1.11.1.21: catalase-peroxidase
This is an abbreviated version!
For detailed information about catalase-peroxidase, go to the full flat file.
Word Map on EC 1.11.1.21
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1.11.1.21
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1.11.1.7
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katgs
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mycobacterium
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tuberculosis
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isoniazid
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dismutase
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ascorbate
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heme
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horseradish
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peroxidases
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guaiacol
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ferric
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myeloperoxidase
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catalases
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1.6.4.2
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lignification
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monofunctional
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lactoperoxidase
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peroxidatic
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isonicotinic
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high-spin
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inh-resistant
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isoniazid-resistant
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o-dianisidine
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pseudomallei
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antituberculosis
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soret
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catalatic
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pro-drug
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antitubercular
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medicine
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mycolic
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isoperoxidase
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monodehydroascorbate
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1.8.5.1
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low-spin
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1.10.3.1
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pyrogallol
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3-amino-1,2,4-triazole
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coniferyl
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1.14.18.1
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4.3.1.5
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synthesis
- 1.11.1.21
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1.11.1.7
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katgs
- mycobacterium
- tuberculosis
- isoniazid
- dismutase
- ascorbate
- heme
- horseradish
- peroxidases
- guaiacol
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ferric
- myeloperoxidase
- catalases
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1.6.4.2
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lignification
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monofunctional
- lactoperoxidase
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peroxidatic
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isonicotinic
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high-spin
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inh-resistant
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isoniazid-resistant
- o-dianisidine
- pseudomallei
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antituberculosis
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soret
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catalatic
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pro-drug
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antitubercular
- medicine
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mycolic
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isoperoxidase
- monodehydroascorbate
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1.8.5.1
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low-spin
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1.10.3.1
- pyrogallol
- 3-amino-1,2,4-triazole
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coniferyl
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1.14.18.1
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4.3.1.5
- synthesis
Reaction
2 H2O2
=
Synonyms
AfKatG, BW16_04845, CAT, CAT-2, catalase -peroxidase KatG, catalase peroxidase, catalase-peroxidase, catalase/peroxidase, CP 2, CP01, CP02, CPX, CthediskatG, EC 1.11.1.7, FeSOD A, FvCP01, FvCP02, FVEG_10866, FVEG_12888, HCP, hemoprotein b-590, HPI, hydroperoxidase I, KatG, KatG1, KatG2, KatP, katX2, KpCP, PCP, Rv1908c
ECTree
1.11.1.21 catalase-peroxidaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 1.11.1.21 - catalase-peroxidase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
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acts as an inhibitor of peroxidase activity at lower pH (pH 3.8-4.5)
Ba2+
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partial inhibition of catalase activity
Sodium azide
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25 mM, 30% inhibition of peroxidase activity, 100% inhibition of catalyse activity
Co2+
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partial inhibition of catalase activity
cyanide
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bo th enzymic activities of catalase-peroxidase are equally inhibited by cyanide
H2O2
at a H2O2 concentration of 1 mM, a half-life of inactivation of approximately 60 s is observed, 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) protects the enzyme from inactivation by H2O2
H2O2
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enzyme inhibition is observed at hydrogen peroxide concentrations greater than 1.0 mM
H2O2
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both the catalatic and the peroxidatic activities are similarly inactivated by treatment with 1 mM H2O2
H2O2
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purified enzyme is sensitive to H2O2 concentrations higher than 10 mM
hydroxylamine
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0.05 mM, 80% inhibition of peroxidase activity, 88% inhibition of catalyse activity
hydroxylamine
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complete inhibition of catalase activity at 1 mM, 42% residual peroxidase activity at 1 mM
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
isoniazid
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i.e. isonicotinic acid hydrazide, strong competitive inhibition
KCN
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0.05 mM, 30% inhibition of peroxidase activity, 22% inhibition of catalyse activity
KCN
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catalase and peroxidase activities are effectively inhibited by KCN
KCN
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4% residual catalase activity at 1 mM, 4% residual peroxidase activity at 1 mM
NaCl
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the peroxidatic activity on diaminobenzidine shows a continuous decrease with increasing NaCl concentration
NaN3
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catalase and peroxidase activities are effectively inhibited by NaN3
NaN3
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8% residual catalase activity at 1 mM, 1% residual peroxidase activity at 1 mM
additional information
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the peroxidase activity of the enzyme against 3,3',5,5'-tetramethylbenzidine, 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), and o-dianisidine is unaffected by the inhibitors isonicotinic acid and niacinamide (all 20 mM), the enzyme is not inhibited by the specific monofunctional catalase inhibitor 3-amino-1,2,4,-triazole
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additional information
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no inhibition of the catalase activity of hCP is seen with 3-amino-l,2,4-triazole
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additional information
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catalatic activity of the purified H catalase-peroxidase is not inhibited by incubation for 2.5 h with 20 mM 3 amino-1,2,4-triazole
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additional information
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the enzyme is not inhibited by 3-amino-1,2,4-triazole
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additional information
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the enzyme is resistant to inhibition by 3-amino-1,2,4-triazole
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additional information
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not inhibited by 3-amino-1,2,4-triazole, nicotinamide, isonicotinamide or pyrazinamide
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additional information
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the enzyme is insensitive to 10 mM 3-amino-1,2,4-triazole
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additional information
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incubation for 60 min with 20 mM 3-amino-l,2,4-triazole has no effect on enzyme activity
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additional information
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p-chloromercuribenzoate at concentrations up to 100 mM does not inhibit the enzyme
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additional information
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the enzyme is insensitive to the eukaryotic catalase inhibitor 3-amino-1,2,4-triazole
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additional information
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the enzyme is not inhibited by 3-amino-1,2,4-triazole
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