BRENDA - Enzyme Database show
show all sequences of 3.5.1.B15

Nicotinamidase/pyrazinamidase of Mycobacterium tuberculosis forms homo-dimers stabilized by disulfide bonds

Rueda, D.; Sheen, P.; Gilman, R.H.; Bueno, C.; Santos, M.; Pando-Robles, V.; Batista, C.V.; Zimic, M.; Tuberculosis 94, 644-648 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene pncA, DNA and amino acid sequence determination and analysis, recombinant enzyme expression in Escherichia coli strain BL21(DE3)pLysS
Mycobacterium tuberculosis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
39700
-
dimeric enzyme, gel filtration
Mycobacterium tuberculosis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
nicotinamide + H2O
Mycobacterium tuberculosis
-
nicotinate + NH3
-
-
?
nicotinamide + H2O
Mycobacterium tuberculosis H37Rv
-
nicotinate + NH3
-
-
?
pyrazinamide + H2O
Mycobacterium tuberculosis
-
pyrazinoic acid + NH3
-
-
?
pyrazinamide + H2O
Mycobacterium tuberculosis H37Rv
-
pyrazinoic acid + NH3
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mycobacterium tuberculosis
I6XD65
gene pncA
-
Mycobacterium tuberculosis H37Rv
I6XD65
gene pncA
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and gel filtration
Mycobacterium tuberculosis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
nicotinamide + H2O
-
735324
Mycobacterium tuberculosis
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
-
735324
Mycobacterium tuberculosis H37Rv
nicotinate + NH3
-
-
-
?
pyrazinamide + H2O
-
735324
Mycobacterium tuberculosis
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
-
735324
Mycobacterium tuberculosis H37Rv
pyrazinoic acid + NH3
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 20500-20700, about, recombinant enzyme, SDS-PAGE and mass spectrometry. Homodimers show a slightly lower specific enzyme activity compared to monomers. Enzyme dimers are dissociated into monomers in response to reducing conditions, disulfide bonds C72-C138 and C138-C138 stabilize the quaternary structure of the enzyme homodimer, quarternary structure analysis, structural model of enzyme homodimer, overview
Mycobacterium tuberculosis
monomer
1 * 20500-20700, about, recombinant enzyme, SDS-PAGE and mass spectrometry. Homodimers show a slightly lower specific enzyme activity compared to monomers. Enzyme dimers are dissociated into monomers in response to reducing conditions, disulfide bonds C72-C138 and C138-C138 stabilize the quaternary structure of the enzyme homodimer, quarternary structure analysis, overview
Mycobacterium tuberculosis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene pncA, DNA and amino acid sequence determination and analysis, recombinant enzyme expression in Escherichia coli strain BL21(DE3)pLysS
Mycobacterium tuberculosis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
39700
-
dimeric enzyme, gel filtration
Mycobacterium tuberculosis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
nicotinamide + H2O
Mycobacterium tuberculosis
-
nicotinate + NH3
-
-
?
nicotinamide + H2O
Mycobacterium tuberculosis H37Rv
-
nicotinate + NH3
-
-
?
pyrazinamide + H2O
Mycobacterium tuberculosis
-
pyrazinoic acid + NH3
-
-
?
pyrazinamide + H2O
Mycobacterium tuberculosis H37Rv
-
pyrazinoic acid + NH3
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and gel filtration
Mycobacterium tuberculosis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
nicotinamide + H2O
-
735324
Mycobacterium tuberculosis
nicotinate + NH3
-
-
-
?
nicotinamide + H2O
-
735324
Mycobacterium tuberculosis H37Rv
nicotinate + NH3
-
-
-
?
pyrazinamide + H2O
-
735324
Mycobacterium tuberculosis
pyrazinoic acid + NH3
-
-
-
?
pyrazinamide + H2O
-
735324
Mycobacterium tuberculosis H37Rv
pyrazinoic acid + NH3
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 20500-20700, about, recombinant enzyme, SDS-PAGE and mass spectrometry. Homodimers show a slightly lower specific enzyme activity compared to monomers. Enzyme dimers are dissociated into monomers in response to reducing conditions, disulfide bonds C72-C138 and C138-C138 stabilize the quaternary structure of the enzyme homodimer, quarternary structure analysis, structural model of enzyme homodimer, overview
Mycobacterium tuberculosis
monomer
1 * 20500-20700, about, recombinant enzyme, SDS-PAGE and mass spectrometry. Homodimers show a slightly lower specific enzyme activity compared to monomers. Enzyme dimers are dissociated into monomers in response to reducing conditions, disulfide bonds C72-C138 and C138-C138 stabilize the quaternary structure of the enzyme homodimer, quarternary structure analysis, overview
Mycobacterium tuberculosis
General Information
General Information
Commentary
Organism
additional information
structural modeling of the enzyme homodimer, docking study and molecular dynamics simulations, overview
Mycobacterium tuberculosis
General Information (protein specific)
General Information
Commentary
Organism
additional information
structural modeling of the enzyme homodimer, docking study and molecular dynamics simulations, overview
Mycobacterium tuberculosis
Other publictions for EC 3.5.1.B15
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
Biochemistry
79
54-61
2014
-
-
1
-
-
-
1
1
-
1
1
-
-
1
-
-
-
-
-
-
-
-
2
1
1
-
2
1
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
1
-
1
1
-
-
-
-
-
-
-
-
-
2
1
1
-
2
1
1
-
-
-
-
-
-
-
1
1
735324
Rueda
Nicotinamidase/pyrazinamidase ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Tuberculosis
94
644-648
2014
-
-
1
-
-
-
-
-
-
-
1
4
-
2
-
-
1
-
-
-
-
-
4
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
4
-
-
-
1
-
-
-
-
4
2
-
-
-
-
-
-
-
-
-
1
1
-
-
-
735054
Zhang
Molecular dynamics simulations ...
Acinetobacter baumannii
PLoS ONE
7
e39546
2012
-
-
-
1
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
710862
Fyfe
Specificity and mechanism of A ...
Acinetobacter baumannii
Angew. Chem. Int. Ed. Engl.
48
9176-9179
2009
-
-
-
-
-
-
-
-
-
4
1
1
-
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
1
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
744296
Du
Crystal structure and mechani ...
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Biochemistry
40
14166-14172
2001
-
-
1
1
-
-
-
-
-
1
-
-
-
6
-
-
1
-
-
-
3
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
3
-
2
-
-
-
-
-
-
-
-
-
-
-
-
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-