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Literature summary for 1.11.1.21 extracted from

  • Unissa, A.N.; Doss C, G.P.; Kumar, T.; Sukumar, S.; Lakshmi, A.R.; Hanna, L.E.
    Significance of catalase-peroxidase (KatG) mutations in mediating isoniazid resistance in clinical strains of Mycobacterium tuberculosis (2018), J. Glob. Antimicrob. Resist., 15, 111-120 .
    View publication on PubMed
Search for more literature for 1.11.1.21

Protein Variants

Protein Variants Comment Organism
S315G site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type Mycobacterium tuberculosis
S315I site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type Mycobacterium tuberculosis
S315N site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type Mycobacterium tuberculosis
S315R site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type Mycobacterium tuberculosis
S315T site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
isoniazid mutation at position 315 in the katG gene, encoding the catalase-peroxidase (KatG) enzyme, is the major cause of isoniazid (INH) resistance in Mycobacterium tuberculosis. INH resistance is regarded as a major impediment to the tuberculosis (TB) control programme and contributes to the emergence of multidrug-resistant strains. Analysis of the molecular mechanisms of INH resistance, overview. The five KatG mutations, S315T, S315I, S315R, S315N and S315G, affect enzyme activity in different ways, which can be attributed to conformational changes in mutant KatG that result in altered binding affinity to INH and eventually to INH resistance, docking study. Analysis of molecular dynamics (MD) experiments suggest that fluctuations and deviations are higher at the INH binding residues for the mutants than for the wild-type. Reduction in the hydrogen bond network after MD in all KatG enzymes implies an increase in the flexibility and stability of protein structures. Since KatG is a conjugated protein, docking is first done with heme, and then it is further docked with INH Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in the heme group Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WIE5
-
-
Mycobacterium tuberculosis ATCC 25618 P9WIE5
-
-
Mycobacterium tuberculosis H37Rv P9WIE5
-
-

Synonyms

Synonyms Comment Organism
KatG
-
 Mycobacterium tuberculosis
Rv1908c
-
 Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
heme docking study with wild-type and mutant enzymes, molecular dynamics, overview Mycobacterium tuberculosis

General Information

General Information Comment Organism
malfunction mutation at position 315 in the katG gene, encoding the catalase-peroxidase (KatG) enzyme, is the major cause of isoniazid (INH) resistance in Mycobacterium tuberculosis. INH resistance is regarded as a major impediment to the tuberculosis (TB) control programme and contributes to the emergence of multidrug-resistant strains. Analysis of the molecular mechanisms of INH resistance, overview. The five KatG mutations, S315T, S315I, S315R, S315N and S315G , affect enzyme activity in different ways, which can be attributed to conformational changes in mutant KatG that result in altered binding affinity to INH and eventually to INH resistance, docking study. Analysis of molecular dynamics (MD) experiments suggest that fluctuations and deviations are higher at the INH binding residues for the mutants than for the wild-type. Reduction in the hydrogen bond network after MD in all KatG enzymes implies an increase in the flexibility and stability of protein structures. Since KatG is a conjugated protein, docking is first done with heme, and then it is further docked with INH Mycobacterium tuberculosis