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Literature summary for 1.11.1.21 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
Search for more literature for 1.11.1.21

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

Inhibitors Comment Organism Structure
cyanide
-
 Mycobacterium tuberculosis

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Storage Stability

Storage Stability Organism
-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)

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

Subunits

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

Synonyms

Synonyms Comment Organism
KatG
-
 Mycobacterium tuberculosis

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

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

General Information

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

kcat/KM [mM/s]

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