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Literature summary extracted from

  • Nagy, J.; Jesmin, J.; Servos, S.; Cass, A.; Brown, K.
    Site-directed mutants of the catalase-peroxidase from Mycobacterium tuberculosis (1998), Biochem. Soc. Trans., 26, S281.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.21 mutant enzymes are expressed in Escherichia coli strain UM255, lacking endogenous catalase Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.21 H108E isoniazid-resistant clinical mutant Mycobacterium tuberculosis
1.11.1.21 H108L the mutant has lost both peroxidatic and catalatic activities Mycobacterium tuberculosis
1.11.1.21 H52L isoniazid-resistant clinical mutant Mycobacterium tuberculosis
1.11.1.21 R463L isoniazid-resistant clinical mutant, which has retained peroxidatic and catalatic activities Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.11.1.21 80000
-
 x * 80000, SDS-PAGE Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.21 Mycobacterium tuberculosis
-
-
-

Subunits

EC Number Subunits Comment Organism
1.11.1.21 ? x * 80000, SDS-PAGE Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
1.11.1.21 KatG
-
 Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.21 heme
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
1.11.1.21 malfunction Mycobacterium tuberculosis isolates with defects in the kutG gene encoding a catalase-peroxidase enzyme exhibit resistance to isoniazid Mycobacterium tuberculosis