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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Subunits
Subunits on EC 1.11.1.21 - catalase-peroxidase
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dimer
homodimer
homotetramer
additional information
homodimer
each subunit is composed of two structurally homologous domains with a topology similar to that of class I peroxidase
homodimer
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each subunit is composed of two structurally homologous domains with a topology similar to that of class I peroxidase
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homodimer
2 * 90000, about 95% of the protein exists in homodimeric form, gel filtration
homodimer
Pyricularia grisea ATCC MYA-4617
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2 * 90000, about 95% of the protein exists in homodimeric form, gel filtration
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homotetramer
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
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4 * 81889, calculated from amino acid sequence
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homotetramer
4 * 88000, about 95% of the protein exists in homodimeric form, gel filtration
homotetramer
Pyricularia grisea ATCC MYA-4617
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4 * 88000, about 95% of the protein exists in homodimeric form, gel filtration
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active site structure analysis of wild-type and mutant W111F enzymes
additional information
each subunit has two dominant alpha-helix domains, which means that the domains originated from gene duplication. The N domain has a heme, an active site and a substrate binding site. While the C domain does not have those, its presence is needed to support the overall enzyme activity. The catalytic activity of katG is mediated by some residues in the active site that resided around the heme group
additional information
-
each subunit has two dominant alpha-helix domains, which means that the domains originated from gene duplication. The N domain has a heme, an active site and a substrate binding site. While the C domain does not have those, its presence is needed to support the overall enzyme activity. The catalytic activity of katG is mediated by some residues in the active site that resided around the heme group
additional information
-
each subunit has two dominant alpha-helix domains, which means that the domains originated from gene duplication. The N domain has a heme, an active site and a substrate binding site. While the C domain does not have those, its presence is needed to support the overall enzyme activity. The catalytic activity of katG is mediated by some residues in the active site that resided around the heme group
-
additional information
-
each subunit has two dominant alpha-helix domains, which means that the domains originated from gene duplication. The N domain has a heme, an active site and a substrate binding site. While the C domain does not have those, its presence is needed to support the overall enzyme activity. The catalytic activity of katG is mediated by some residues in the active site that resided around the heme group
-
additional information
the N-terminal domain sequence is well conserved, it contains heme b and is enzymatically active. The heme-less inactive C-terminal domain sequence is less well conserved, but is required for dimerization of the enzyme and for the conformation of the active heme cavity of the N-terminal half
additional information
-
the N-terminal domain sequence is well conserved, it contains heme b and is enzymatically active. The heme-less inactive C-terminal domain sequence is less well conserved, but is required for dimerization of the enzyme and for the conformation of the active heme cavity of the N-terminal half
additional information
-
the N-terminal domain sequence is well conserved, it contains heme b and is enzymatically active. The heme-less inactive C-terminal domain sequence is less well conserved, but is required for dimerization of the enzyme and for the conformation of the active heme cavity of the N-terminal half
-
additional information
-
the N-terminal domain sequence is well conserved, it contains heme b and is enzymatically active. The heme-less inactive C-terminal domain sequence is less well conserved, but is required for dimerization of the enzyme and for the conformation of the active heme cavity of the N-terminal half
-
additional information
-
the N-terminal domain sequence is well conserved, it contains heme b and is enzymatically active. The heme-less inactive C-terminal domain sequence is less well conserved, but is required for dimerization of the enzyme and for the conformation of the active heme cavity of the N-terminal half
-
additional information
-
the N-terminal domain sequence is well conserved, it contains heme b and is enzymatically active. The heme-less inactive C-terminal domain sequence is less well conserved, but is required for dimerization of the enzyme and for the conformation of the active heme cavity of the N-terminal half
-
additional information
-
the N-terminal domain sequence is well conserved, it contains heme b and is enzymatically active. The heme-less inactive C-terminal domain sequence is less well conserved, but is required for dimerization of the enzyme and for the conformation of the active heme cavity of the N-terminal half
-