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
-
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
- 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
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 (Substrates Products
Substrates Products on EC 1.11.1.21 - catalase-peroxidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + tert-butyl hydroperoxide
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + ?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
oxidized 2,6-dimethoxyphenol + H2O
-
-
-
-
?
2-dianisidine + tert-butyl hydroperoxide
?
-
peroxidase activity
-
-
?
3,3',5,5'-tetramethylbenzidine + H2O2
oxidized 3,3',5,5'-tetramethylbenzidine + H2O
-
-
-
-
?
isoniazid + NADH
isonicotinic acyl-NADH
-
isoniazid activation
the product is a strong inhibitor of the NADH-dependent enoyl-[acyl carrier protein] reductase InhA and the beta-ketoacyl [acyl carrier protein] synthase
-
?
o-dianisidine + tert-butyl hydroperoxide
o-dianisidine quinonediimine + ?
-
-
-
-
?
o-dianisidine + tert-butyl hydroperoxide
oxidized o-dianisidine + ?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
KatP has stronger catalase than peroxidase activity
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + H2O
-
-
-
-
?
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
-
-
?
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
Pyricularia grisea ATCC MYA-4617
-
-
-
?
3,3'-diaminobenzidine + H2O2
oxidized 3,3'-diaminobenzidine + H2O
-
-
-
?
3,3'-diaminobenzidine + H2O2
oxidized 3,3'-diaminobenzidine + H2O
-
-
-
-
?
3,3'-diaminobenzidine + H2O2
oxidized 3,3'-diaminobenzidine + H2O
-
-
-
-
?
3,3'-diaminobenzidine + H2O2
oxidized 3,3'-diaminobenzidine + H2O
-
-
-
-
?
3,3'-dimethoxybenzidine + H2O2
oxidized 3,3'-dimethoxybenzidine + H2O
-
-
-
?
3,3'-dimethoxybenzidine + H2O2
oxidized 3,3'-dimethoxybenzidine + H2O
-
-
-
-
?
3-methoxyphenol + H2O2
? + H2O
about 90% conversion
products are oligomers of different weight, i.g. of 27 monomer units and of 23 monomer units
-
?
3-methoxyphenol + H2O2
? + H2O
about 90% conversion
products are oligomers of different weight, i.g. of 27 monomer units and of 23 monomer units
-
?
4-aminoantipyrine + H2O2
oxidized 4-aminoantipyrine + H2O
-
-
-
-
?
4-aminoantipyrine + H2O2
oxidized 4-aminoantipyrine + H2O
-
-
-
-
?
4-phenylenediamine + H2O2
oxidized 4-phenylenediamine + H2O
-
-
-
?
4-phenylenediamine + H2O2
oxidized 4-phenylenediamine + H2O
-
highest specific peroxidase activity
-
-
?
catechol + H2O2
? + H2O
about 90% conversion
products are oligomers of 7 monomer units
-
?
catechol + H2O2
? + H2O
about 90% conversion
products are oligomers of 7 monomer units
-
?
donor + H2O2
oxidized donor + 2 H2O
catalase activity
-
-
?
donor + H2O2
oxidized donor + 2 H2O
catalase activity
-
-
?
H2O2
O2 + H2O
detoxification enzyme, protection against peroxides
-
-
?
H2O2
O2 + H2O
-
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
-
-
?
H2O2
O2 + H2O
-
-
-
-
?
isoniazid + H2O2
?
-
activation of antituberculosis drug isonazid, catalytic mechanism
-
-
?
isoniazid + H2O2
?
enzyme binding structure analysis, modeling, overview
-
-
?
isoniazid + H2O2
?
i.e. isonicotinylhydrazide (INH), binding of isoniazid to the active site residues of the enzyme, molecular docking and density functional theory analysis, and modeling using the the molecular mechanics model of the INH-KatG system, detailed overview. Seven amino acid residues directly interact with INH: Arg104, Asp137, His108, Ile228, Trp107, Tyr229, and Val230
-
-
?
isoniazid + H2O2
?
enzyme binding structure analysis, modeling, overview
-
-
?
isoniazid + H2O2
?
pro-drug activation
-
-
?
isoniazid + H2O2
?
i.e. isonicotinylhydrazide (INH), binding of isoniazid to the active site residues of the enzyme, molecular docking and density functional theory analysis, and modeling using the the molecular mechanics model of the INH-KatG system, detailed overview. Seven amino acid residues directly interact with INH: Arg104, Asp137, His108, Ile228, Trp107, Tyr229, and Val230
-
-
?
isoniazid + H2O2
?
enzyme binding structure analysis, modeling, overview
-
-
?
isoniazid + H2O2
?
i.e. isonicotinylhydrazide (INH), binding of isoniazid to the active site residues of the enzyme, molecular docking and density functional theory analysis, and modeling using the the molecular mechanics model of the INH-KatG system, detailed overview. Seven amino acid residues directly interact with INH: Arg104, Asp137, His108, Ile228, Trp107, Tyr229, and Val230
-
-
?
isoniazid + H2O2
oxidized isoniazid + H2O
-
i.e. isonicotinic acid hydrazide
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + 2 H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + 2 H2O
catalase activity
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + 2 H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + 2 H2O
catalase activity
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + 2 H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + 2 H2O
catalase activity
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + 2 H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + 2 H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + 2 H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + 2 H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + 2 H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + tert-butyl hydroperoxide + H2O2
o-dianisidin quinone diimine + ?
-
-
-
?
o-dianisidine + tert-butyl hydroperoxide + H2O2
o-dianisidin quinone diimine + ?
-
-
-
?
peroxyacetic acid
?
-
-
in the absence of peroxidatic one-electron donors, the ferryl intermediates generated with a low excess of peroxyacetic acid slowly decay to the ferric resting state after several minutes. The Fe(IV)=O Trp330 radical cation, Fe(IV)=O Trp139 radical, and Fe(IV)=O Trp153 radical intermediates of the peroxidase-like cycle, formed with a low excess of peroxyacetic acid at low temperature, are also generated with a high excess of peroxyacetic acid at room temperature. Under high excess conditions, there is a rapid conversion to a persistent Fe(IV)=O intermediate. Specific tryptophan residues including W330, W139, and W153, methionine residues including Met264 of the M-Y-W adduct, and cysteine residues are either modified with one, two, or three oxygen atoms or cannot be identified in the spectrum because of other undetermined modifications. These oxidized residues are the source of electrons used to reduce the excess of peroxyacetic acid to acetic acid and return the enzyme to the ferric state
-
?
peroxyacetic acid + 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
?
-
-
-
-
?
peroxyacetic acid + 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
?
-
-
-
?
peroxyacetic acid + 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
?
-
-
-
?
phenol + H2O2
? + H2O
about 90% conversion
products are oligomers of different weight, i.g. of 27 monomer units and of 23 monomer units
-
?
phenol + H2O2
? + H2O
about 90% conversion
products are oligomers of different weight, i.g. of 27 monomer units and of 23 monomer units
-
?
reduced 2,3',6'-trichloroindophenol + H2O2
oxidized 2,3',6'-trichloroindophenol + H2O
-
-
-
-
?
reduced 2,3',6'-trichloroindophenol + H2O2
oxidized 2,3',6'-trichloroindophenol + H2O
-
-
-
-
?
tert-butyl hydroperoxide + H2O2
oxidized tert-butyl hydroperoxide + H2O
-
-
-
-
?
tert-butyl hydroperoxide + H2O2
oxidized tert-butyl hydroperoxide + H2O
-
-
-
-
?
tert-butyl hydroperoxide + H2O2
oxidized tert-butyl hydroperoxide + H2O
-
-
-
-
?
additional information
?
-
no activity is detected with NADH or NADPH
-
-
?
additional information
?
-
-
no activity is detected with NADH or NADPH
-
-
?
additional information
?
-
the catalase activity strongly exceeds the peroxidase activity
-
-
?
additional information
?
-
-
the catalase activity strongly exceeds the peroxidase activity
-
-
?
additional information
?
-
-
for phenolic substrates, the phenolic oxygen is not directly coordinated to the heme iron. No substrates: pyrogallol, catechol, or hydroquinone
-
-
?
additional information
?
-
-
guaicol (methoxyphenol) and 2-chloronaphthol are not peroxidized by the enzyme
-
-
?
additional information
?
-
-
guiacol and ascorbate are no substrates
-
-
?
additional information
?
-
-
guiacol and ascorbate are no substrates
-
-
?
additional information
?
-
-
the wild type enzyme functions as a highly active catalase as well as a broad specificity peroxidase
-
-
?
additional information
?
-
-
interaction between the side chain of residue Arg418 and Tyr229 in the adduct radical formed from covalently linked side chains of conserved amino acids Met255, Tyr229, and Trp107 favors reaction of the radical with the adjacent dioxyheme intermediate present throughout turnover. Release of molecular oxygen and regeneration of resting enzyme are thereby catalyzed in the last step of a proposed catalase reaction
-
-
?
additional information
?
-
-
presence of a low- and high-KM component for catalase activity at pH 5.0. Electron donors increase the apparent kcat for the low-KM component. During stimulated catalase activity, less than 0.008 equivalents of oxidized donor accumulate for every H2O2 consumed. A Fe(III)-O2 radical anion-like intermediate dominates during donor-stimulated catalatic turnover, and this intermediate converts directly to the ferric state upon depletion of H2O2
-
-
?
additional information
?
-
-
the enzyme is very slowly reduced by dithionite
-
-
?
additional information
?
-
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
the enzyme is very slowly reduced by dithionite
-
-
?
additional information
?
-
CAT-2 requires the Met-Tyr-Trp adduct for catalase activity. CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. The second-order rate constant is one order of magnitude higher for CAT-2_intein compared to CAT-2_His6 besides the CAT-2_His6 enzyme does not saturate with o-dianisidine. Because the N-terminal end is close to the entrance channel, its increased size due to the histidine tag can possibly interfere with the channel
-
-
-
additional information
?
-
-
CAT-2 requires the Met-Tyr-Trp adduct for catalase activity. CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. The second-order rate constant is one order of magnitude higher for CAT-2_intein compared to CAT-2_His6 besides the CAT-2_His6 enzyme does not saturate with o-dianisidine. Because the N-terminal end is close to the entrance channel, its increased size due to the histidine tag can possibly interfere with the channel
-
-
-
additional information
?
-
CAT-2 requires the Met-Tyr-Trp adduct for catalase activity. CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. The second-order rate constant is one order of magnitude higher for CAT-2_intein compared to CAT-2_His6 besides the CAT-2_His6 enzyme does not saturate with o-dianisidine. Because the N-terminal end is close to the entrance channel, its increased size due to the histidine tag can possibly interfere with the channel
-
-
-
additional information
?
-
CAT-2 requires the Met-Tyr-Trp adduct for catalase activity. CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. The second-order rate constant is one order of magnitude higher for CAT-2_intein compared to CAT-2_His6 besides the CAT-2_His6 enzyme does not saturate with o-dianisidine. Because the N-terminal end is close to the entrance channel, its increased size due to the histidine tag can possibly interfere with the channel
-
-
-
additional information
?
-
CAT-2 requires the Met-Tyr-Trp adduct for catalase activity. CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. The second-order rate constant is one order of magnitude higher for CAT-2_intein compared to CAT-2_His6 besides the CAT-2_His6 enzyme does not saturate with o-dianisidine. Because the N-terminal end is close to the entrance channel, its increased size due to the histidine tag can possibly interfere with the channel
-
-
-
additional information
?
-
CAT-2 requires the Met-Tyr-Trp adduct for catalase activity. CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. The second-order rate constant is one order of magnitude higher for CAT-2_intein compared to CAT-2_His6 besides the CAT-2_His6 enzyme does not saturate with o-dianisidine. Because the N-terminal end is close to the entrance channel, its increased size due to the histidine tag can possibly interfere with the channel
-
-
-
additional information
?
-
CAT-2 requires the Met-Tyr-Trp adduct for catalase activity. CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. The second-order rate constant is one order of magnitude higher for CAT-2_intein compared to CAT-2_His6 besides the CAT-2_His6 enzyme does not saturate with o-dianisidine. Because the N-terminal end is close to the entrance channel, its increased size due to the histidine tag can possibly interfere with the channel
-
-
-
additional information
?
-
-
NADPH, vanilly1 alcohol and veratryl alcohol do not serve as electron donors
-
-
?
additional information
?
-
-
no reaction is detected with guaiacol or with ascorbate
-
-
?
additional information
?
-
-
the enzyme does not accept electrons from ascorbate, glutathione, and NADH
-
-
?
additional information
?
-
-
bifunctional enzyme providing catalase and peroxidase activities, intermediate structure
-
-
?
additional information
?
-
-
the recombinant protein contains high catalase activity and an appreciable peroxidase activity with o-dianisidine, guaiacol and pyrogallol, but not with NAD(P)H, ferrocytochrome c, ascorbate or glutathione as electron donors
-
-
?
additional information
?
-
-
bifunctional enzyme showing both catalase and peroxidase activities
-
-
?
