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Enzyme Nomenclature
Information on EC 1.11.1.21 - catalase-peroxidase
for references in articles please use BRENDA:EC1.11.1.21
Word Map on EC 1.11.1.21
- 1.11.1.21
-
katgs
- mycobacterium
- tuberculosis
- isoniazid
- heme
-
ferric
- catalases
-
isoniazid-resistant
- peroxidases
-
antituberculosis
-
catalatic
-
monofunctional
-
inh-resistant
-
peroxidatic
-
isonicotinic
- pseudomallei
-
high-spin
- o-dianisidine
-
soret
- 3-amino-1,2,4-triazole
-
pro-drug
-
antitubercular
- pyrogallol
-
mycolic
-
peroxyacetic
- medicine
-
oxyferrous
- reticuli
- synthesis
-
peroxidase-like
- marismortui
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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.11.1.21
-
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RECOMMENDED NAME
GeneOntology No.
catalase-peroxidase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
donor + H2O2 = oxidized donor + 2 H2O
-
-
-
-
2 H2O2 = O2 + 2 H2O
-
-
-
-
2 H2O2 = O2 + 2 H2O
distal site Asp152 is essential for the catalase activity of catalase-peroxidase, mechanism for hydrogen peroxide oxidation in volving residues Trp122 and Asp152
-
2 H2O2 = O2 + 2 H2O
the catalytically relevant active site residues Trp111, Tyr238, and Met264 are linked by a covalent structure
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
donor:hydrogen-peroxide oxidoreductase
Differs from EC 1.11.1.7, peroxidase in having a relatively high catalase (EC 1.11.1.6) activity with H2O2 as donor, releasing O2; both activities use the same heme active site. In Mycobacterium tuberculosis it is responsible for activation of the commonly used antitubercular drug, isoniazid.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene katG, KatG is a bifunctional enzyme showing both catalase and peroxidase activities
-
-
gene katG, bifunctional enzyme KatG with catalase and peroxidase activities
SwissProt
-
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
Mycobacterium tuberculosis isolates with defects in the kutG gene encoding a catalase-peroxidase enzyme exhibit resistance to isoniazid
malfunction
-
catalase-peroxidase activity is decreased in a Caulobacter crescentus rho::TN5 mutant
malfunction
the null katG mutation has little effect on the growth rate in the absence of added H2O2. However, growth inhibition is evident with low levels of exogenous H2O2
malfunction
although the rate of H2O2 decomposition is about 30times lower in the katG deletion mutant than in the wild type, the strain has a normal phenotype and its doubling time as well as its resistance to H2O2 and methyl viologen are indistinguishable from those of the wild type
malfunction
-
a knockout mutation in katG that causes loss of catalase-peroxidase activity correlates with increased susceptibility to H2O2 and a superoxide generator and is avirulent in a plant model system. The katG mutant shows a 10fold increase in resistance to tert-butyl hydroperoxide compared with the wild type strain
physiological function
-
oxidation of isoniazid by KatG in the presence of InhA leads to the inactivation of InhA
physiological function
-
periplasmic catalase-peroxidases contributes to bacterial virulence
physiological function
-
hemoprotein b-590 plays a role in removal of peroxides generated during respiration
physiological function
the catalatic and/or peroxidatic activity of KatG is important in reducing H2O2 concentration to a steady-state level compatible with sustained exponential growth. Catalase-peroxidase clearly plays a critical role in stationary-phase survival
physiological function
catalase-peroxidase has a protective role against environmental H2O2
physiological function
-
KatG is required for virulence of Xanthomonas campestris pv. campestris in a Chinese radish host plant by providing protection against low levels of H2O2
physiological function
-
catalase-peroxidase is involved in isoniazid activation
physiological function
-
catalase-peroxidase confers isoniazid (isonicotinic acid hydrazide) sensitivity in Mycobacterium tuberculosis
physiological function
expression in Bacillus subtilis improves its resistance to oxidative stress
physiological function
-
expression in Bacillus subtilis improves its resistance to oxidative stress
-
physiological function
-
hemoprotein b-590 plays a role in removal of peroxides generated during respiration
-
physiological function
Mycobacterium smegmatis mc(2)155 / ATCC 700084
-
catalase-peroxidase is involved in isoniazid activation
-
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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
-
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'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
-
-
?
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
-
-
?
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
-
?
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
oxidized isoniazid + H2O
-
i.e. isonicotinic acid hydrazide
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
Mycobacterium smegmatis mc(2)155 / ATCC 700084
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
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
?
-
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 enzyme is very slowly reduced by dithionite
-
-
-
additional information
?
-
Mycobacterium smegmatis mc(2)155 / ATCC 700084
-
the enzyme is very slowly reduced by dithionite
-
-
-
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
?
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
isoniazid + H2O2
?
-
activation of antituberculosis drug isonazid, catalytic mechanism
-
-
?
H2O2
O2 + H2O
Q939D2
detoxification enzyme, protection against peroxides
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
the heme content of the enzyme is calculated to be 0.98 heme per dimer
heme
-
there are 1-1.2 molecules of protoheme IX per tetrameric molecule
heme
-
ferric KatP possesses a mixture of pentacoordinate and hexacoordinate high-spin heme iron
heme
-
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
-
wild-type and S315T mutant enzyme, determination of Fe2+-binding/interaction structure
heme
-
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
-
the enzyme contains 1 heme per homodimer
heme
-
the enzyme lacks heme a and is a high-spin ferric protohemoprotein
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
-
-
heme
one pentacoordinated heme b per subunit, residue Tyr340 is the axial ligand
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CO
-
complexed with the enzyme, structure determination, binding kinetics
Fe
-
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+
-
2 mM K+ have a stimulatory effect on catalase activity
Mg2+
-
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+
-
wild-type and S315T mutant enzyme, determination of Fe2+-binding/interaction structure
Fe2+
-
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
Mn2+
-
2 mM Mn2+ have a stimulatory effect on catalase activity
Na+
-
2 mM Na+ have a stimulatory effect on catalase activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
acts as an inhibitor of peroxidase activity at lower pH (pH 3.8-4.5)
Ba2+
-
partial inhibition of catalase activity
Sodium azide
-
25 mM, 30% inhibition of peroxidase activity, 100% inhibition of catalyse activity
Co2+
-
partial inhibition of catalase activity
cyanide
-
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
-
enzyme inhibition is observed at hydrogen peroxide concentrations greater than 1.0 mM
H2O2
-
both the catalatic and the peroxidatic activities are similarly inactivated by treatment with 1 mM H2O2
H2O2
-
purified enzyme is sensitive to H2O2 concentrations higher than 10 mM
hydroxylamine
; inhibits the peroxidase activity of the enzyme
hydroxylamine
-
0.05 mM, 80% inhibition of peroxidase activity, 88% inhibition of catalyse activity
hydroxylamine
-
complete inhibition of catalase activity at 1 mM, 42% residual peroxidase activity at 1 mM
isoniazid
-
i.e. isonicotinic acid hydrazide, strong competitive inhibition
KCN
-
0.05 mM, 30% inhibition of peroxidase activity, 22% inhibition of catalyse activity
KCN
-
catalase and peroxidase activities are effectively inhibited by KCN
KCN
-
4% residual catalase activity at 1 mM, 4% residual peroxidase activity at 1 mM
NaCl
-
the peroxidatic activity on diaminobenzidine shows a continuous decrease with increasing NaCl concentration
NaN3
-
catalase and peroxidase activities are effectively inhibited by NaN3
NaN3
-
8% residual catalase activity at 1 mM, 1% residual peroxidase activity at 1 mM
additional information
-
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
-
additional information
-
no inhibition of the catalase activity of hCP is seen with 3-amino-l,2,4-triazole
-
additional information
-
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
-
additional information
-
the enzyme is not inhibited by 3-amino-1,2,4-triazole
-
additional information
-
not inhibited by 3-amino-1,2,4-triazole, nicotinamide, isonicotinamide or pyrazinamide
-
additional information
-
the enzyme is resistant to inhibition by 3-amino-1,2,4-triazole
-
additional information
-
the enzyme is insensitive to 10 mM 3-amino-1,2,4-triazole
-
additional information
-
incubation for 60 min with 20 mM 3-amino-l,2,4-triazole has no effect on enzyme activity
-
additional information
-
p-chloromercuribenzoate at concentrations up to 100 mM does not inhibit the enzyme
-
additional information
-
the enzyme is insensitive to the eukaryotic catalase inhibitor 3-amino-1,2,4-triazole
-
additional information
-
the enzyme is not inhibited by 3-amino-1,2,4-triazole
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-Amino-1,2,4-triazole
-
156% relative catalase activity at 10 mM, 121% relative peroxidase activity at 10 mM
ammonium sulfate
-
additions of ammonium sulfate even at weak concentrations (10 to 70 mM) stimulate catalatic activity measured in the presence of 1.5 M NaC1 by about 30%
NaCl
-
peroxidase activity is maximal at NaCl concentrations above 1 M, although catalase activity requires 2 M NaCl for optimal function
NaCl
-
76% stimulation of catalase by addition of 10 mM NaCl
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.23
NADH
-
peroxidatic activity, in 50 mM phosphate buffer, pH 7.0, at 25°C
0.17
NADPH
-
peroxidatic activity, in 50 mM phosphate buffer, pH 7.0, at 25°C
additional information
additional information
-
steady- and transient-state kinetics
-
0.0055
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme R108A/W111F/D141A, peroxidase activity, at pH 4.5 and 25°C
0.007
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.3 and 25°C
0.0092
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme D141N, peroxidase activity, at pH 4.5 and 25°C
0.012
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme KatGDELTAFG, in 50 mM acetate buffer pH 5.0, at 23°C
0.016
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.5 and 25°C
0.016
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 5.0 and 25°C
0.023
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme E291K, at pH 5.0 and 23°C
0.024
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.3 and 25°C
0.024
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme R108A/W111F, peroxidase activity, at pH 4.5 and 25°C
0.028
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme E291K/E292A, at pH 5.0 and 23°C
0.03
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme D141A, peroxidase activity, at pH 4.5 and 25°C
0.031
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.0 and 25°C
0.037
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme I290A/Q293A, at pH 5.0 and 23°C
0.043
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant Y22F, pH 5.0, 23°C
0.048
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme R102L, at pH 6.0 and 25°C
0.05
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Q293E, at pH 5.0 and 23°C
0.055
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, wild type enzyme, at pH 6.0 and 25°C
0.061
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
0.067
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.8 and 25°C
0.07
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme D141E, peroxidase activity, at pH 4.5 and 25°C; mutant enzyme R108A/D141A, peroxidase activity, at pH 4.5 and 25°C
0.071
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme E291A, at pH 5.0 and 23°C
0.08
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme H106C, at pH 6.0 and 25°C
0.08
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Q293A, at pH 5.0 and 23°C
0.081
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme I290V/Q293V, at pH 5.0 and 23°C
0.086
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTA200-214, pH 5.0, 23°C
0.087
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
0.087
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild type enzyme, at pH 5.0 and 23°C
0.09
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Q293V, at pH 5.0 and 23°C
0.1
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme R102C, at pH 6.0 and 25°C
0.11
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidatic activity, wild type enzyme, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
0.11
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidatic activity, in 50 mM phosphate buffer, pH 7.0, at 25°C
0.13
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme I290V, at pH 5.0 and 23°C
0.14
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild type enzyme, peroxidase activity, at pH 4.5 and 25°C
0.16
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme I290A, at pH 5.0 and 23°C
0.23
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, wild type enzyme, in 50 mM acetate buffer pH 5.0, at 23°C
0.24
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme W105L, at pH 6.0 and 25°C
0.3
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.5 and 25°C
0.31
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild-type, pH 5.0, 23°C
0.32
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidatic activity, mutant enzyme W107F/W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
0.33
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme H106Y, at pH 6.0 and 25°C
0.36
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidatic activity, mutant enzyme W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
0.4
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme R102K, at pH 6.0 and 25°C
0.41
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme R108A, peroxidase activity, at pH 4.5 and 25°C
0.47
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidatic activity, mutant enzyme W107F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
0.48
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme W105F, at pH 6.0 and 25°C
0.55
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme R108K, peroxidase activity, at pH 4.5 and 25°C
0.83
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 23°C
0.96
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidatic activity, using tert-butyl hydroperoxide as cosubstrate, in 10 mM K2HPO4/KH2PO4 (pH 7.5), at 25°C
1.06
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTAL193-N228, pH 5.0, 23°C
1.2
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant E695A/Y697A, pH 7.0, 23°C
1.2
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTA209-228, pH 5.0, 23°C
1.6
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidatic activity, mutant enzyme H108L, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
1.9
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant Y697A, pH 7.0, 23°C
2.2
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant L690A/R691A/E695A/Y697A, pH 7.0, 23°C
2.4
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild-type, N- and C-terminal domain separately expressed, pH 7.0, 23°C
2.7
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant L690A/R691A, pH 7.0, 23°C; mutant R691A, pH 7.0, 23°C
2.9
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant E695A, pH 7.0, 23°C
3
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
in 50 mM acetate buffer, pH 5.0, at 23°C
3.3
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant L690A/R691A, N- and C-terminal domain separately expressed, pH 7.0, 23°C
3.6
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant E695A, N- and C-terminal domain separately expressed, pH 7.0, 23°C
4
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant R691A, N- and C-terminal domain separately expressed, pH 7.0, 23°C
4.5
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild-type, pH 7.0, 23°C
6
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant Y697A, N- and C-terminal domain separately expressed, pH 7.0, 23°C
0.06
H2O2
-
mutant enzyme E291K, at pH 5.0 and 23°C; mutant enzyme E291K/E292A, at pH 5.0 and 23°C
0.07
H2O2
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
0.07
H2O2
-
mutant enzyme S315T, catalase activity, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C; wild type enzyme, catalase activity, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
0.09
H2O2
-
mutant enzyme D141N, peroxidase activity, at pH 4.5 and 25°C
0.12
H2O2
-
mutant enzyme D141E, peroxidase activity, at pH 4.5 and 25°C
0.14
H2O2
-
peroxidase activity, in 50 mM potassium phosphate containing 2 M NaCl, pH 7.5, at 25°C
0.18
H2O2
-
wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
0.19
H2O2
-
mutant enzyme D141A, peroxidase activity, at pH 4.5 and 25°C
0.27
H2O2
-
mutant enzyme R108A/D141A, peroxidase activity, at pH 4.5 and 25°C
0.31
H2O2
-
wild type enzyme, peroxidase activity, at pH 4.5 and 25°C
0.5
H2O2
-
mutant enzyme R108A, peroxidase activity, at pH 4.5 and 25°C
0.56
H2O2
-
mutant enzyme R108A/W111F, peroxidase activity, at pH 4.5 and 25°C
0.6
H2O2
-
catalatic activity, in 50 mM phosphate buffer, pH 7.0, at 25°C
0.83
H2O2
-
peroxidase activity, wild type enzyme, in 50 mM acetate buffer pH 5.0, at 23°C
0.85
H2O2
peroxidase activity, 50 mM potassium phosphate/sodium citrate buffer, pH 4.5, at 80°C
0.92
H2O2
-
mutant enzyme R108A/W111F/D141A, peroxidase activity, at pH 4.5 and 25°C
0.98
H2O2
-
mutant enzyme R108K, peroxidase activity, at pH 4.5 and 25°C
1.47
H2O2
-
peroxidase activity, in 50 mM potassium phosphate buffer (pH 7.0), at 30°C
1.5
H2O2
-
peroxidase activity, mutant enzyme KatGDELTAFG, in 50 mM acetate buffer pH 5.0, at 23°C
1.7
H2O2
-
catalase activity, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C
2.3
H2O2
-
catalase activity, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C
2.8
H2O2
wild type enzyme, in 25 mM HEPES-NaOH buffer (pH 7.0) at 25°C
3.03
H2O2
-
mutant C55A, pH not specified in the publication, temperature not specified in the publication
3.21
H2O2
-
mutant C55A/C74A, pH not specified in the publication, temperature not specified in the publication
3.5
H2O2
-
wild type enzyme, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C
3.52
H2O2
-
mutant C26A/C74A, pH not specified in the publication, temperature not specified in the publication
3.66
H2O2
-
mutant C74A, pH not specified in the publication, temperature not specified in the publication
3.7
H2O2
-
catalase activity, in 50 mM potassium phosphate containing 2 M NaCl, pH 6.5, at 25°C
3.84
H2O2
-
wild-type, pH not specified in the publication, temperature not specified in the publication
4
H2O2
-
catalase activity, wild type enzyme, 100 mM phosphate buffer pH 7.0, at 23°C
4.1
H2O2
-
catalase activity, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C
4.3
H2O2
-
catalase activity, in 67 mM phosphate buffer (pH 7.0), at 25°C
4.5
H2O2
-
catalase activity, mutant enzyme KatGDELTAFG, 100 mM phosphate buffer pH 7.0, at 23°C
5.18
H2O2
-
wild type enzyme, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C
5.2
H2O2
-
mutant enzyme Y111A, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C
6.16
H2O2
-
mutant enzyme R463L, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C
6.3
H2O2
-
catalase activity, in 50 mM potassium phosphate buffer (pH 7.0), at 30°C
6.7
H2O2
-
catalase activity, pH and temperature not specified in the publication
13
H2O2
-
mutant enzyme R108A, catalase activity, at pH 7.0 and 37°C
24
H2O2
-
catalase activity, in 20 mM Tris-HCl buffer (pH 9.0), at 30°C
30
H2O2
-
catalatic activity, in 10 mM K2HPO4/KH2PO4 (pH 7.5), at 25°C
31.5
H2O2
-
catalatic activity, mutant enzyme W107F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
32
H2O2
-
mutant enzyme R108A/D141A, catalase activity, at pH 7.0 and 37°C
32.1
H2O2
-
catalatic activity, mutant enzyme W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
33
H2O2
-
catalatic activity, mutant enzyme W107F/W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
35
H2O2
-
mutant enzyme R108A/W111F/D141A, catalase activity, at pH 7.0 and 37°C
36
H2O2
-
mutant enzyme R108A/W111F, catalase activity, at pH 7.0 and 37°C
42.6
H2O2
-
catalatic activity, wild type enzyme, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
54.9
H2O2
-
catalatic activity, mutant enzyme H108L, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
60
H2O2
-
mutant enzyme D141A, catalase activity, at pH 7.0 and 37°C
75
H2O2
-
mutant enzyme D141E, catalase activity, at pH 7.0 and 37°C
95
H2O2
-
mutant enzyme D141N, catalase activity, at pH 7.0 and 37°C
180
H2O2
-
mutant enzyme R108K, catalase activity, at pH 7.0 and 37°C
0.08
isoniazid
-
mutant enzyme S315T, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
0.43
isoniazid
-
wild type enzyme, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
0.0478
o-Dianisidine
-
peroxidase activity, in 50 mM potassium phosphate buffer (pH 7.0), at 30°C
0.14
o-Dianisidine
-
peroxidatic activity, with hydrogen peroxide as cosubstrate, in 50 mM phosphate buffer, pH 7.0, at 25°C; peroxidatic activity, with tert-butyl hydroperoxide as cosubstrate, in 50 mM phosphate buffer, pH 7.0, at 25°C
0.31
pyrogallol
-
peroxidatic activity, in 50 mM phosphate buffer, pH 7.0, at 25°C
5.7
tert-butyl hydroperoxide
-
peroxidatic activity, mutant enzyme W107F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
12.7
tert-butyl hydroperoxide
-
peroxidatic activity, mutant enzyme H108L, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
15.5
tert-butyl hydroperoxide
-
peroxidatic activity, mutant enzyme W107F/W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
91.2
tert-butyl hydroperoxide
-
peroxidatic activity, mutant enzyme W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
97.9
tert-butyl hydroperoxide
-
peroxidatic activity, wild type enzyme, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.34
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidatic activity, mutant enzyme H108L, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
0.37
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidatic activity, mutant enzyme W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
0.72
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidatic activity, wild type enzyme, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
1.1
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme H106Y, at pH 6.0 and 25°C
1.6
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme H106C, at pH 6.0 and 25°C
2.4
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidatic activity, mutant enzyme W107F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
4.5
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidatic activity, using tert-butyl hydroperoxide as cosubstrate, in 10 mM K2HPO4/KH2PO4 (pH 7.5), at 25°C
5.4
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidatic activity, mutant enzyme W107F/W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
7.7
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 5.0 and 25°C
7.9
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.5 and 25°C
11
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.0 and 25°C
13
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.3 and 25°C
13.3
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme I290A/Q293A, at pH 5.0 and 23°C
15.2
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Q293V, at pH 5.0 and 23°C
17
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.5 and 25°C
19
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.8 and 25°C
20
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Q293E, at pH 5.0 and 23°C
22.5
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme I290V/Q293V, at pH 5.0 and 23°C
25
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.3 and 25°C
26
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme KatGDELTAFG, in 50 mM acetate buffer pH 5.0, at 23°C
28.5
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme I290V, at pH 5.0 and 23°C
29.3
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Q293A, at pH 5.0 and 23°C
29.6
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme E291K, at pH 5.0 and 23°C
32.5
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme I290A, at pH 5.0 and 23°C
33.3
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
38
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme E291K/E292A, at pH 5.0 and 23°C
39.7
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme E291A, at pH 5.0 and 23°C
50.2
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTA200-214, pH 5.0, 23°C
52
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, wild type enzyme, in 50 mM acetate buffer pH 5.0, at 23°C
55
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild type enzyme, at pH 5.0 and 23°C
55.2
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
77
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
in 50 mM acetate buffer, pH 5.0, at 23°C
83
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild-type, pH 5.0, 23°C
97
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant Y22F, pH 5.0, 23°C
160
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant L690A/R691A/E695A/Y697A, pH 7.0, 23°C
660
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme R102L, at pH 6.0 and 25°C
710
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme R102C, at pH 6.0 and 25°C
740
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTAL193-N228, pH 5.0, 23°C
1020
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant E695A/Y697A, pH 7.0, 23°C
1050
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant Y697A, N- and C-terminal domain separately expressed, pH 7.0, 23°C
1100
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTA209-228, pH 5.0, 23°C
2200
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant E695A, N- and C-terminal domain separately expressed, pH 7.0, 23°C
2700
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant L690A/R691A, N- and C-terminal domain separately expressed, pH 7.0, 23°C
3300
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 23°C
3500
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant R691A, N- and C-terminal domain separately expressed, pH 7.0, 23°C
3700
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme R102K, at pH 6.0 and 25°C
4000
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild-type, N- and C-terminal domain separately expressed, pH 7.0, 23°C
4800
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant L690A/R691A, pH 7.0, 23°C
6800
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant R691A, pH 7.0, 23°C
8300
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant Y697A, pH 7.0, 23°C
8900
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant E695A, pH 7.0, 23°C
11500
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild-type, pH 7.0, 23°C
17000
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, wild type enzyme, at pH 6.0 and 25°C
140000
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme W105L, at pH 6.0 and 25°C
210000
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase activity, mutant enzyme W105F, at pH 6.0 and 25°C
0.22
H2O2
-
mutant enzyme R108A/W111F, peroxidase activity, at pH 4.5 and 25°C
0.29
H2O2
-
mutant enzyme R108A/W111F/D141A, peroxidase activity, at pH 4.5 and 25°C
2
H2O2
-
catalase activity, mutant enzyme H123E, in 100 mM phosphate buffer, pH 7.0, at 23°C
3.8
H2O2
-
mutant enzyme R108K, peroxidase activity, at pH 4.5 and 25°C
4.8
H2O2
-
catalatic activity, mutant enzyme W107F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
5.9
H2O2
-
mutant enzyme R108A/D141A, peroxidase activity, at pH 4.5 and 25°C
6
H2O2
-
catalase activity, mutant enzyme Y249F, in 100 mM phosphate buffer, pH 7.0, at 23°C
7.3
H2O2
-
mutant enzyme D141E, peroxidase activity, at pH 4.5 and 25°C
7.7
H2O2
-
catalatic activity, mutant enzyme W107F/W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
8.2
H2O2
-
mutant enzyme D141A, peroxidase activity, at pH 4.5 and 25°C; mutant enzyme R108A, peroxidase activity, at pH 4.5 and 25°C
9.8
H2O2
-
mutant enzyme D141N, peroxidase activity, at pH 4.5 and 25°C
12
H2O2
-
catalatic activity, mutant enzyme H108L, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
14.4
H2O2
-
wild type enzyme, peroxidase activity, at pH 4.5 and 25°C
22.4
H2O2
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
26
H2O2
-
catalase activity, mutant enzyme KatGDELTAFG, 100 mM phosphate buffer pH 7.0, at 23°C; peroxidase activity, mutant enzyme KatGDELTAFG, in 50 mM acetate buffer pH 5.0, at 23°C
26
H2O2
-
mutant enzyme I290A, at pH 5.0 and 23°C; mutant enzyme I290V, at pH 5.0 and 23°C; mutant enzyme Q293V, at pH 5.0 and 23°C
32
H2O2
-
mutant enzyme R108A/W111F/D141A, catalase activity, at pH 7.0 and 37°C
34
H2O2
-
mutant enzyme R108A/W111F, catalase activity, at pH 7.0 and 37°C
58
H2O2
-
peroxidase activity, wild type enzyme, in 50 mM acetate buffer pH 5.0, at 23°C
65
H2O2
-
wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
170
H2O2
-
catalase activity, mutant enzyme R439A, in 100 mM phosphate buffer, pH 7.0, at 23°C
200
H2O2
-
mutant enzyme D152S, catalase activity, pH and temperature not specified in the publication
200
H2O2
-
catalase activity, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C
200
H2O2
-
catalase activity, mutant enzyme D152S, in 100 mM phosphate buffer, pH 7.0, at 23°C
265
H2O2
-
mutant enzyme D141A, catalase activity, at pH 7.0 and 37°C
580
H2O2
-
catalase activity, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C
890
H2O2
-
mutant enzyme E243Q, catalase activity, pH and temperature not specified in the publication
1190
H2O2
-
mutant enzyme D141N, catalase activity, at pH 7.0 and 37°C
1950
H2O2
-
mutant enzyme R108A, catalase activity, at pH 7.0 and 37°C
2100
H2O2
-
mutant enzyme S315T, catalase activity, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
2110
H2O2
-
mutant enzyme R108K, catalase activity, at pH 7.0 and 37°C
2140
H2O2
-
mutant enzyme Y111A, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C
2300
H2O2
-
catalatic activity, mutant enzyme W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
2300
H2O2
-
catalatic activity, in 10 mM K2HPO4/KH2PO4 (pH 7.5), at 25°C
3500
H2O2
-
wild type enzyme, catalase activity, pH and temperature not specified in the publication
3500
H2O2
-
catalase activity, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C
3500
H2O2
-
catalase activity, wild type enzyme, in 100 mM phosphate buffer, pH 7.0, at 23°C
4620
H2O2
-
mutant enzyme R108A/D141A, catalase activity, at pH 7.0 and 37°C
5680
H2O2
-
wild type enzyme, catalase activity, at pH 7.0 and 37°C
5800
H2O2
-
wild type enzyme, catalase activity, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
6000
H2O2
-
catalase activity, wild type enzyme, in 100 mM phosphate buffer, pH 7.0, at 23°C
6140
H2O2
-
mutant enzyme D141E, catalase activity, at pH 7.0 and 37°C
6446
H2O2
-
wild-type, pH not specified in the publication, temperature not specified in the publication
6729
H2O2
-
mutant C55A/C74A, pH not specified in the publication, temperature not specified in the publication
6745
H2O2
-
mutant C55A, pH not specified in the publication, temperature not specified in the publication
6800
H2O2
-
catalatic activity, wild type enzyme, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
7113
H2O2
-
mutant C26A/C74A, pH not specified in the publication, temperature not specified in the publication
7200
H2O2
-
catalase activity, in 67 mM phosphate buffer (pH 7.0), at 25°C
7565
H2O2
-
mutant C74A, pH not specified in the publication, temperature not specified in the publication
10100
H2O2
-
wild type enzyme, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C
11000
H2O2
-
wild type enzyme, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C
11400
H2O2
-
mutant enzyme R463L, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C
12000
H2O2
-
catalase activity, wild type enzyme, 100 mM phosphate buffer pH 7.0, at 23°C
0.057
isoniazid
-
wild type enzyme, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
0.081
isoniazid
-
mutant enzyme S315T, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
1.2
o-Dianisidine
-
mutant enzyme S315T, peroxidase activity, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
2
o-Dianisidine
-
wild type enzyme, peroxidase activity, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM