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Literature summary for 1.11.1.21 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)

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

Protein Variants

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Subunits

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

Synonyms

Synonyms Comment Organism
KatG
-
Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
heme
-
Mycobacterium tuberculosis

General Information

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