3.5.1.B15: pyrazinamidase
This is an abbreviated version!
For detailed information about pyrazinamidase, go to the full flat file.
Word Map on EC 3.5.1.B15
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3.5.1.B15
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tuberculosis
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mycobacterium
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pzase
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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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enterocolitica
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wayne
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mdr-tb
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middlebrooks
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autoagglutination
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pza-susceptible
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kristensenii
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kansasii
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diagnostics
- 3.5.1.B15
- tuberculosis
- mycobacterium
- pzase
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pyrazinoic
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pza-resistant
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bactec
-
pyrazinamide-resistant
- enterocolitica
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wayne
-
mdr-tb
-
middlebrooks
-
autoagglutination
-
pza-susceptible
- kristensenii
- kansasii
- diagnostics
Reaction
Synonyms
ASAC_0847, BsPncA, More, nicotinamidase/pyrazinamidase, PH0999, PncA, PolyNic, pyrazinamidase, pyrazinamidase/nicotinamidase, PZAase, PZAse
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3.5.1.B15 pyrazinamidaseAdvanced search results
results (
results (Subunits
Subunits on EC 3.5.1.B15 - pyrazinamidase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer or tetramer
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the structure of BsPncA consists of an alpha/beta domain and a subdomain. The subdomain of BsPncA has a different conformation compared to PncA enzymes from other organisms. The B-factor analysis reveals a rigid structure of the alpha/beta domain, while the subdomain is highly flexible. Both dimers and tetramers are observed in BsPncA protein crystals, but only dimers are observed in solution
homodimer
monomer
additional information
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
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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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additional information
enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1)
additional information
enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1)
additional information
enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1)
additional information
PZase consists of six parallel beta-sheets surrounded by alpha-helices. The metal binding site contains iron (Fe2+ ion) in coordination with one aspartate (Asp49) and three histidines residues (His51, His57, and His71), while Asp8, Lys96, and Cys138 form the catalytic triad
additional information
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PZase consists of six parallel beta-sheets surrounded by alpha-helices. The metal binding site contains iron (Fe2+ ion) in coordination with one aspartate (Asp49) and three histidines residues (His51, His57, and His71), while Asp8, Lys96, and Cys138 form the catalytic triad
additional information
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PZase consists of six parallel beta-sheets surrounded by alpha-helices. The metal binding site contains iron (Fe2+ ion) in coordination with one aspartate (Asp49) and three histidines residues (His51, His57, and His71), while Asp8, Lys96, and Cys138 form the catalytic triad
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additional information
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PZase consists of six parallel beta-sheets surrounded by alpha-helices. The metal binding site contains iron (Fe2+ ion) in coordination with one aspartate (Asp49) and three histidines residues (His51, His57, and His71), while Asp8, Lys96, and Cys138 form the catalytic triad
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additional information
enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1)
additional information
enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1)
additional information
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enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1)
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additional information
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enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1)
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additional information
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enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1)
-
additional information
-
enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1)
-
additional information
-
enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1)
-
additional information
-
enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1)
-
additional information
enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1)
