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Literature summary extracted from

  • Johnsson, K.; Froland, W.A.; Schultz, P.G.
    Overexpression, purification, and characterization of the catalase-peroxidase KatG from Mycobacterium tuberculosis (1997), J. Biol. Chem., 272, 2834-2840.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.21 expressed in Escherichia coli strain UM262 Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.21 R463L the mutation is found in isoniazid-resistant strains and does not lead to a loss of peroxidase or catalase activity Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.11.1.21 cyanide
-
 Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.21 5.18
-
 H2O2 wild type enzyme, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C Mycobacterium tuberculosis
1.11.1.21 6.16
-
 H2O2 mutant enzyme R463L, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.11.1.21 82000
-
 2 * 82000, SDS-PAGE Mycobacterium tuberculosis
1.11.1.21 160000
-
 Superose 12HR gel filtration Mycobacterium tuberculosis
1.11.1.21 175000
-
 Sephadex G200 gel filtration Mycobacterium tuberculosis

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.21 ammonium sulfate precipitation, Mono Q column chromatography, DEAE-Sephacel gel filtration, and Superdex S200 gel filtration Mycobacterium tuberculosis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.11.1.21 0.00904
-
 specific peroxidase activity, using isoniazid as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C Mycobacterium tuberculosis
1.11.1.21 0.0098
-
 specific peroxidase activity, using isoniazid as substrate, purified mutant enzyme R463L, in 50 mM Na2HPO4, pH 5.5, 25°C Mycobacterium tuberculosis
1.11.1.21 0.208
-
 specific peroxidase activity, using NADH as substrate, purified mutant enzyme R463L, in 50 mM Na2HPO4, pH 5.5, 25°C Mycobacterium tuberculosis
1.11.1.21 0.212
-
 specific peroxidase activity, using NADH as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C Mycobacterium tuberculosis
1.11.1.21 0.264
-
 specific peroxidase activity, using NADPH as substrate, purified mutant enzyme R463L, in 50 mM Na2HPO4, pH 5.5, 25°C Mycobacterium tuberculosis
1.11.1.21 0.272
-
 specific peroxidase activity, using NADPH as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C Mycobacterium tuberculosis
1.11.1.21 2.12
-
 specific peroxidase activity, using pyrogallol as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C Mycobacterium tuberculosis
1.11.1.21 2.29
-
 specific peroxidase activity, using pyrogallol as substrate, purified mutant enzyme R463L, in 50 mM Na2HPO4, pH 5.5, 25°C Mycobacterium tuberculosis
1.11.1.21 22.8
-
 specific peroxidase activity, using o-dianisidine as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C Mycobacterium tuberculosis
1.11.1.21 25.9
-
 specific peroxidase activity, using o-dianisidine as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C Mycobacterium tuberculosis
1.11.1.21 99.4
-
 specific peroxidase activity, using 4-phenylendiamine as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C Mycobacterium tuberculosis
1.11.1.21 100.7
-
 specific peroxidase activity, using 4-phenylendiamine as substrate, purified mutant enzyme R463L, in 50 mM Na2HPO4, pH 5.5, 25°C Mycobacterium tuberculosis
1.11.1.21 226
-
 specific catalase activity, crude extract, in 50 mM Na2HPO4, pH 7.0, 25°C Mycobacterium tuberculosis
1.11.1.21 2420
-
 specific catalase activity, after 10.7fold purification, in 50 mM Na2HPO4, pH 7.0, 25°C Mycobacterium tuberculosis

Storage Stability

EC Number Storage Stability Organism
1.11.1.21 -80°C, 20 mM MOPS, pH 7.5, containing 40% (v/v) glycerol, 6 months, no loss of activity Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.21 4-phenylenediamine + H2O2 highest specific peroxidase activity Mycobacterium tuberculosis oxidized 4-phenylenediamine + H2O
-
 ?
1.11.1.21 H2O2
-
 Mycobacterium tuberculosis O2 + H2O
-
 ?
1.11.1.21 isoniazid + H2O2 i.e. isonicotinic acid hydrazide Mycobacterium tuberculosis oxidized isoniazid + H2O
-
 ?
1.11.1.21 additional information the wild type enzyme functions as a highly active catalase as well as a broad specificity peroxidase Mycobacterium tuberculosis ?
-
 ?
1.11.1.21 NADH + H2O2
-
 Mycobacterium tuberculosis ?
-
 ?
1.11.1.21 NADPH + H2O2
-
 Mycobacterium tuberculosis ?
-
 ?
1.11.1.21 o-dianisidine + H2O2
-
 Mycobacterium tuberculosis oxidized o-dianisidine + H2O
-
 ?
1.11.1.21 pyrogallol + H2O2
-
 Mycobacterium tuberculosis ? + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.11.1.21 homodimer 2 * 82000, SDS-PAGE Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
1.11.1.21 KatG
-
 Mycobacterium tuberculosis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.11.1.21 10100
-
 H2O2 wild type enzyme, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C Mycobacterium tuberculosis
1.11.1.21 11400
-
 H2O2 mutant enzyme R463L, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.21 7
-
 for catalase activity Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.21 heme the heme content of the enzyme is calculated to be 0.98 heme per dimer Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
1.11.1.21 physiological function oxidation of isoniazid by KatG in the presence of InhA leads to the inactivation of InhA Mycobacterium tuberculosis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.11.1.21 1850
-
 H2O2 mutant enzyme R463L, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C Mycobacterium tuberculosis
1.11.1.21 1950
-
 H2O2 wild type enzyme, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C Mycobacterium tuberculosis