50
nicotinamide
pH and temperature not specified in the publication
76.9
nicotinamide
pH 7.5, 60°C
76.9
nicotinamide
pH and temperature not specified in the publication
0.1
Pyrazinamide
-
mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C
0.43
Pyrazinamide
recombinant mutant E65H, pH 7.3, 37°C
0.45
Pyrazinamide
recombinant mutant Q96K, pH 7.3, 37°C
1.3
Pyrazinamide
37°C, pH 7.3, mutant enzyme H75S
1.61
Pyrazinamide
recombinant mutant Q96A, pH 7.3, 37°C
2.56
Pyrazinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
2.6
Pyrazinamide
recombinant wild-type enzyme, pH 7.3, 37°C
3.1
Pyrazinamide
37°C, pH 7.3, mutant enzyme W83F
3.31
Pyrazinamide
recombinant mutant C133A, pH 7.3, 37°C
3.5
Pyrazinamide
37°C, pH 7.3, mutant enzyme H75E
3.8
Pyrazinamide
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
3.94
Pyrazinamide
recombinant mutant F68W, pH 7.3, 37°C
5.21
Pyrazinamide
recombinant mutant F68W/C133A, pH 7.3, 37°C
7.2
Pyrazinamide
-
pH 7.3, temperature not specified in the publication
7.5
Pyrazinamide
37°C, pH 7.3, mutant enzyme A151C
18.7
Pyrazinamide
37°C, pH 7.3, wild-type enzyme
135.7
Pyrazinamide
pH 7.5, 60°C
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0.0086
1-methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
3.4 - 29.04
5-methyl nicotinamide
0.061 - 53.9
5-Methylnicotinamide
0.05 - 0.41
ethyl nicotinate
0.1 - 2.8
ethylnicotinate
0.31 - 1.17
methyl nicotinate
1.4 - 50.5
methylnicotinate
0.0096 - 3000
nicotinamide
0.05
Thionicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
3.4
5-methyl nicotinamide
recombinant mutant Q96K, pH 7.3, 37°C
7.5
5-methyl nicotinamide
recombinant wild-type enzyme, pH 7.3, 37°C
11.07
5-methyl nicotinamide
recombinant mutant C133A, pH 7.3, 37°C
29.04
5-methyl nicotinamide
recombinant mutant Q96A, pH 7.3, 37°C
0.061
5-Methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
18.5
5-Methylnicotinamide
37°C, pH 7.3, mutant enzyme W83F
18.9
5-Methylnicotinamide
-
pH 7.3, temperature not specified in the publication
29
5-Methylnicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
35
5-Methylnicotinamide
37°C, pH 7.3, mutant enzyme H75E
40.1
5-Methylnicotinamide
37°C, pH 7.3, wild-type enzyme
45.7
5-Methylnicotinamide
37°C, pH 7.3, mutant enzyme A151C
53.9
5-Methylnicotinamide
37°C, pH 7.3, mutant enzyme H75S
0.025
Benzamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.35
Benzamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.05
ethyl nicotinate
recombinant mutant Q96K, pH 7.3, 37°C
0.1
ethyl nicotinate
recombinant wild-type enzyme, pH 7.3, 37°C
0.13
ethyl nicotinate
recombinant mutant Q96A, pH 7.3, 37°C
0.41
ethyl nicotinate
recombinant mutant C133A, pH 7.3, 37°C
0.1
ethylnicotinate
37°C, pH 7.3, mutant enzyme W83F
0.2
ethylnicotinate
37°C, pH 7.3, mutant enzyme H75E
0.2
ethylnicotinate
37°C, pH 7.3, mutant enzyme H75S
0.3
ethylnicotinate
37°C, pH 7.3, mutant enzyme A151C
1
ethylnicotinate
-
pH 7.3, temperature not specified in the publication
2.8
ethylnicotinate
37°C, pH 7.3, wild-type enzyme
0.31
methyl nicotinate
recombinant wild-type enzyme, pH 7.3, 37°C
0.38
methyl nicotinate
recombinant mutant Q96K, pH 7.3, 37°C
1.14
methyl nicotinate
recombinant mutant C133A, pH 7.3, 37°C
1.17
methyl nicotinate
recombinant mutant Q96A, pH 7.3, 37°C
1.4
methylnicotinate
37°C, pH 7.3, mutant enzyme W83F
2.8
methylnicotinate
37°C, pH 7.3, mutant enzyme H75S
14.1
methylnicotinate
37°C, pH 7.3, mutant enzyme H75E
19.7
methylnicotinate
-
pH 7.3, temperature not specified in the publication
20.5
methylnicotinate
37°C, pH 7.3, mutant enzyme A151C
50.5
methylnicotinate
37°C, pH 7.3, wild-type enzyme
0.0096
nicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
2.2
nicotinamide
mutant enzyme H53A, in 50 mM sodium phosphate (pH 7.5), at 25°C
4.15
nicotinamide
recombinant mutant Q96K, pH 7.3, 37°C
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
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
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
34
nicotinamide
recombinant mutant C133A, pH 7.3, 37°C
35
nicotinamide
kcat/Km above 35 (1/sec*mM), mutant enzyme D51N, in 50 mM sodium phosphate (pH 7.5), at 25°C
37
nicotinamide
-
mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C
39.7
nicotinamide
37°C, pH 7.3, mutant enzyme W83F
42.65
nicotinamide
recombinant mutant E65H, pH 7.3, 37°C
43.48
nicotinamide
recombinant wild-type enzyme, pH 7.3, 37°C
44.59
nicotinamide
recombinant mutant Q96A, pH 7.3, 37°C
51
nicotinamide
37°C, pH 7.3, mutant enzyme A151C
52.01
nicotinamide
recombinant mutant F68W, pH 7.3, 37°C
52.8
nicotinamide
recombinant mutant F68W/C133A, pH 7.3, 37°C
54.3
nicotinamide
37°C, pH 7.3, mutant enzyme H75S
68
nicotinamide
37°C, pH 7.3, mutant enzyme H75E
72
nicotinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
102
nicotinamide
-
pH 7.3, temperature not specified in the publication
189.2
nicotinamide
37°C, pH 7.3, wild-type enzyme
220
nicotinamide
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
427
nicotinamide
pH 7.5, 60°C
427
nicotinamide
pH and temperature not specified in the publication
3000
nicotinamide
pH and temperature not specified in the publication
0.157
Pyrazinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.39
Pyrazinamide
recombinant mutant Q96K, pH 7.3, 37°C
0.52
Pyrazinamide
recombinant mutant E65H, pH 7.3, 37°C
1.1
Pyrazinamide
37°C, pH 7.3, mutant enzyme W83F
1.34
Pyrazinamide
recombinant mutant Q96A, pH 7.3, 37°C
2.2
Pyrazinamide
37°C, pH 7.3, mutant enzyme H75S
3.2
Pyrazinamide
recombinant wild-type enzyme, pH 7.3, 37°C
5.2
Pyrazinamide
37°C, pH 7.3, mutant enzyme H75E
6.2
Pyrazinamide
-
mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C
6.28
Pyrazinamide
recombinant mutant F68W/C133A, pH 7.3, 37°C
7.9
Pyrazinamide
recombinant mutant F68W, pH 7.3, 37°C
9.19
Pyrazinamide
recombinant mutant C133A, pH 7.3, 37°C
13
Pyrazinamide
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
16
Pyrazinamide
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
34.1
Pyrazinamide
37°C, pH 7.3, mutant enzyme A151C
56.7
Pyrazinamide
37°C, pH 7.3, wild-type enzyme
69.9
Pyrazinamide
-
pH 7.3, temperature not specified in the publication
331
Pyrazinamide
pH 7.5, 60°C
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0.37 - 5
2-chloropyridine-3-carbaldehyde
0.316
3-acetylpyridine
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.085 - 2
3-Cyanopyridine
0.00029
3-pyridine carboxaldehyde
-
wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
0.00044 - 0.153
4-methoxylnicotinaldehyde
0.00007 - 0.0044
5-bromonicotinaldehyde
0.00059 - 0.004
5-bromopyridine-3-carbaldehyde
0.000039 - 0.0038
5-methoxypyridine-3-carbaldehyde
0.000023
5-methylnicotinaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.000023 - 0.00065
5-methylpyridine-3-carbaldehyde
0.004 - 0.018
6-fluoropyridine-3-carbaldehyde
0.0206
benzaldehyde
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.000011 - 0.0035
nicotinaldehyde
6.7
pyrazinoic acid
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.1
pyridine-3-carbonitrile
-
Ki about 0.1 mM, wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C
0.37
2-chloropyridine-3-carbaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
5
2-chloropyridine-3-carbaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.085
3-Cyanopyridine
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.5
3-Cyanopyridine
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
1
3-Cyanopyridine
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
2
3-Cyanopyridine
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.00044
4-methoxylnicotinaldehyde
-
isoform PNC2, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.001
4-methoxylnicotinaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.05
4-methoxylnicotinaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.068
4-methoxylnicotinaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.153
4-methoxylnicotinaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.00007
5-bromonicotinaldehyde
-
pH 7.3, temperature not specified in the publication, substrate: pyrazinamide
0.00147
5-bromonicotinaldehyde
37°C, pH 7.3
0.0044
5-bromonicotinaldehyde
recombinant wild-type enzyme, pH 7.3, 37°C
0.00059
5-bromopyridine-3-carbaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.004
5-bromopyridine-3-carbaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.000039
5-methoxypyridine-3-carbaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.000056
5-methoxypyridine-3-carbaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.00014
5-methoxypyridine-3-carbaldehyde
-
isoform PNC2, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.00031
5-methoxypyridine-3-carbaldehyde
-
isoform PNC1, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.00085
5-methoxypyridine-3-carbaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.0038
5-methoxypyridine-3-carbaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.000023
5-methylpyridine-3-carbaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.00019
5-methylpyridine-3-carbaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.00065
5-methylpyridine-3-carbaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.004
6-fluoropyridine-3-carbaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.018
6-fluoropyridine-3-carbaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.000011
nicotinaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.000015
nicotinaldehyde
-
pH 7.3, temperature not specified in the publication, substrate: pyrazinamide
0.000022
nicotinaldehyde
-
isoform PNC2, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.000034
nicotinaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.00011
nicotinaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.00011
nicotinaldehyde
-
isoform PNC1, in 100 mM phosphate buffer, pH 7.3 at 25°C
0.00018
nicotinaldehyde
37°C, pH 7.3
0.00094
nicotinaldehyde
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
0.0014
nicotinaldehyde
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
0.0035
nicotinaldehyde
recombinant wild-type enzyme, pH 7.3, 37°C
0.12
nicotinic acid
wild type enzyme, in 50 mM sodium phosphate (pH 7.5), at 25°C
2
nicotinic acid
-
in 100 mM phosphate buffer, pH 7.3 at 25°C
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evolution
-
nicotinamidases are a family of peptide hydrolases that generally contain a Zn2+ ion
malfunction
-
the generation of nicotinamidase null mutants leads to a decrease in NAD+ content, associated with a metabolic shutdown-like phenotype with an extensive lag phase of growth. The null mutants are also unable to establish a sustained infection in a mouse model
malfunction
deletion of this gene abolishes nicotinamide deamination activity in crude extracts of Thermus thermophilus and disrupts the NAD+ salvage pathway in Thermus thermophilus. Disruption of the salvage pathway leads to the severe growth retardation at a higher temperature (80°C), owing to the drastic decrease in the intracellular concentrations of NAD+ and NADH
malfunction
-
the mutant Yb2DELTApncA shows a similar growth rate but decreased NAD+ quantities in both the exponential and stationary phases in tryptic soy broth culture, compared with the wild-type strain Yb2. In addition, Yb2DELTApncA-infected ducks show much lower bacterial loads in their blood, and no visible histological changes were observed in the heart, liver, and spleen
malfunction
-
the mutant Yb2DELTApncA shows a similar growth rate but decreased NAD+ quantities in both the exponential and stationary phases in tryptic soy broth culture, compared with the wild-type strain Yb2. In addition, Yb2DELTApncA-infected ducks show much lower bacterial loads in their blood, and no visible histological changes were observed in the heart, liver, and spleen
-
malfunction
-
the generation of nicotinamidase null mutants leads to a decrease in NAD+ content, associated with a metabolic shutdown-like phenotype with an extensive lag phase of growth. The null mutants are also unable to establish a sustained infection in a mouse model
-
metabolism
-
nicotinamide phosphoribosyltransferase, Nampt, the equivalent enzyme in nicotinamide recycling to NAD+ in vertebrates, can functionally substitute for PNC-1
metabolism
-
the enzyme catalyzes the deamination of nicotinamide, which is an important step in the NAD+ salvage pathway. In Mycobacterium tuberculosis the enzyme converts the nicotinamide analogue prodrug pyrazinamide into the bacteriostatic pyrazinoic acid, hence the alternative name, pyrazinamidase, PncA
metabolism
-
the enzyme is involved in the NAD+ salvage pathway
metabolism
-
nicotinamidase is a key enzyme in NAD+ metabolism
metabolism
nicotinamidases catalyze the hydrolysis of nicotinamide to nicotinic acid and ammonia, an important reaction in the NAD+ salvage pathway
metabolism
-
nicotinamidases catalyze the hydrolysis of nicotinamide to nicotinic acid and ammonia, an important reaction in the NAD+ salvage pathway
-
metabolism
-
the enzyme is involved in the NAD+ salvage pathway
-
physiological function
-
the reaction product pyrazinoic acid inhibits Mycobacterium tuberculosis type I fatty acid synthase, represses mycolic acid biosynthesis, and appears to affect membrane energetics and acidification of the cytoplasm
physiological function
-
consistent with its centrality to NAD+ homeostasis, nicotinamidase is essential for viability
physiological function
-
consistent with its centrality to NAD+ homeostasis, nicotinamidase is essential for viability
physiological function
-
consistent with its centrality to NAD+ homeostasis, nicotinamidase is essential for viability
physiological function
-
consistent with its centrality to NAD+ homeostasis, nicotinamidase is essential for viability
physiological function
-
consistent with its centrality to NAD+ homeostasis, nicotinamidase is essential for viability
physiological function
-
Leishmania infantum nicotinamidase is required for late-stage intravectorial development in Phlebotomus perniciosus. Nicotinamide degradation by the parasitic nicotinamidase is important during blood meal digestion and especially for establishing mature infection after blood meal defecation
physiological function
-
Leishmania nicotinamidase is essential for NAD+ production and parasite proliferation
physiological function
the enzyme is involved in the maintenance of NAD+ homeostasis and in the NAD+ salvage pathway of most prokaryotes
physiological function
key enzyme of the NAD+ salvage pathway
physiological function
-
nicotinamidase is a key enzyme in the NAD+ salvage pathway
physiological function
-
the enzyme is an essential component of the NAD+ salvage pathway
physiological function
-
the enzyme is involved in degradation of nicotinamide
physiological function
-
nicotinamidases catalyze the hydrolysis of the amide bond in nicotinamide (NAM) to produce ammonia and nicotinic acid (NA). These enzymes are an essential component of the NAD+ salvage pathway and are implicated in the viability of several pathogenic organisms
physiological function
-
the enzyme is involved in the maintenance of NAD+ homeostasis and in the NAD+ salvage pathway of most prokaryotes
-
physiological function
-
nicotinamidase is a key enzyme in the NAD+ salvage pathway
-
physiological function
-
Leishmania nicotinamidase is essential for NAD+ production and parasite proliferation
-
additional information
-
a correlation between the limited detected expression patterns of the PNC-1a and b promoters and the function of PNC-1 in development is not obvious
additional information
-
catalytic mechanism, substrate binding and roles of active site residues, quantum mechanics/molecular mechanics methods and modeling, overview. The polar protein environment has a significant effect in stabilizing reaction intermediates and in particular transition states
additional information
protein conformational changes after ligand dissociation, molecular dynamics simulation methods are performed to investigate the unbinding process of nicotinamide using the enzyme's crystal structure, PDB ID 3O94, the C136S mutation in 3O94 is restored to the wild-type Cys residue
additional information
protein conformational changes after ligand dissociation, molecular dynamics simulation methods are performed to investigate the unbinding process of nicotinamide using the enzyme's crystal structure. PDB ID 2WT9
additional information
structural modeling of the enzyme homodimer, docking study and molecular dynamics simulations, overview
additional information
-
structural modeling of the enzyme homodimer, docking study and molecular dynamics simulations, overview
additional information
two for residues involved in the catalysis (K104 and Q96), one for the fourth residue involved in metal binding (E65), one for the residue forming hydrogen bonds between the main and lateral chains (T12), one for the residue involved in the cis-peptide bond and in the formation of the oxyanion hole (C133), and one for the residue forming one of the faces of the active site F68
additional information
-
combined whole-cell high-throughput functional screening for identification of nicotinamidases/pyrazinamidases in metagenomic/polygenomic libraries, screening of mesophilic marine bacteria (MB) polygenomic library. Development of two whole-cell methods using the chemical property of one of the products formed in the enzymatic reaction (pyrazinoic or NA) to form colored complexes with stable iron salts, such as ammonium ferrous sulfate or sodium nitroprusside (SNP), optimization of the assay. A fosmid polygenomic expression library obtained from deep-sea mesophilic bacteria is screened, discovering several positive clones with the ammonium ferrous sulfate method. Quantitative rescreening with the SNP method allowing the finding of the first nicotinamidase with balanced catalytic efficiency toward NAM (nicotinamidase activity) and pyrazinamide (pyrazinamidase activity). PolyNic contains all the conserved catalytic triad residues of the cysteine-hydrolases family:a catalytic cysteine at position 150, an aspartate at position 25, and a lysine at position 111. Other residues important for substrate and metal binding are F30, L36, W83, A112, Y120, and V149
additional information
-
two for residues involved in the catalysis (K104 and Q96), one for the fourth residue involved in metal binding (E65), one for the residue forming hydrogen bonds between the main and lateral chains (T12), one for the residue involved in the cis-peptide bond and in the formation of the oxyanion hole (C133), and one for the residue forming one of the faces of the active site F68
-
additional information
-
structural modeling of the enzyme homodimer, docking study and molecular dynamics simulations, overview
-
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C138A
-
significant decrease in enzyme activity
D49A
-
significant decrease in enzyme activity
D8A
-
significant decrease in enzyme activity
H51A
-
significant decrease in enzyme activity
H57A
-
significant decrease in enzyme activity
H57D
-
the mutant has reduced Mn2+ content and shows a 6fold and 38fold decrease in kcat value for nicotinamide and pyrazinamide, respectively
H71A
-
significant decrease in enzyme activity
K96A
-
significant decrease in enzyme activity
S104A
-
partial loss of enzyme activity
S95A
-
partial loss of enzyme activity
H57D
-
the mutant has reduced Mn2+ content and shows a 6fold and 38fold decrease in kcat value for nicotinamide and pyrazinamide, respectively
-
C133A
site-directed mutagenesis, the mutation affectes the active site cavity, and enhances the binding of pyrazinamide compared to the wild-type enzyme
E65H
site-directed mutagenesis, the mutation highly reduces the activity with pyrazinamide compared to the wild-type enzyme
F68W
site-directed mutagenesis, the mutation affectes the active site cavity, and enhances the binding of pyrazinamide compared to the wild-type enzyme
F68W/C133A
site-directed mutagenesis, the mutation affectes the active site cavity, and enhances the binding of pyrazinamide compared to the wild-type enzyme
K104A
site-directed mutagenesis, the mutant shows 98.55% reduced activity compared to the wild-type enzyme
Q96A
site-directed mutagenesis, the mutant shows similar activity with nicotinamide and increased activity with 5-methyl nicotinamide compared to the wild-type enzyme
Q96K
site-directed mutagenesis, the mutant shows 62.7% reduced activity compared to the wild-type enzyme
T12Q
site-directed mutagenesis, the mutant shows 98.42% reduced activity compared to the wild-type enzyme
C133A
-
site-directed mutagenesis, the mutation affectes the active site cavity, and enhances the binding of pyrazinamide compared to the wild-type enzyme
-
K104A
-
site-directed mutagenesis, the mutant shows 98.55% reduced activity compared to the wild-type enzyme
-
Q96A
-
site-directed mutagenesis, the mutant shows similar activity with nicotinamide and increased activity with 5-methyl nicotinamide compared to the wild-type enzyme
-
T12Q
-
site-directed mutagenesis, the mutant shows 98.42% reduced activity compared to the wild-type enzyme
-
D51A
the zinc-binding mutant shows decreased kcat value compared to the wild type enzyme
D51N
the zinc-binding mutant shows decreased kcat value compared to the wild type enzyme
D8A
the mutant shows 770fold decreased kcat value compared to the wild type enzyme
D8E
the mutant shows 100fold decreased kcat value compared to the wild type enzyme
D8N
the mutant shows 1000fold decreased kcat value compared to the wild type enzyme
H53A
the zinc-binding mutant shows decreased kcat value compared to the wild type enzyme
H94A
the zinc-binding mutant shows decreased kcat value compared to the wild type enzyme
K122A
the mutant shows 16fold decreased kcat value compared to the wild type enzyme
K122R
the mutant shows 770fold decreased kcat value compared to the wild type enzyme
C136A
-
the mutant is unable to catalyze nicotinamide hydrolysis
K103A
-
the mutant has only 0.15% of the catalytic activity of the native enzyme
R97A
-
the mutant is a robust nicotinamidase and is nearly as good as the native enzyme
C161A
-
inactive
C167A
-
site-directed mutagenesis, inactive mutant, no rescue the inhibition of NAD+-dependent histone deacetylase, i.e. HDAC, activity of Sir2 by nicotinamide
C167A
the mutant shows most strongly decreased kcat value compared to the wild type enzyme (below the assay detection limit)
C136S
inactive
C136S
-
the mutant is unable to catalyze nicotinamide hydrolysis
additional information
-
a gene disruption PncA mutant, a nicotinamidase/pyrazinamidase mutant, fails to replicate in HeLa cells and shows lower replication rates compared to the wild-type in macrophages, the mutant does not co-localize with host late endosomes or lysosomes, effects of gene disruption in vivo and in vitro, overview
additional information
-
a gene disruption PncA mutant, a nicotinamidase/pyrazinamidase mutant, fails to replicate in HeLa cells and shows lower replication rates compared to the wild-type in macrophages, the mutant does not co-localize with host late endosomes or lysosomes, effects of gene disruption in vivo and in vitro, overview
-
additional information
-
mutations in PNC-1 cause developmental and functional defects in the reproductive system. The development of the gonad is delayed, four uterine cells die by necrosis and the mutant animals are egg-laying defective. The temporal delay in gonad development results from depletion of the salvage pathway product NAD+, whereas the uv1 cell necrosis and egg-laying defects result from accumulation of the substrate nicotinamide, phenotype, overview. The bacterial food source partially compensates for pnc-1 reproductive defects. Although the secreted isoform is sufficient to rescue all phenotypes, the concentrations of NAD+ and nicotinamide in the cytoplasm and/or cellular organelles presumably elicit phenotypes
additional information
mutation of residues Cys133 and Phe68 is required for increasing pyrazinamidase activity 2.9 and 2.5fold, respectively. In addition, the change in the fourth residue involved in the ion metal binding (Glu65) is detrimental to pyrazinamidase activity decreasing it 6fold
additional information
-
mutation of residues Cys133 and Phe68 is required for increasing pyrazinamidase activity 2.9 and 2.5fold, respectively. In addition, the change in the fourth residue involved in the ion metal binding (Glu65) is detrimental to pyrazinamidase activity decreasing it 6fold
-
additional information
-
PNC1 overexpression suppresses the inhibitory effect of exogenously added nicotinamide on silencing, life span, and Hst1-mediated transcriptional repression
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Shibata, K.; Hayakawa, T.; Iwai, K.
Tissue distribution of the enzymes concerned with the biosynthesis of NAD in rats
Agric. Biol. Chem.
50
3037-3041
1986
Rattus norvegicus
-
brenda
Foster, J.W.; Brestel, C.
NAD metabolism in Vibrio cholerae
J. Bacteriol.
149
368-371
1982
Vibrio cholerae serotype O1
brenda
Sarma, D.S.; Rajalakshmi, S.; Sarma, P.
Studies on the enzymes involved in nicotinamide adenine dinucleotide metabolism in Aspergillus niger
Biochim. Biophys. Acta
81
311-322
1964
Aspergillus niger
-
brenda
Petrack, B.; Greengard, P.; Craston, N.; Sheppy, F.
Nicotinamide deaminase from mammalian liver
J. Biol. Chem.
240
1725-1730
1965
Oryctolagus cuniculus, Rattus norvegicus
brenda
Pardee, B.P.
Hyperproduction and purification of nicotinamide deamidase, a microconstitutive enzyme of Escherichia coli
J. Biol. Chem.
246
6792-6796
1971
Escherichia coli
brenda
Albizati, L.D.; Hedrick, J.L.
Active-site studies on rabbit liver nicotinamide deamidase
Biochemistry
11
1508-1516
1972
Oryctolagus cuniculus
brenda
Tanigawa, J.; Shimiyama, M.; Dohi, K.; Ueda, I.
Purification and properties of nicotinamide deamidase from Flavobacterium peregrinum
J. Biol. Chem.
247
8036-8042
1972
Flavobacterium peregrinum
brenda
Gillam, S.S.; Watson, J.G.; Chaykin, S.
Nicotinamide deamidase from rabbit liver. 3. Inhibition and sedimentation studies
Arch. Biochem. Biophys.
157
268-284
1973
Oryctolagus cuniculus
brenda
Gadd, R.E.A.; Johson, W.J.
Kinetic studies of nicotinamide deaminase from Micrococcus lysodeikticus
Int. J. Biochem.
5
397-407
1974
Micrococcus luteus
-
brenda
Johnson, W.J.; Gadd, R.E.A.
Inhibition of nicotinamide deaminase from Micrococcus lysodeikticus by analogues of nicotinamide
Int. J. Biochem.
5
633-641
1974
Micrococcus luteus
-
brenda
Foster, W.J.; Kinney, D.M.; Moat, A.G.
Pyridine nucleotide cycle of Salmonella typhimurium: regulation of nicotinic acid phosphoribosyltransferase and nicotinamide deamidase
J. Bacteriol.
138
957-961
1979
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Wintzerith, M.; Dierich, A.; Mandel, P.
Purification and characterization of a nicotinamide deamidase released into the growth medium of neuroblastoma in vitro
Biochim. Biophys. Acta
613
191-202
1980
Mus musculus
brenda
Fuller, L.
Determination of nicotinamide
Methods Enzymol.
66
3-4
1980
Saccharomyces cerevisiae
-
brenda
Tanigawa, Y.; Shimiyama, M.; Ueda, I.
Nicotinamide deamidase from Flavobacterium peregrinum
Methods Enzymol.
66
132-136
1980
Flavobacterium peregrinum
brenda
Yan, C.; Sloan, D.L.
Purification and characterization of nicotinamide deamidase from yeast
J. Biol. Chem.
262
9082-9087
1987
Saccharomyces cerevisiae
brenda
Frothingham, R.; Meeker-OConnell, W.A.; Talbot, E.A.S.; George, J.W.; Kreuzer K.N.
Identification, cloning, and expression of the Escherichia coli pyrazinamidase and nicotinamidase gene, pncA
Antimicrob. Agents Chemother.
40
1426-1431
1996
Escherichia coli
brenda
Sun, Z.; Zhang, Y.
Reduced pyrazinamidase activity and the natural resistance of Mycobacterium kansasii to the antituberculois drug pyrazinamide
Antimicrob. Agents Chemother.
43
537-542
1999
Mycobacterium kansasii
brenda
Guo, M.; Sun, Z.; Zhang, Y.
Mycobacterium smegmatis has two pyrazinamidase enzymes PncA and PzaA
J. Bacteriol.
182
3881-3884
2000
Mycolicibacterium smegmatis
brenda
Boshoff, H.I.; Mizrahi, V.
Purification, gene cloning, targeted knockout, overexpression, and biochemical characterization of the major pyrazinamidase from Mycobacterium smegmatis
J. Bacteriol.
180
5809-5814
1998
Mycobacterium tuberculosis, Mycolicibacterium smegmatis
brenda
Zrez, C.R.; Roth, E.F.; Schulman, S.; Tanaka, K.R.
Increased nicotinamideadenine dinucleotide content and synthesis in Plasmodium falciparum - infected human erythrocytes
Blood
75
1705-1710
1990
Plasmodium falciparum
brenda
Raynaud, C.; Etienne, G.; Peyron, P.; Laneelle, M.A.; Daffe, M.
Extracellular enzyme activities potentially involved in the pathogenicity of Mycobacterium tuberculosis
Microbiology
144
577-587
1998
Mycobacterium tuberculosis, Mycobacterium tuberculosis variant bovis, Mycolicibacterium fortuitum, Mycobacterium kansasii, Mycolicibacterium phlei
-
brenda
Kgayama, T.; Ohe, T.
Purification and properties of an aromatic amidase from Pseudomonas sp. GDI 211
Agric. Biol. Chem.
54
2565-2571
1990
Pseudomonas sp., Pseudomonas sp. GDI 211
-
brenda
Zheng, X.Q.; Hayashibe, E.; Ashihara, H.
Changes in trigonelline (N-methylnicotinic acid) content and nicotinic acid metabolism during germination of mungbean (Phaseolus aureus) seeds
J. Exp. Bot.
56
1615-1623
2005
Vigna radiata var. radiata
brenda
Kim, S.; Kurokawa, D.; Watanabe, K.; Makino, S.i.; Shirahata, T.; Watarai, M.
Brucella abortus nicotinamidase (PncA) contributes to its intracellular replication and infectivity in mice
FEMS Microbiol. Lett.
234
289-295
2004
Brucella abortus, Brucella abortus 544 / ATCC 23448
brenda
Gallo, C.M.; Smith, D.L.; Smith, J.S.
Nicotinamide clearance by Pnc1 directly regulates Sir2-mediated silencing and longevity
Mol. Cell. Biol.
24
1301-1312
2004
Saccharomyces cerevisiae
brenda
Hu, G.; Taylor, A.B.; McAlister-Henn, L.; Hart, P.J.
Crystal structure of the yeast nicotinamidase Pnc1p
Arch. Biochem. Biophys.
461
66-75
2007
Saccharomyces cerevisiae (P53184), Saccharomyces cerevisiae
brenda
Zhang, H.; Deng, J.Y.; Bi, L.J.; Zhou, Y.F.; Zhang, Z.P.; Zhang, C.G.; Zhang, Y.; Zhang, X.E.
Characterization of Mycobacterium tuberculosis nicotinamidase/pyrazinamidase
FEBS J.
275
753-762
2008
Mycobacterium tuberculosis
brenda
van der Horst, A.; Schavemaker, J.M.; Pellis-van Berkel, W.; Burgering, B.M.
The Caenorhabditis elegans nicotinamidase PNC-1 enhances survival
Mech. Ageing Dev.
128
346-349
2007
Caenorhabditis elegans
brenda
Wang, G.; Pichersky, E.
Nicotinamidase participates in the salvage pathway of NAD biosynthesis in Arabidopsis
Plant J.
49
1020-1029
2007
Arabidopsis thaliana
brenda
Hunt, L.; Holdsworth, M.J.; Gray, J.E.
Nicotinamidase activity is important for germination
Plant J.
51
341-351
2007
Arabidopsis thaliana
brenda
Chong, Z.Z.; Maiese, K.
Enhanced tolerance against early and late apoptotic oxidative stress in mammalian neurons through nicotinamidase and sirtuin mediated pathways
Curr. Neurovasc. Res.
5
159-170
2008
Drosophila melanogaster
brenda
McClure, J.M.; Gallo, C.M.; Smith, D.L.; Matecic, M.; Hontz, R.D.; Buck, S.W.; Racette, F.G.; Smith, J.S.
Pnc1p-mediated nicotinamide clearance modifies the epigenetic properties of rDNA silencing in Saccharomyces cerevisiae
Genetics
180
797-810
2008
Saccharomyces cerevisiae
brenda
Balan, V.; Miller, G.S.; Kaplun, L.; Balan, K.; Chong, Z.Z.; Li, F.; Kaplun, A.; VanBerkum, M.F.; Arking, R.; Freeman, D.C.; Maiese, K.; Tzivion, G.
Life span extension and neuronal cell protection by Drosophila nicotinamidase
J. Biol. Chem.
283
27810-27819
2008
Drosophila melanogaster
brenda
Yin, Y.; Matsui, A.; Sakuta, M.; Ashihara, H.
Changes in pyridine metabolism profile during growth of trigonelline-forming Lotus japonicus cell cultures
Phytochemistry
69
2891-2898
2008
Lotus japonicus
brenda
Fyfe, P.; Rao, V.; Zemla, A.; Cameron, S.; Hunter, W.
Specificity and mechanism of Acinetobacter baumanii nicotinamidase: Implications for activation of the front-line tuberculosis drug pyrazinamide
Angew. Chem. Int. Ed. Engl.
48
9176-9179
2009
Acinetobacter baumannii
brenda
Vrablik, T.L.; Huang, L.; Lange, S.E.; Hanna-Rose, W.
Nicotinamidase modulation of NAD+ biosynthesis and nicotinamide levels separately affect reproductive development and cell survival in C. elegans
Development
136
3637-3646
2009
Caenorhabditis elegans
brenda
French, J.B.; Cen, Y.; Vrablik, T.L.; Xu, P.; Allen, E.; Hanna-Rose, W.; Sauve, A.A.
Characterization of nicotinamidases: steady state kinetic parameters, classwide inhibition by nicotinaldehydes, and catalytic mechanism
Biochemistry
49
10421-10439
2010
Borreliella burgdorferi, Saccharomyces cerevisiae, Caenorhabditis elegans, Streptococcus pneumoniae, Plasmodium falciparum
brenda
French, J.B.; Cen, Y.; Sauve, A.A.; Ealick, S.E.
High-resolution crystal structures of Streptococcus pneumoniae nicotinamidase with trapped intermediates provide insights into the catalytic mechanism and inhibition by aldehydes
Biochemistry
49
8803-8812
2010
Streptococcus pneumoniae (A0A0H2UR34), Streptococcus pneumoniae
brenda
Seiner, D.R.; Hegde, S.S.; Blanchard, J.S.
Kinetics and inhibition of nicotinamidase from Mycobacterium tuberculosis
Biochemistry
49
9613-9619
2010
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Smith, B.C.; Anderson, M.A.; Hoadley, K.A.; Keck, J.L.; Cleland, W.W.; Denu, J.M.
Structural and kinetic isotope effect studies of nicotinamidase (Pnc1) from Saccharomyces cerevisiae
Biochemistry
51
243-256
2012
Saccharomyces cerevisiae (P53184), Saccharomyces cerevisiae
brenda
Gazanion, E.; Seblova, V.; Votypka, J.; Vergnes, B.; Garcia, D.; Volf, P.; Sereno, D.
Leishmania infantum nicotinamidase is required for late-stage development in its natural sand fly vector, Phlebotomus perniciosus
Int. J. Parasitol.
42
323-327
2012
Leishmania infantum
brenda
Gazanion, E.; Garcia, D.; Silvestre, R.; Gerard, C.; Guichou, J.F.; Labesse, G.; Seveno, M.; Cordeiro-Da-Silva, A.; Ouaissi, A.; Sereno, D.; Vergnes, B.
The Leishmania nicotinamidase is essential for NAD+ production and parasite proliferation
Mol. Microbiol.
82
21-38
2011
Leishmania infantum, Leishmania infantum MHOM/MA/67/ITMAP-263
brenda
Stekhanova, T.N.; Bezsudnova, E.Y.; Mardanov, A.V.; Osipov, E.M.; Ravin, N.V.; Skryabin, K.G.; Popov, V.O.
Nicotinamidase from the thermophilic archaeon Acidilobus saccharovorans: structural and functional characteristics
Biochemistry
79
54-61
2014
Acidilobus saccharovorans (D9Q1R5), Acidilobus saccharovorans, Acidilobus saccharovorans DSM 16705 (D9Q1R5)
brenda
Stekhanova, T.N.; Bezsudnova, E.Y.; Mardanov, A.V.; Osipov, E.M.; Ravin, N.V.; Skryabin, K.G.; Popov, V.O.
Nicotinamidase from the thermophilic archaeon Acidilobus saccharovorans: structural and functional characteristics
Biochemistry (Moscow)
79
54-61
2014
Acidilobus saccharovorans (D9Q1R5), Acidilobus saccharovorans, Acidilobus saccharovorans DSM 16705 (D9Q1R5)
brenda
Ion, B.F.; Kazim, E.; Gauld, J.W.
A multi-scale computational study on the mechanism of Streptococcus pneumoniae nicotinamidase (SpNic)
Molecules
19
15735-15753
2014
Streptococcus pneumoniae
brenda
Zhang, J.L.; Zheng, Q.C.; Li, Z.Q.; Zhang, H.X.
Molecular dynamics simulations suggest ligands binding to nicotinamidase/pyrazinamidase
PLoS ONE
7
e39546
2012
Streptococcus pneumoniae (A0A0H2UR34), Acinetobacter baumannii (B0VA03)
brenda
Sanchez-Carron, G.; Garcia-Garcia, M.I.; Zapata-Perez, R.; Takami, H.; Garcia-Carmona, F.; Sanchez-Ferrer, A.
Biochemical and mutational analysis of a novel nicotinamidase from Oceanobacillus iheyensis HTE831
PLoS ONE
8
e56727
2013
Oceanobacillus iheyensis (Q8ESQ6), Oceanobacillus iheyensis HTE831 (Q8ESQ6), Oceanobacillus iheyensis HTE831
brenda
Rueda, D.; Sheen, P.; Gilman, R.H.; Bueno, C.; Santos, M.; Pando-Robles, V.; Batista, C.V.; Zimic, M.
Nicotinamidase/pyrazinamidase of Mycobacterium tuberculosis forms homo-dimers stabilized by disulfide bonds
Tuberculosis
94
644-648
2014
Mycobacterium tuberculosis (I6XD65), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (I6XD65)
brenda
Wang, X.; Liu, B.; Dou, Y.; Fan, H.; Wang, S.; Li, T.; Ding, C.; Yu, S.
The Riemerella anatipestifer AS87_01735 gene encodes nicotinamidase PncA, an important virulence factor
Appl. Environ. Microbiol.
82
5815-5823
2016
Riemerella anatipestifer, Riemerella anatipestifer Yb2
brenda
Shang, F.; Chen, J.; Wang, L.; Jin, L.; Zou, L.; Bu, T.; Dong, Y.; Ha, N.C.; Nam, K.H.; Quan, C.; Xu, Y.
Crystal structure of the nicotinamidase/pyrazinamidase PncA from Bacillus subtilis
Biochem. Biophys. Res. Commun.
503
2906-2911
2018
Bacillus velezensis (A0A223CGG0)
brenda
Zapata-Perez, R.; Garcia-Saura, A.G.; Jebbar, M.; Golyshin, P.N.; Sanchez-Ferrer, A.
Combined whole-cell high-throughput functional screening for identification of new nicotinamidases/pyrazinamidases in metagenomic/polygenomic libraries
Front. Microbiol.
7
1915
2016
uncultured bacterium, no activity in Homo sapiens, unidentified
brenda
Taniguchi, H.; Sungwallek, S.; Chotchuang, P.; Okano, K.; Honda, K.
A key enzyme of the NAD+ salvage pathway in Thermus thermophilus characterization of nicotinamidase and the impact of its gene deletion at high temperatures
J. Bacteriol.
199
e00359-17
2017
Thermus thermophilus (Q5SLG5), Thermus thermophilus
brenda
Zapata-Perez, R.; Martinez-Monino, A.B.; Garcia-Saura, A.G.; Cabanes, J.; Takami, H.; Sanchez-Ferrer, A.
Biochemical characterization of a new nicotinamidase from an unclassified bacterium thriving in a geothermal water stream microbial mat community
PLoS ONE
12
e0181561
2017
uncultured Acidobacteria bacterium (H5SPS2)
brenda
Hu, C.; Zhao, S.; Li, K.; Yu, H.
Microbial degradation of nicotinamide by a strain Alcaligenes sp. P156
Sci. Rep.
9
3647
2019
Alcaligenes sp. P156
brenda