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
-
ferric
- myeloperoxidase
- catalases
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1.6.4.2
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lignification
-
monofunctional
- lactoperoxidase
-
peroxidatic
-
isonicotinic
-
high-spin
-
inh-resistant
-
isoniazid-resistant
- o-dianisidine
- pseudomallei
-
antituberculosis
-
soret
-
catalatic
-
pro-drug
-
antitubercular
- medicine
-
mycolic
-
isoperoxidase
- monodehydroascorbate
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1.8.5.1
-
low-spin
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1.10.3.1
- pyrogallol
- 3-amino-1,2,4-triazole
-
coniferyl
-
1.14.18.1
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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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Cofactor
Cofactor on EC 1.11.1.21 - catalase-peroxidase
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heme
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binding pocket distal side: triad residues P151, D152, and N153 are important for stability, they interact with the binding pocket proximal side residues W341, D402, and H290
heme
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wild-type and S315T mutant enzyme, determination of Fe2+-binding/interaction structure
heme
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it is proposed that binding of substrate H2O2 to Asp141 and Arg108 controls H2O2 access to the heme active site, thereby modulating the catalase reaction
heme
oxidoreductase with a predominant five-coordinated high-spin heme b, ferric MagKatG1 exhibits the typical bands of a heme b-containing peroxidase
heme
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catalase-peroxidase contains 2 heme molecules per tetramer
heme
ferric and ferrous KatG show predominant five-coordinate high-spin heme. However, the ferric form shows also small amounts of both six-coordinate high-spin and six-coordinate low-spin, and the ferrous form also exhibits a 6-coordinate low-spin heme
heme
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ferric KatP possesses a mixture of pentacoordinate and hexacoordinate high-spin heme iron
heme
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the enzyme contains 1 heme per homodimer
heme
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the enzyme lacks heme a and is a high-spin ferric protohemoprotein
heme
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the heme content of the enzyme is calculated to be 0.98 heme per dimer
heme
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there are 1-1.2 molecules of protoheme IX per tetrameric molecule
heme
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one pentacoordinated heme b per subunit, residue Tyr340 is the axial ligand
heme
determination and analysis of the structure of the heme environment of wild-type KatG and KatG bound to isoniazid, overview. The inactivated pro-drug added to the sample is not perturbing the heme site
heme
docking study with wild-type and mutant enzymes, molecular dynamics, overview
heme
The amino acids residues that are essential for both activities are His91, Asn121 and Arg87 of the distal side of the heme cavity and His279, Asp389 and Trp330 of the proximal side, together with the M-Y-W adduct, Arg426 and Asp120, which are only required for the catalase reaction