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
-
tuberculosis
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isoniazid
-
dismutase
-
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
-
1.11.1.7
-
katgs
- mycobacterium
- tuberculosis
- isoniazid
- dismutase
- ascorbate
- heme
- horseradish
- peroxidases
- guaiacol
-
ferric
- myeloperoxidase
- catalases
-
1.6.4.2
-
lignification
-
monofunctional
- lactoperoxidase
-
peroxidatic
-
isonicotinic
-
high-spin
-
inh-resistant
-
isoniazid-resistant
- o-dianisidine
- pseudomallei
-
antituberculosis
-
soret
-
catalatic
-
pro-drug
-
antitubercular
- medicine
-
mycolic
-
isoperoxidase
- monodehydroascorbate
-
1.8.5.1
-
low-spin
-
1.10.3.1
- pyrogallol
- 3-amino-1,2,4-triazole
-
coniferyl
-
1.14.18.1
-
4.3.1.5
- synthesis
Reaction
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
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Metals Ions
Metals Ions on EC 1.11.1.21 - catalase-peroxidase
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CO
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complexed with the enzyme, structure determination, binding kinetics
Fe
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dioxygen binding to ferrous KatG and Y249F is reversible and monophasic. Ferrous wild-type KatG is rapidly converted by hydrogen peroxide in a two-phasic reaction via compound II to compound III, the latter being also efficiently transformed to ferric KatG. Determination of bimolecular rate constant and dissociation constant
Fe2+
K+
Mg2+
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2 mM Mg2+ have a stimulatory effect on catalase activity
Mn2+
Na+
NO
-
complexed with the enzyme, structure determination, binding kinetics
Fe2+
-
enzyme contains a heme modified with a special hydroperoxide group added to ring I
Fe2+
-
the bacterial manganese-dependent SOD A when bound to iron has peroxidase activity
Fe2+
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wild-type and S315T mutant enzyme, determination of Fe2+-binding/interaction structure
Fe2+
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iron is present at 1 atom per homodimer
Fe2+
-
dioxygen binding to ferrous KatG and Y249F is reversible and monophasic. Ferrous wild-type KatG is rapidly converted by hydrogen peroxide in a two-phasic reaction via compound II to compound III, the latter being also efficiently transformed to ferric KatG. Determination of bimolecular rate constant and dissociation constant
the CAT-2 homodimer crystallographic structure contains two K+ ions bound by Glu107 residues, binding structure, modeling, overview
K+
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2 mM K+ have a stimulatory effect on catalase activity
Mn2+
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2 mM Mn2+ have a stimulatory effect on catalase activity
Na+
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2 mM Na+ have a stimulatory effect on catalase activity