3.5.1.19: nicotinamidase
This is an abbreviated version!
For detailed information about nicotinamidase, go to the full flat file.
Word Map on EC 3.5.1.19
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3.5.1.19
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mycobacterium
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tuberculosis
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pyrazinamide
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pyrazinoic
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pza-resistant
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bactec
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pyrazinamide-resistant
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sir2-dependent
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kansasii
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wayne
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sir2-mediated
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pza-susceptible
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analysis
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drug development
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medicine
- 3.5.1.19
- mycobacterium
- tuberculosis
- pyrazinamide
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pyrazinoic
-
pza-resistant
-
bactec
-
pyrazinamide-resistant
-
sir2-dependent
- kansasii
-
wayne
-
sir2-mediated
-
pza-susceptible
- analysis
- drug development
- medicine
Reaction
Synonyms
AS87_01735, ASAC_0847, NAAA, NA_As0847, NIC, nicotinamidase, nicotinamidase PNC-1, nicotinamidase Pnc1p, nicotinamidase PncA, nicotinamidase/pyrazinamidase, nicotinamidase/pyrazinamidase PncA, nicotinamide amidase, nicotinamide deaminase, Nicotine deamidase, OiNIC, PNC-1, Pnc1, Pnc1p, PNC2, PncA, polygenomic nicotinamidase, PolyNic, pyrazinamidase, PZAase, PZAse, SpNic, TTHA0328, UbNic, YNDase
ECTree
3.5.1.19 nicotinamidaseAdvanced search results
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results (Engineering
Engineering on EC 3.5.1.19 - nicotinamidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C161A
H57D
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the mutant has reduced Mn2+ content and shows a 6fold and 38fold decrease in kcat value for nicotinamide and pyrazinamide, respectively
H57D
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the mutant has reduced Mn2+ content and shows a 6fold and 38fold decrease in kcat value for nicotinamide and pyrazinamide, respectively
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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
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site-directed mutagenesis, the mutation affectes the active site cavity, and enhances the binding of pyrazinamide compared to the wild-type enzyme
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K104A
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site-directed mutagenesis, the mutant shows 98.55% reduced activity compared to the wild-type enzyme
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Q96A
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site-directed mutagenesis, the mutant shows similar activity with nicotinamide and increased activity with 5-methyl nicotinamide compared to the wild-type enzyme
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T12Q
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site-directed mutagenesis, the mutant shows 98.42% reduced activity compared to the wild-type enzyme
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C167A
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
C136S
K103A
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the mutant has only 0.15% of the catalytic activity of the native enzyme
R97A
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the mutant is a robust nicotinamidase and is nearly as good as the native enzyme
additional information
C167A
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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)
additional information
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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
Brucella abortus 544 / ATCC 23448
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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
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additional information
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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
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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
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additional information
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PNC1 overexpression suppresses the inhibitory effect of exogenously added nicotinamide on silencing, life span, and Hst1-mediated transcriptional repression
