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Literature summary extracted from

  • Prabhavadhni, A.; Gorai, B.; Visalakshi, P.; Sivaraman, T.
    In silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium (2015), J. Pharm. Sci. Res., 7, 416-419 .
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.B15 additional information in silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium Mycobacterium tuberculosis variant bovis
3.5.1.B15 additional information in silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium Mycobacterium kansasii
3.5.1.B15 additional information in silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium Mycobacterium avium
3.5.1.B15 additional information in silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium Mycolicibacterium smegmatis
3.5.1.B15 additional information in silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium Mycobacteroides abscessus
3.5.1.B15 additional information in silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium Mycobacterium marinum

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.B15 Mycobacterium avium P94914
-
-
3.5.1.B15 Mycobacterium kansasii O07691
-
-
3.5.1.B15 Mycobacterium marinum A0A3E2MTZ2
-
-
3.5.1.B15 Mycobacterium tuberculosis variant bovis U5TP36
-
-
3.5.1.B15 Mycobacteroides abscessus B1MLY1 i.e. Mycobacterium abscessus
-
3.5.1.B15 Mycobacteroides abscessus ATCC 19977 B1MLY1 i.e. Mycobacterium abscessus
-
3.5.1.B15 Mycobacteroides abscessus CIP 104536 B1MLY1 i.e. Mycobacterium abscessus
-
3.5.1.B15 Mycobacteroides abscessus DSM 44196 B1MLY1 i.e. Mycobacterium abscessus
-
3.5.1.B15 Mycobacteroides abscessus JCM 13569 B1MLY1 i.e. Mycobacterium abscessus
-
3.5.1.B15 Mycobacteroides abscessus NCTC 13031 B1MLY1 i.e. Mycobacterium abscessus
-
3.5.1.B15 Mycobacteroides abscessus TMC 1543 B1MLY1 i.e. Mycobacterium abscessus
-
3.5.1.B15 Mycolicibacterium smegmatis Q9ZF59
-
-

Subunits

EC Number Subunits Comment Organism
3.5.1.B15 More enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1) Mycobacterium tuberculosis variant bovis
3.5.1.B15 More enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1) Mycobacterium kansasii
3.5.1.B15 More enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1) Mycobacterium avium
3.5.1.B15 More enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1) Mycolicibacterium smegmatis
3.5.1.B15 More enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1) Mycobacteroides abscessus
3.5.1.B15 More enzyme structure comparison with the crystal structure of pyrazinamidase of Mycobacterium tuberculosis (PDB ID 3PL1) Mycobacterium marinum

Synonyms

EC Number Synonyms Comment Organism
3.5.1.B15 PncA
-
 Mycobacterium tuberculosis variant bovis
3.5.1.B15 PncA
-
 Mycobacterium kansasii
3.5.1.B15 PncA
-
 Mycobacterium avium
3.5.1.B15 PncA
-
 Mycolicibacterium smegmatis
3.5.1.B15 PncA
-
 Mycobacteroides abscessus
3.5.1.B15 PncA
-
 Mycobacterium marinum
3.5.1.B15 PZAse
-
 Mycobacterium tuberculosis variant bovis
3.5.1.B15 PZAse
-
 Mycobacterium kansasii
3.5.1.B15 PZAse
-
 Mycobacterium avium
3.5.1.B15 PZAse
-
 Mycolicibacterium smegmatis
3.5.1.B15 PZAse
-
 Mycobacteroides abscessus
3.5.1.B15 PZAse
-
 Mycobacterium marinum

General Information

EC Number General Information Comment Organism
3.5.1.B15 malfunction Mycobacterium abscessus is resistant to pyrazinamide due to the random mutations in the primary sequences of the pyrazinamidase. In silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium Mycobacteroides abscessus
3.5.1.B15 malfunction Mycobacterium avium is resistant to pyrazinamide due to the random mutations in the primary sequences of the pyrazinamidase. In silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium Mycobacterium avium
3.5.1.B15 malfunction Mycobacterium bovis is resistant to pyrazinamide due to the random mutations in the primary sequences of the pyrazinamidase. In silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium Mycobacterium tuberculosis variant bovis
3.5.1.B15 malfunction Mycobacterium kansasii is resistant to pyrazinamide due to the random mutations in the primary sequences of the pyrazinamidase. In silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium Mycobacterium kansasii
3.5.1.B15 malfunction Mycobacterium marinum is resistant to pyrazinamide due to the random mutations in the primary sequences of the pyrazinamidase. In silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium Mycobacterium marinum
3.5.1.B15 malfunction Mycobacterium smegmatis is resistant to pyrazinamide due to the random mutations in the primary sequences of the pyrazinamidase. In silico structural characterizations of pyrazinamidase variants from various species of Mycobacterium Mycolicibacterium smegmatis
3.5.1.B15 additional information the substrate binding site involves residues D8, F13, D49, K96, I133, A135, H137, and C138, binding sites architectures and GATE analysis, molecular dynamics simulations, overview Mycobacterium tuberculosis variant bovis
3.5.1.B15 additional information the substrate binding site involves residues D8, F13, D49, K96, I133, A135, H137, and C138, binding sites architectures and GATE analysis, molecular dynamics simulations, overview Mycobacterium kansasii
3.5.1.B15 additional information the substrate binding site involves residues D8, F13, D49, K96, I133, A135, H137, and C138, binding sites architectures and GATE analysis, molecular dynamics simulations, overview Mycobacterium avium
3.5.1.B15 additional information the substrate binding site involves residues D8, F13, D49, K96, I133, A135, H137, and C138, binding sites architectures and GATE analysis, molecular dynamics simulations, overview Mycolicibacterium smegmatis
3.5.1.B15 additional information the substrate binding site involves residues D8, F13, D49, K96, I133, A135, H137, and C138, binding sites architectures and GATE analysis, molecular dynamics simulations, overview Mycobacteroides abscessus
3.5.1.B15 additional information the substrate binding site involves residues D8, F13, D49, K96, I133, A135, H137, and C138, binding sites architectures and GATE analysis, molecular dynamics simulations, overview Mycobacterium marinum