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Enzyme Nomenclature
Information on EC 3.5.1.B15 - pyrazinamidase
for references in articles please use BRENDA:EC3.5.1.B15
Word Map on EC 3.5.1.B15
- 3.5.1.B15
- mycobacterium
- tuberculosis
- pzase
-
pyrazinoic
-
pyrazinamide-resistant
-
pza-resistant
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bactec
- nicotinamidase
- enterocolitica
-
wayne
-
autoagglutination
-
mycolic
-
mdr-tb
- kristensenii
-
pza-susceptible
-
middlebrooks
- kansasii
-
spoligotype
- frederiksenii
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The expected taxonomic range for this enzyme is: Archaea, Bacteria
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EC NUMBER 
COMMENTARY 
3.5.1.B15
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
pyrazinamidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pyrazinamide + H2O = pyrazinoic acid + NH3
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-
-
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SYSTEMATIC NAME
IUBMB Comments
pyrazinamide amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
39419-71-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
in Mycobacterium tuberculosis the enzyme converts the nicotinamide analogue prodrug pyrazinamide into the bacteriostatic pyrazinoic acid
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
additional information
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
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structural modeling of the enzyme homodimer, docking study and molecular dynamics simulations, overview
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nicotinamide + H2O
nicotinate + NH3
binding structure involving residues A155, C159, and Ile154, and unbinding mechanism, modeling, overview
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
the enzyme also catalyzes the hydrolysis of nicotinamide
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
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the enzyme also catalyzes the hydrolysis of nicotinamide
-
-
?
pyrazinamide + H2O
pyrazinoic acid + NH3
-
a nicotinamide prodrug. In Mycobacterium tuberculosis the enzyme converts the nicotinamide analogue prodrug pyrazinamide into the bacteriostatic pyrazinoic acid
a bacteriostatic drug
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyrazinamide + H2O
pyrazinoic acid + NH3
-
a nicotinamide prodrug. In Mycobacterium tuberculosis the enzyme converts the nicotinamide analogue prodrug pyrazinamide into the bacteriostatic pyrazinoic acid
a bacteriostatic drug
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Zn2+
Zn2+
-
activates, best cation, the active site Cys159 is located at the N-terminus of a6 at one side of the active site with the Zn2+ ion positioned on the other side. The metal ion is bound tightly in the AbPncA active site
Zn2+
Zn2+ increases the kcat of the enzyme by about 19-fold. fold. Other divalent ions, including Mg2+, Mn2+, Ca2+, and Cd2+, do not increase the activity. A metal ion-binding site is revealed in the active site and confirmed by crystal structure of the enzyme in complex with Zn2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
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
homodimer
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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
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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
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
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure (PDB ID 2WT9) analysis, and modeling of substrate binding and unbinding, overview
three-dimensional structure of pyrazinamidase at 2.05 A resolution and the structure of its complex with Zn2+ at 1.65 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography, ultrafiltration, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in a methionine auxotroph, Escherichia coli strain B834
gene pncA, DNA and amino acid sequence determination and analysis, recombinant enzyme expression in Escherichia coli strain BL21(DE3)pLysS
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LINKS TO OTHER DATABASES (specific for EC-Number 3.5.1.B15)
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