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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) + tert-butyl hydroperoxide
oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) + ?
-
-
-
-
?
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
2,4-dichlorophenol + H2O2
?
-
-
-
?
2,6-dimethoxyphenol + H2O2
oxidized 2,6-dimethoxyphenol + H2O
-
-
-
-
?
2-dianisidine + tert-butyl hydroperoxide
?
-
peroxidase activity
-
-
?
3,3',5,5'-tetramethylbenzidine + H2O2
? + H2O
-
-
-
-
?
3,3',5,5'-tetramethylbenzidine + H2O2
oxidized 3,3',5,5'-tetramethylbenzidine + H2O
-
-
-
-
?
3,3'-diaminobenzidine + H2O2
oxidized 3,3'-diaminobenzidine + H2O
3,3'-dimethoxybenzidine + H2O2
oxidized 3,3'-dimethoxybenzidine + H2O
3-chloro-peroxybenzoic acid
?
-
-
-
-
?
3-chloroperoxybenzoic acid
?
-
-
-
-
?
3-methoxyphenol + H2O2
? + H2O
4-aminoantipyrine + H2O2
oxidized 4-aminoantipyrine + H2O
4-phenylenediamine + H2O2
oxidized 4-phenylenediamine + H2O
aminoantipyrine + H2O2
oxidized aminoantipyrine + H2O
-
-
-
?
ascorbate + H2O2
monodehydroascorbate + H2O
chlorpromazine + H2O2
? + H2O
-
-
-
-
?
diaminobenzidine + H2O2
oxidized diaminobenzidine + H2O
donor + H2O2
oxidized donor + 2 H2O
ethanol + H2O2
acetaldehyde + ?
guaiacol + H2O2
tetraguaiacol + H2O
guajacol + H2O2
? + H2O
-
peroxidase activity
-
-
?
H2O2 + o-dianisidine
?
-
peroxidase activity
-
-
?
isoniazid + H2O2
oxidized isoniazid + 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
-
?
isoniazid + phenol + H2O2
benzoquinone + ?
methanol + H2O2
formaldehyde + H2O
-
at pH 4.5
-
-
?
N,N,N',N'-tetramethyl-p-phenylenediamine + H2O2
? + H2O
-
-
-
-
?
o-dianisidine + H2O2
? + H2O
o-dianisidine + H2O2
oxidized o-dianisidine + 2 H2O
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
o-dianisidine + tert-butyl hydroperoxide
o-dianisidine quinonediimine + ?
-
-
-
-
?
o-dianisidine + tert-butyl hydroperoxide
oxidized o-dianisidine + ?
-
-
-
-
?
o-dianisidine + tert-butyl hydroperoxide + H2O2
o-dianisidin quinone diimine + ?
o-phenylenediamine + H2O2
oxidized o-phenylenediamine + H2O
-
-
-
-
?
penicillin G + H2O2
penicillin G (R)-sulfoxide + H2O
-
-
-
-
?
peroxyacetic acid + 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
?
pyrogallol + H2O2
? + H2O
reduced 2,3',6'-trichloroindophenol + H2O2
oxidized 2,3',6'-trichloroindophenol + H2O
reduced cytochrome c + H2O2
oxidized cytochrome c + H2O
-
-
-
-
?
tert-butyl hydroperoxide + H2O2
oxidized tert-butyl hydroperoxide + H2O
tert-butyl peroxide + H2O2
?
additional information
?
-
2 H2O2
2 H2O + O2
-
-
-
-
?
2 H2O2
2 H2O + O2
-
-
-
?
2 H2O2
2 H2O + O2
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
peroxidase activity
-
-
?
2 H2O2
O2 + 2 H2O
peroxidase activity
-
-
?
2 H2O2
O2 + 2 H2O
peroxidase activity
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
-
?
2 H2O2
O2 + 2 H2O
peroxidase activity
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
peroxidase activity
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
peroxidase activity
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + 2 H2O
-
-
-
?
2 H2O2
O2 + H2O
-
-
-
-
?
2 H2O2
O2 + H2O
-
-
-
-
?
2 H2O2
O2 + H2O
-
-
-
-
?
2 H2O2
O2 + H2O
-
-
-
-
?
2 H2O2
O2 + H2O
-
-
-
-
?
2 H2O2
O2 + H2O
-
-
-
-
?
2 H2O2
O2 + H2O
-
-
-
-
?
2 H2O2
O2 + H2O
-
-
-
-
?
2 H2O2
O2 + H2O
-
-
-
-
?
2 H2O2
O2 + H2O
-
-
-
-
?
2 H2O2
O2 + 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
? + 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
?
-
-
-
?
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-aminoantipyrine + H2O2
oxidized 4-aminoantipyrine + H2O
-
-
-
-
?
4-phenylenediamine + H2O2
oxidized 4-phenylenediamine + H2O
-
-
-
?
4-phenylenediamine + H2O2
oxidized 4-phenylenediamine + H2O
-
highest specific peroxidase activity
-
-
?
aniline + H2O2
? + H2O
about 25% conversion
-
-
?
aniline + H2O2
? + H2O
about 25% conversion
-
-
?
ascorbate + H2O2
monodehydroascorbate + H2O
-
-
-
-
?
ascorbate + H2O2
monodehydroascorbate + H2O
-
-
-
-
?
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
-
?
diaminobenzidine + H2O2
oxidized diaminobenzidine + H2O
-
-
-
-
?
diaminobenzidine + H2O2
oxidized diaminobenzidine + H2O
-
-
-
-
?
diaminobenzidine + H2O2
oxidized diaminobenzidine + H2O
-
-
-
-
?
donor + H2O2
oxidized donor + 2 H2O
catalase activity
-
-
?
donor + H2O2
oxidized donor + 2 H2O
catalase activity
-
-
?
donor + H2O2
oxidized donor + 2 H2O
catalase activity
-
-
?
ethanol + H2O2
acetaldehyde + ?
-
-
-
?
ethanol + H2O2
acetaldehyde + ?
-
-
-
?
guaiacol + H2O2
?
-
-
-
?
guaiacol + H2O2
?
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
-
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
-
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
-
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
-
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
-
-
-
?
guaiacol + H2O2
tetraguaiacol + H2O
-
-
-
-
?
H2O2
O2 + H2O
-
-
-
-
?
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
-
KatP has stronger catalase than peroxidase activity
-
-
?
H2O2
O2 + H2O
-
-
439783, 654206, 654769, 713946, 714145, 714795, 715014, 715431, 715806, 716245, 716246 -
-
?
H2O2
O2 + H2O
-
catalase activity
-
-
?
H2O2
O2 + H2O
-
catalase activity
-
-
?
H2O2
O2 + H2O
-
catalase activity
-
-
?
isoniazid + H2O2
?
-
-
-
?
isoniazid + H2O2
?
-
-
-
?
isoniazid + H2O2
?
-
-
-
-
?
isoniazid + H2O2
?
-
-
-
-
?
isoniazid + H2O2
?
-
-
-
-
?
isoniazid + H2O2
?
-
-
-
-
?
isoniazid + H2O2
?
-
-
-
-
?
isoniazid + H2O2
?
-
-
-
?
isoniazid + H2O2
?
-
-
-
-
?
isoniazid + H2O2
?
-
activation of antituberculosis drug isonazid, catalytic mechanism
-
-
?
isoniazid + H2O2
?
pro-drug activation
-
-
?
isoniazid + H2O2
?
-
pro-drug activation
-
-
?
isoniazid + H2O2
?
pro-drug activation
-
-
?
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
?
-
-
-
?
isoniazid + H2O2
?
pro-drug activation
-
-
?
isoniazid + H2O2
?
enzyme binding structure analysis, modeling, overview
-
-
?
isoniazid + H2O2
?
-
-
-
?
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
?
-
-
-
?
isoniazid + H2O2
?
pro-drug activation
-
-
?
isoniazid + H2O2
?
enzyme binding structure analysis, modeling, overview
-
-
?
isoniazid + H2O2
?
-
-
-
?
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
oxidized isoniazid + H2O
-
-
-
-
?
isoniazid + H2O2
oxidized isoniazid + H2O
-
-
-
-
?
isoniazid + H2O2
oxidized isoniazid + H2O
-
-
-
-
?
isoniazid + H2O2
oxidized isoniazid + H2O
-
i.e. isonicotinic acid hydrazide
-
-
?
isoniazid + H2O2
oxidized isoniazid + H2O
-
-
-
?
isoniazid + H2O2
oxidized isoniazid + H2O
-
-
-
?
isoniazid + phenol + H2O2
benzoquinone + ?
-
-
-
?
isoniazid + phenol + H2O2
benzoquinone + ?
-
-
-
?
NADH + H2O2
?
-
-
-
-
?
NADPH + H2O2
?
-
-
-
-
?
o-dianisidine + H2O2
?
-
-
-
?
o-dianisidine + H2O2
?
-
-
-
?
o-dianisidine + H2O2
?
-
-
-
?
o-dianisidine + H2O2
?
-
-
-
?
o-dianisidine + H2O2
? + H2O
-
-
-
?
o-dianisidine + H2O2
? + H2O
-
-
-
?
o-dianisidine + H2O2
? + H2O
-
-
-
-
?
o-dianisidine + H2O2
? + H2O
-
peroxidase 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
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 + 2 H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
o-dianisidine + H2O2
oxidized o-dianisidine + H2O
-
-
-
-
?
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
?
-
-
-
-
?
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
?
-
-
-
-
?
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
-
?
pyrogallol + H2O2
?
-
-
-
?
pyrogallol + H2O2
?
-
-
-
?
pyrogallol + H2O2
? + H2O
-
-
-
-
?
pyrogallol + H2O2
? + H2O
-
-
-
-
?
pyrogallol + H2O2
? + H2O
-
-
-
-
?
pyrogallol + H2O2
? + H2O
-
-
-
-
?
pyrogallol + H2O2
? + H2O
-
-
-
-
?
pyrogallol + H2O2
? + H2O
-
-
-
-
?
pyrogallol + H2O2
? + H2O
-
-
-
-
?
pyrogallol + H2O2
? + H2O
-
-
-
-
?
pyrogallol + H2O2
? + H2O
-
-
-
-
?
pyrogallol + H2O2
? + H2O
-
-
-
-
?
pyrogallol + H2O2
? + H2O
-
peroxidase activity
-
-
?
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
-
-
-
-
?
tert-butyl peroxide + H2O2
?
-
-
-
?
tert-butyl peroxide + H2O2
?
-
-
-
?
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
?
-
-
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
-
-
?
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0.0055 - 6
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
0.063 - 0.096
2-dianisidine
0.7
3,3',5,5'-tetramethylbenzidine
-
pH 5.0, 23°C
0.13
ascorbate
-
pH 5.0, 23°C
1.1
chlorpromazine
-
pH 5.0, 23°C
1.2
N,N,N',N'-tetramethyl-p-phenylenediamine
-
pH 5.0, 23°C
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
0.04 - 0.49
o-Dianisidine
0.97
peroxyacetic acid
pH 4.5, 37°C
5.7 - 97.9
tert-butyl hydroperoxide
additional information
additional information
-
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)
mutant enzyme R108A/W111F, peroxidase activity, at pH 4.5 and 25°C
0.024
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
peroxidase reaction, at pH 4.3 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
0.032
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 4.0, 23°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
0.053
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 4.5, 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
0.06
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 6.0, 23°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
0.07
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
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)
-
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)
-
pH 5.5, 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, in 50 mM phosphate buffer, pH 7.0, at 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
0.13
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 DELTA209-228, pH 5.0, 23°C
1.2
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant E695A/Y697A, pH 7.0, 23°C
1.6
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
2.7
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
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
0.063
2-dianisidine
-
recombinant mutant D735A, 23°C
0.064
2-dianisidine
-
recombinant mutant A110V, 23°C
0.065
2-dianisidine
-
recombinant mutant L634F, 23°C
0.078
2-dianisidine
-
recombinant mutant L619P, 23°C
0.081
2-dianisidine
-
recombinant mutant S315N, 23°C
0.084
2-dianisidine
-
recombinant wild-type enzyme, 23°C
0.096
2-dianisidine
-
recombinant mutant A139P, 23°C
0.06
H2O2
-
peroxidase reaction, at pH 4.3 and 25°C
0.06
H2O2
-
mutant enzyme E291K, at pH 5.0 and 23°C
0.06
H2O2
-
mutant enzyme E291K/E292A, at pH 5.0 and 23°C
0.07
H2O2
-
mutant enzyme S315T, catalase activity, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
0.07
H2O2
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
0.07
H2O2
-
wild type enzyme, catalase activity, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
0.07
H2O2
-
mutant enzyme I290A/Q293A, at pH 5.0 and 23°C
0.078
H2O2
-
mutant enzyme Q293A, at pH 5.0 and 23°C
0.08
H2O2
-
mutant enzyme I290V, at pH 5.0 and 23°C
0.089
H2O2
-
mutant enzyme Q293E, at pH 5.0 and 23°C
0.09
H2O2
mutant enzyme D141N, peroxidase activity, at pH 4.5 and 25°C
0.09
H2O2
-
mutant enzyme I290A, at pH 5.0 and 23°C
0.095
H2O2
-
peroxidase reaction, at pH 4.5 and 25°C
0.1
H2O2
-
mutant enzyme E291A, at pH 5.0 and 23°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
0.21
H2O2
-
peroxidase reaction, at pH 4.0 and 25°C
0.21
H2O2
-
mutant enzyme I290V/Q293V, at pH 5.0 and 23°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
0.31
H2O2
-
wild type enzyme, at pH 5.0 and 23°C
0.36
H2O2
-
peroxidase reaction, at pH 4.8 and 25°C
0.5
H2O2
mutant enzyme R108A, peroxidase activity, at pH 4.5 and 25°C
0.5
H2O2
-
peroxidatic activity, pH 6.0, 25°C
0.5
H2O2
-
mutant enzyme Q293V, at pH 5.0 and 23°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
0.65
H2O2
-
peroxidase activity, pH 5.3, 30°C
0.7
H2O2
-
peroxidase reaction, at pH 4.5 and 25°C
0.8
H2O2
-
no electron donor present, pH 5.0, 23°C
0.83
H2O2
-
peroxidase activity, wild type enzyme, in 50 mM acetate buffer pH 5.0, at 23°C
0.83
H2O2
-
peroxidase reaction, at pH 5.0 and 25°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
H2O2
-
peroxidase reaction, at pH 4.3 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
2.4
H2O2
-
mutant D152S, pH 7.0, 30°C
2.4
H2O2
-
mutant D152S, pH 7.0, 30°C
2.4
H2O2
-
catalase reaction, at pH 7.0 and 37°C
2.5
H2O2
-
mutants D152N and P151A, pH 7.0, 30°C
2.5
H2O2
-
mutants D152N and P151A, pH 7.0, 30°C
2.5
H2O2
-
catalatic activity, pH 7.5, 25°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
3.1
H2O2
-
catalase reaction, at pH 7.0 and 37°C
3.16
H2O2
wild type enzyme, at pH 7.0 and 30°C
3.2
H2O2
-
mutant D152W, pH 7.0, 30°C
3.2
H2O2
-
mutant D152W, pH 7.0, 30°C
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
3.7
H2O2
-
catalase reaction, at pH 7.0 and 37°C
3.7
H2O2
-
catalase reaction, at pH 7.0 and 37°C
3.7
H2O2
wild type enzyme, catalase activity, at pH 7.0 and 37°C
3.8
H2O2
-
catalase reaction, at pH 7.0 and 37°C
3.82
H2O2
-
catalase activity, pH 7.0, 37°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
-
wild-type enzyme, pH 7.0, 30°C
4.1
H2O2
-
wild-type enzyme, pH 7.0, 30°C
4.1
H2O2
-
catalase activity, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C
4.2
H2O2
-
catalase reaction, at pH 7.0 and 37°C
4.3
H2O2
-
mutant W341A, pH 7.0, 30°C
4.3
H2O2
-
catalase activity, in 67 mM phosphate buffer (pH 7.0), at 25°C
4.44
H2O2
mutant enzyme N238S, at pH 7.0 and 30°C
4.5
H2O2
-
catalase activity, mutant enzyme KatGDELTAFG, 100 mM phosphate buffer pH 7.0, at 23°C
4.5
H2O2
-
catalase reaction, at pH 7.0 and 37°C
4.8
H2O2
at pH 6.0 and 25°C
4.9
H2O2
-
catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°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
5.9
H2O2
-
mutant D402E, pH 7.0, 30°C
5.9
H2O2
-
recombinant wild-type enzyme, 23°C
5.9
H2O2
-
catalase activity, wild type enzyme, at pH 7.0 and 37°C
6.16
H2O2
-
mutant enzyme R463L, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C
6.3
H2O2
-
mutant W341F, pH 7.0, 30°C
6.3
H2O2
-
catalase activity, in 50 mM potassium phosphate buffer (pH 7.0), at 30°C
6.4
H2O2
-
mutant D402N, pH 7.0, 30°C
6.5
H2O2
-
catalase activity, pH 6.3, 30°C
6.7
H2O2
-
catalase activity, pH and temperature not specified in the publication
10.3
H2O2
-
recombinant mutant A110V, 23°C
10.7
H2O2
-
recombinant mutant A139P, 23°C
10.8
H2O2
-
catalase activity, at pH 6.4 and 25°C
12
H2O2
-
catalase activity, mutant enzyme R102K, at pH 7.0 and 37°C
13
H2O2
mutant enzyme R108A, catalase activity, at pH 7.0 and 37°C
14.3
H2O2
-
recombinant mutant L634F, 23°C
14.8
H2O2
-
recombinant mutant D735A, 23°C
15
H2O2
-
mutant H290Q, pH 7.0, 30°C
16.8
H2O2
-
recombinant mutant S315N, 23°C
17.1
H2O2
-
recombinant mutant L619P, 23°C
20
H2O2
-
catalase reaction, at pH 5.5-6.0 and 37°C
24
H2O2
-
catalase activity, in 20 mM Tris-HCl buffer (pH 9.0), at 30°C
27
H2O2
-
in 100 mM phosphate buffer, pH 7.0, at 23°C
28
H2O2
-
catalase activity, mutant enzyme H106C, at pH 7.0 and 37°C
30
H2O2
-
catalase reaction, at pH 5.5-6.0 and 37°C
30
H2O2
-
catalatic activity, in 10 mM K2HPO4/KH2PO4 (pH 7.5), at 25°C
31
H2O2
-
catalase activity, mutant enzyme R102C, at pH 7.0 and 37°C
31.5
H2O2
-
catalatic activity, mutant enzyme W107F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
32
H2O2
-
catalase reaction, at pH 5.5-6.0 and 37°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
-
catalase activity, mutant enzyme R102L, at pH 7.0 and 37°C
33
H2O2
-
catalatic activity, mutant enzyme W107F/W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
35
H2O2
-
catalase reaction, at pH 5.5-6.0 and 37°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
53
H2O2
-
catalase activity, mutant enzyme H267Y, at pH 7.0 and 37°C
53
H2O2
pH 5.5, 25°C, recombinant intein-tagged enzyme
54.9
H2O2
-
catalatic activity, mutant enzyme H108L, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
56
H2O2
-
catalase reaction, at pH 5.5-6.0 and 37°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
77
H2O2
-
catalase activity, mutant enzyme W105L, at pH 7.0 and 37°C
90
H2O2
-
catalase reaction, at pH 5.5-6.0 and 37°C
91
H2O2
-
catalase activity, mutant enzyme W105F, at pH 7.0 and 37°C
95
H2O2
mutant enzyme D141N, catalase activity, at pH 7.0 and 37°C
100
H2O2
-
catalase activity, mutant enzyme H106Y, at pH 7.0 and 37°C
180
H2O2
mutant enzyme R108K, catalase activity, at pH 7.0 and 37°C
225
H2O2
-
catalase reaction, at pH 5.5-6.0 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
5.6
isoniazid
wild type enzyme, at pH 7.8 and 37°C
10.18
isoniazid
mutant enzyme S308T, at pH 7.8 and 37°C
0.04
o-Dianisidine
-
pH 4.0, 23°C
0.0478
o-Dianisidine
-
peroxidase activity, in 50 mM potassium phosphate buffer (pH 7.0), at 30°C
0.05
o-Dianisidine
-
pH 4.5, 23°C
0.09
o-Dianisidine
-
pH 5.0, 23°C
0.11
o-Dianisidine
-
pH 5.5, 23°C
0.12
o-Dianisidine
-
pH 6.0, 23°C
0.14
o-Dianisidine
-
peroxidatic activity, with hydrogen peroxide as cosubstrate, in 50 mM phosphate buffer, pH 7.0, at 25°C
0.14
o-Dianisidine
-
peroxidatic activity, with tert-butyl hydroperoxide as cosubstrate, in 50 mM phosphate buffer, pH 7.0, at 25°C
0.25
o-Dianisidine
wild type enzyme, at pH 4.5 and 30°C
0.35
o-Dianisidine
mutant enzyme N238S, at pH 4.5 and 30°C
0.49
o-Dianisidine
-
pH 5.0, 23°C
0.2
pyrogallol
-
pH 5.0, 23°C
0.31
pyrogallol
-
peroxidatic activity, in 50 mM phosphate buffer, pH 7.0, at 25°C
1.1
pyrogallol
-
pH 4.5, 23°C
1.1
pyrogallol
-
pH 4.0, 23°C
1.3
pyrogallol
-
pH 5.0, 23°C
1.5
pyrogallol
-
pH 5.5, 23°C
1.6
pyrogallol
-
pH 6.0, 23°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
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
steady- and transient-state kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.34 - 210000
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
0.86 - 4.85
2-dianisidine
5220
3,3',5,5'-tetramethylbenzidine
-
pH 5.0, 23°C
520
ascorbate
-
pH 5.0, 23°C
7940
chlorpromazine
-
pH 5.0, 23°C
7012
N,N,N',N'-tetramethyl-p-phenylenediamine
-
pH 5.0, 23°C
19.42
peroxyacetic acid
pH 4.5, 37°C
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
11
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 6.0, 23°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)
-
pH 5.5, 23°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)
-
pH 5.0, 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
92
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 4.5, 23°C
97
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant Y22F, pH 5.0, 23°C
151
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 4.0, 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
0.86
2-dianisidine
-
recombinant mutant S315N, 23°C
0.99
2-dianisidine
-
recombinant mutants L634F and D735A, 23°C
1.06
2-dianisidine
-
recombinant mutant L619P, 23°C
1.69
2-dianisidine
-
recombinant mutant A139P, 23°C
3.48
2-dianisidine
-
recombinant wild-type enzyme, 23°C
4.85
2-dianisidine
-
recombinant mutant A110V, 23°C
0.0061
H2O2
-
catalase activity, mutant enzyme H106Y, at pH 7.0 and 37°C
0.089
H2O2
-
catalase activity, mutant enzyme H106C, at pH 7.0 and 37°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
1.1
H2O2
-
catalase activity, mutant enzyme W105F, at pH 7.0 and 37°C
2
H2O2
-
catalase activity, mutant enzyme H123E, in 100 mM phosphate buffer, pH 7.0, at 23°C
2.1
H2O2
-
catalase activity, mutant enzyme R102K, at pH 7.0 and 37°C
2.6
H2O2
-
catalase activity, mutant enzyme H267Y, at pH 7.0 and 37°C
3
H2O2
-
mutant H290Q, pH 7.0, 30°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
8.2
H2O2
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
13.6
H2O2
-
mutant enzyme I290A/Q293A, at pH 5.0 and 23°C
14.4
H2O2
wild type enzyme, peroxidase activity, at pH 4.5 and 25°C
16
H2O2
-
mutant W341A, pH 7.0, 30°C
17
H2O2
-
mutant D402N, pH 7.0, 30°C
20
H2O2
-
mutant D152W, pH 7.0, 30°C
20
H2O2
-
mutant D152W, pH 7.0, 30°C
21
H2O2
-
mutant D402E, pH 7.0, 30°C
22.4
H2O2
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
23
H2O2
-
catalase activity, mutant enzyme W105L, at pH 7.0 and 37°C
23.8
H2O2
-
mutant enzyme Q293E, at pH 5.0 and 23°C
24
H2O2
-
mutant enzyme I290V/Q293V, at pH 5.0 and 23°C
26
H2O2
-
catalase activity, mutant enzyme KatGDELTAFG, 100 mM phosphate buffer pH 7.0, at 23°C
26
H2O2
-
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
26
H2O2
-
mutant enzyme I290V, at pH 5.0 and 23°C
26
H2O2
-
mutant enzyme Q293V, at pH 5.0 and 23°C
27.8
H2O2
-
mutant enzyme Q293A, 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
34
H2O2
-
mutant enzyme E291K, at pH 5.0 and 23°C
35.3
H2O2
-
mutant enzyme E291K/E292A, at pH 5.0 and 23°C
40
H2O2
-
mutant enzyme E291A, at pH 5.0 and 23°C
53.5
H2O2
-
catalase activity, mutant enzyme R102C, 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
83
H2O2
-
wild type enzyme, at pH 5.0 and 23°C
95
H2O2
-
mutant D152N, pH 7.0, 30°C
95
H2O2
-
mutant D152N, pH 7.0, 30°C
98
H2O2
pH 5.0, 25°C, with o-dianisidine, recombinant intein-tagged enzyme
170
H2O2
-
catalase activity, mutant enzyme R439A, in 100 mM phosphate buffer, pH 7.0, at 23°C
200
H2O2
-
mutant D152S, pH 7.0, 30°C
200
H2O2
-
mutant D152S, pH 7.0, 30°C
200
H2O2
-
catalase activity, mutant enzyme D152S, in 100 mM phosphate buffer, pH 7.0, at 23°C
200
H2O2
-
catalase activity, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C
200
H2O2
-
mutant enzyme D152S, catalase activity, pH and temperature not specified in the publication
227.5
H2O2
mutant enzyme N238S, at pH 7.0 and 30°C
265
H2O2
mutant enzyme D141A, catalase activity, at pH 7.0 and 37°C
270
H2O2
mutant enzyme R461A, at pH 5.5 and 30°C
272.3
H2O2
wild type enzyme, at pH 7.0 and 30°C
551
H2O2
pH 5.5, 25°C, recombinant intein-tagged enzyme
570
H2O2
-
no electron donor present, pH 5.0, 23°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
900
H2O2
-
catalase activity, mutant enzyme R102L, at pH 7.0 and 37°C
1190
H2O2
mutant enzyme D141N, catalase activity, at pH 7.0 and 37°C
1460
H2O2
-
mutant W341F, pH 7.0, 30°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, in 10 mM K2HPO4/KH2PO4 (pH 7.5), at 25°C
2300
H2O2
-
catalatic activity, mutant enzyme W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
2500
H2O2
-
mutant P151A, pH 7.0, 30°C
2500
H2O2
-
mutant P151A, pH 7.0, 30°C
2750
H2O2
-
recombinant mutant D735A, 23°C
2950
H2O2
-
catalase reaction, at pH 7.0 and 37°C
2990
H2O2
-
recombinant mutant S315N, 23°C
3180
H2O2
-
recombinant mutant L619P, 23°C
3270
H2O2
-
recombinant wild-type enzyme, 23°C
3330
H2O2
-
recombinant mutant A139P, 23°C
3450
H2O2
-
recombinant mutant L634F, 23°C
3500
H2O2
-
wild-type enzyme, pH 7.0, 30°C
3500
H2O2
-
wild-type enzyme, pH 7.0, 30°C
3500
H2O2
-
catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C
3500
H2O2
-
catalase activity, wild type enzyme, in 100 mM phosphate buffer, pH 7.0, at 23°C
3500
H2O2
-
catalase activity, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C
3500
H2O2
-
wild type enzyme, catalase activity, pH and temperature not specified in the publication
4300
H2O2
-
catalase reaction, at pH 7.0 and 37°C
4350
H2O2
-
catalase reaction, at pH 7.0 and 37°C
4620
H2O2
mutant enzyme R108A/D141A, catalase activity, at pH 7.0 and 37°C
4970
H2O2
-
catalase reaction, at pH 5.5-6.0 and 37°C
5230
H2O2
-
recombinant mutant A110V, 23°C
5300
H2O2
-
catalase activity, wild type enzyme, at pH 7.0 and 37°C
5680
H2O2
-
catalase reaction, 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
6450
H2O2
wild type enzyme, at pH 5.3 and 30°C
6640
H2O2
-
catalase reaction, at pH 7.0 and 37°C
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
7010
H2O2
at pH 6.0 and 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
7600
H2O2
-
catalase reaction, at pH 5.5-6.0 and 37°C
7630
H2O2
-
catalase reaction, at pH 7.0 and 37°C
7770
H2O2
-
catalase reaction, at pH 7.0 and 37°C
8000
H2O2
-
catalase reaction, at pH 5.5-6.0 and 37°C
9600
H2O2
-
mutant DELTA200-214, catalase activity, pH 7.0, 23°C
10100
H2O2
-
wild type enzyme, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C
10200
H2O2
-
catalase reaction, at pH 5.5-6.0 and 37°C
11000
H2O2
-
wild type enzyme, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C
11000
H2O2
-
wild-type, catalase activity, 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
14100
H2O2
-
catalase reaction, at pH 5.5-6.0 and 37°C
15680
H2O2
-
catalase reaction, at pH 5.5-6.0 and 37°C
15900
H2O2
-
catalase reaction, at pH 5.5-6.0 and 37°C
18000
H2O2
-
in 100 mM phosphate buffer, pH 7.0, at 23°C
339000
H2O2
-
pH 7.0, 37°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
24
o-Dianisidine
-
pH 4.0, 23°C
33.3
o-Dianisidine
mutant enzyme N238S, at pH 4.5 and 30°C
37
o-Dianisidine
-
pH 4.5, 23°C
44
o-Dianisidine
pH 5.0, 25°C, recombinant intein-tagged enzyme
49
o-Dianisidine
wild type enzyme, at pH 4.5 and 30°C
58
o-Dianisidine
-
pH 5.0, 23°C
69
o-Dianisidine
-
pH 5.5, 23°C
71
o-Dianisidine
-
pH 6.0, 23°C
5600
o-Dianisidine
-
pH 5.0, 23°C
27
pyrogallol
-
pH 4.0, 23°C
44
pyrogallol
-
pH 4.5, 23°C
56
pyrogallol
-
pH 5.0, 23°C
64
pyrogallol
-
pH 5.5, 23°C
69
pyrogallol
-
pH 6.0, 23°C
630
pyrogallol
-
pH 5.0, 23°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.21 - 4400
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
7400
3,3',5,5'-tetramethylbenzidine
-
pH 5.0, 23°C
3900
ascorbate
-
pH 5.0, 23°C
7200
chlorpromazine
-
pH 5.0, 23°C
6000
N,N,N',N'-tetramethyl-p-phenylenediamine
-
pH 5.0, 23°C
20.02
peroxyacetic acid
pH 4.5, 37°C
3200
pyrogallol
-
pH 5.0, 23°C
0.014 - 0.48
tert-butyl hydroperoxide
0.21
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
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
5.1
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
6.3
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
17
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
26
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
in 50 mM acetate buffer, pH 5.0, at 23°C
70
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant L690A/R691A/E695A/Y697A, pH 7.0, 23°C
140
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme E291K/E292A, at pH 5.0 and 23°C
160
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Q293V, at pH 5.0 and 23°C
200
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant Y697A, N- and C-terminal domain separately expressed, pH 7.0, 23°C
200
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme I290A, at pH 5.0 and 23°C
220
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme I290V, at pH 5.0 and 23°C
270
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild-type, pH 5.0, 23°C
280
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme I290V/Q293V, at pH 5.0 and 23°C
350
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme I290A/Q293A, at pH 5.0 and 23°C
370
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Q293A, at pH 5.0 and 23°C
390
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Q293E, at pH 5.0 and 23°C
546
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
560
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme E291A, at pH 5.0 and 23°C
580
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTA200-214, pH 5.0, 23°C
600
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant E695A, N- and C-terminal domain separately expressed, pH 7.0, 23°C
630
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild type enzyme, at pH 5.0 and 23°C
634
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
750
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTAL193-N228, pH 5.0, 23°C
800
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant L690A/R691A, N- and C-terminal domain separately expressed, pH 7.0, 23°C
850
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant E695A/Y697A, pH 7.0, 23°C
900
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant R691A, N- and C-terminal domain separately expressed, pH 7.0, 23°C
960
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant DELTA209-228, pH 5.0, 23°C
1260
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant enzyme E291K, at pH 5.0 and 23°C
1700
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant L690A/R691A, pH 7.0, 23°C
1700
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild-type, N- and C-terminal domain separately expressed, pH 7.0, 23°C
2300
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant Y22F, pH 5.0, 23°C
2500
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant R691A, pH 7.0, 23°C
2500
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
wild-type, pH 7.0, 23°C
3100
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant E695A, pH 7.0, 23°C
4000
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
pH 5.0, 23°C
4400
2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
mutant Y697A, pH 7.0, 23°C
0.15
H2O2
-
catalatic activity, mutant enzyme W107F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
0.22
H2O2
-
catalatic activity, mutant enzyme H108L, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
0.23
H2O2
-
catalatic activity, mutant enzyme W107F/W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
0.32
H2O2
mutant enzyme R108A/W111F/D141A, peroxidase activity, at pH 4.5 and 25°C
0.39
H2O2
mutant enzyme R108A/W111F, peroxidase activity, at pH 4.5 and 25°C
0.9
H2O2
mutant enzyme R108A/W111F, catalase activity, at pH 7.0 and 37°C
0.9
H2O2
mutant enzyme R108A/W111F/D141A, catalase activity, at pH 7.0 and 37°C
1.3
H2O2
mutant enzyme D141N, catalase activity, at pH 7.0 and 37°C
3.9
H2O2
mutant enzyme R108K, peroxidase activity, at pH 4.5 and 25°C
4.4
H2O2
mutant enzyme D141A, catalase activity, at pH 7.0 and 37°C
5.7
H2O2
-
catalase activity, mutant enzyme KatGDELTAFG, 100 mM phosphate buffer pH 7.0, at 23°C
8.2
H2O2
mutant enzyme D141E, catalase activity, at pH 7.0 and 37°C
12
H2O2
mutant enzyme R108K, catalase activity, at pH 7.0 and 37°C
16
H2O2
mutant enzyme R108A, peroxidase activity, at pH 4.5 and 25°C
22
H2O2
mutant enzyme R108A/D141A, peroxidase activity, at pH 4.5 and 25°C
43
H2O2
mutant enzyme D141A, peroxidase activity, at pH 4.5 and 25°C
46
H2O2
wild type enzyme, peroxidase activity, at pH 4.5 and 25°C
49
H2O2
-
mutant enzyme Q293V, at pH 5.0 and 23°C
51.2
H2O2
mutant enzyme N238S, at pH 7.0 and 30°C
61
H2O2
mutant enzyme D141E, peroxidase activity, at pH 4.5 and 25°C
73
H2O2
-
catalatic activity, mutant enzyme W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
86.2
H2O2
wild type enzyme, at pH 7.0 and 30°C
110
H2O2
mutant enzyme D141N, peroxidase activity, at pH 4.5 and 25°C
110
H2O2
-
mutant enzyme I290V/Q293V, at pH 5.0 and 23°C
120
H2O2
-
catalase activity, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C
140
H2O2
mutant enzyme R108A/D141A, catalase activity, at pH 7.0 and 37°C
150
H2O2
mutant enzyme R108A, catalase activity, at pH 7.0 and 37°C
160
H2O2
-
catalatic activity, wild type enzyme, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
160
H2O2
-
mutant enzyme S315T, catalase activity, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
210
H2O2
-
mutant enzyme I290A/Q293A, at pH 5.0 and 23°C
250
H2O2
-
catalase activity, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C
268
H2O2
-
mutant enzyme Q293E, at pH 5.0 and 23°C
270
H2O2
-
wild type enzyme, at pH 5.0 and 23°C
310
H2O2
-
mutant enzyme I290A, at pH 5.0 and 23°C
320
H2O2
-
mutant enzyme Y111A, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
350
H2O2
-
mutant enzyme I290V, at pH 5.0 and 23°C
360
H2O2
-
wild type enzyme, peroxidase activity, in 50 mM acetate buffer, pH 5.0, 23°C
380
H2O2
-
mutant enzyme Q293A, at pH 5.0 and 23°C
390
H2O2
-
mutant enzyme E291A, at pH 5.0 and 23°C
410
H2O2
-
mutant enzyme Y111A, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C
600
H2O2
-
mutant enzyme E291K, at pH 5.0 and 23°C
620
H2O2
-
mutant enzyme E291K/E292A, at pH 5.0 and 23°C
640
H2O2
-
in 100 mM phosphate buffer, pH 7.0, at 23°C
710
H2O2
-
catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C
710
H2O2
-
no electron donor present, pH 5.0, 23°C
850
H2O2
-
catalase activity, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C
1000
H2O2
-
wild type enzyme, catalase activity, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
1300
H2O2
-
catalase activity, pH 7.0, 37°C
1500
H2O2
wild type enzyme, catalase activity, at pH 7.0 and 37°C
1680
H2O2
wild-type, pH not specified in the publication, temperature not specified in the publication
1850
H2O2
-
mutant enzyme R463L, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C
1880
H2O2
mutant C26A/C74A, pH not specified in the publication, temperature not specified in the publication
1880
H2O2
mutant C55A/C74A, pH not specified in the publication, temperature not specified in the publication
1950
H2O2
-
wild type enzyme, catalase activity, in 50 mM Na2HPO4, pH 7.0, 25°C
2020
H2O2
mutant C74A, pH not specified in the publication, temperature not specified in the publication
2170
H2O2
mutant C55A, pH not specified in the publication, temperature not specified in the publication
3100
H2O2
-
catalase activity, wild type enzyme, 100 mM phosphate buffer pH 7.0, at 23°C
3200
H2O2
-
wild type enzyme, catalase activity, in 100 mM phosphate buffer, pH 7.0, 23°C
19
o-Dianisidine
-
mutant enzyme S315T, peroxidase activity, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
32
o-Dianisidine
-
wild type enzyme, peroxidase activity, in 50 mM sodium phosphate buffer (pH 7.5), at 37°C
96
o-Dianisidine
mutant enzyme N238S, at pH 4.5 and 30°C
199
o-Dianisidine
wild type enzyme, at pH 4.5 and 30°C
1200
o-Dianisidine
-
pH 5.0, 23°C
0.014
tert-butyl hydroperoxide
-
peroxidatic activity, mutant enzyme W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
0.028
tert-butyl hydroperoxide
-
peroxidatic activity, mutant enzyme H108L, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
0.029
tert-butyl hydroperoxide
-
peroxidatic activity, wild type enzyme, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
0.42
tert-butyl hydroperoxide
-
peroxidatic activity, mutant enzyme W107F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
0.48
tert-butyl hydroperoxide
-
peroxidatic activity, mutant enzyme W107F/W321F, in 10 mM KH2PO4/K2HPO4, pH 6.0, at 25°C
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0.00904
-
specific peroxidase activity, using isoniazid as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C
0.0098
-
specific peroxidase activity, using isoniazid as substrate, purified mutant enzyme R463L, in 50 mM Na2HPO4, pH 5.5, 25°C
0.16
-
catalase activity, mutant enzyme H106Y, at pH 7.0 and 37°C
0.18
-
substrate o-dianisidine, mutant H290Q
0.208
-
specific peroxidase activity, using NADH as substrate, purified mutant enzyme R463L, in 50 mM Na2HPO4, pH 5.5, 25°C
0.212
-
specific peroxidase activity, using NADH as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C
0.25
-
catalase activity, mutant enzyme H106C, at pH 7.0 and 37°C
0.264
-
specific peroxidase activity, using NADPH as substrate, purified mutant enzyme R463L, in 50 mM Na2HPO4, pH 5.5, 25°C
0.272
-
specific peroxidase activity, using NADPH as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C
0.45
peroxidase activity from crude extract, in 50 mM potassium phosphate/sodium citrate buffer, pH 4.5, at 80°C
0.5
-
substrate guajacol, mutant P151A
0.55
-
peroxidase activity, using guaiacol as substrate, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C
0.61
-
crude enzyme, peroxidase activity, in 67 mM phosphate buffer, pH 7.0, at 25°C
0.8
-
substrate o-dianisidine, mutant W341A
1
-
peroxidase specific activity, using o-dianisidine as substrate, at pH 5.0 and 25°C
1.7
-
after 2.79fold purification, peroxidase activity, in 67 mM phosphate buffer, pH 7.0, at 25°C
1.8
-
substrate o-dianisidine, mutant D402N
100.7
-
specific peroxidase activity, using 4-phenylendiamine as substrate, purified mutant enzyme R463L, in 50 mM Na2HPO4, pH 5.5, 25°C
104.3
-
after 29.6fold purification, peroxidase activity, in 50 mM potassium phosphate containing 2 M NaCl, pH 7.5, at 25°C
1145
-
after 47.3fold purification, in 50 mM potassium phosphate buffer (pH 7.0), at 30°C
12.5
-
substrate pyrogallol, mutant D152N
13.6
-
substrate pyrogallol, mutant D152S
1300
-
peroxidase activity, mutant enzyme W105L, at pH 7.0 and 37°C
14.9
purified recombinant intein-tagged enzyme, pH 5.5, 25°C, peroxidase activity
150
-
peroxidase activity using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 5.4 and 25°C
16
-
peroxidase activity using 3,3'-diaminobenzidine as substrate, at pH 5.4 and 25°C
168
-
unpurified cytosolic fraction, peroxidase activity, in 50 mM Tris-HCl buffer (pH 8.5), at 30°C
18
-
peroxidase activity, mutant enzyme H106Y, at pH 7.0 and 37°C
19
-
catalase activity, mutant enzyme R102L, at pH 7.0 and 37°C
2
-
peroxidase specific activity, using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 5.0 and 25°C
2.1
-
substrate o-dianisidine, mutant D402E
2.12
-
specific peroxidase activity, using pyrogallol as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C
2.29
-
specific peroxidase activity, using pyrogallol as substrate, purified mutant enzyme R463L, in 50 mM Na2HPO4, pH 5.5, 25°C
22.8
-
specific peroxidase activity, using o-dianisidine as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C
226
-
specific catalase activity, crude extract, in 50 mM Na2HPO4, pH 7.0, 25°C
23.3
peroxidase activity after 3.17fold purification, in 50 mM potassium phosphate/sodium citrate buffer, pH 4.5, at 80°C
2375
catalase activity after heat treatment of the crude extract, in 50 mM potassium phosphate/sodium citrate buffer, pH 6.0, at 70°C
24.2
-
crude extract, in 50 mM potassium phosphate buffer (pH 7.0), at 30°C
2420
-
specific catalase activity, after 10.7fold purification, in 50 mM Na2HPO4, pH 7.0, 25°C
25.9
-
specific peroxidase activity, using o-dianisidine as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C
250
-
cell extract, at 25°C, pH 6.4
28
-
peroxidase activity using 3,3'-dimethoxybenzidine as substrate, at pH 5.4 and 25°C
2960
-
purified enzyme, at 25°C, pH 6.4
3.4
-
crude extract, catalase activity, in 50 mM potassium phosphate containing 2 M NaCl, pH 6.5, at 25°C
3.8
-
peroxidase activity, using o-dianisidine as substrate, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C
3.9
-
crude extract, peroxidase activity, in 50 mM potassium phosphate containing 2 M NaCl, pH 7.5, at 25°C
3120
-
catalase specific activity, at pH 7.0 and 37°C
316
-
unpurified cytosolic fraction, catalase activity, in 20 mM Tris-HCl buffer (pH 9.0), at 30°C
35
-
catalase activity, mutant enzyme R102K, at pH 7.0 and 37°C
35000
-
after 110.7fold purification, catalase activity, in 20 mM Tris-HCl buffer (pH 9.0), at 30°C
3630
-
catalase specific activity, at pH 7.0 and 37°C
368
-
crude enzyme, catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C
4.3
-
peroxidase activity, using o-dianisidine as substrate, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C
4.4
-
crude extract, in 67 mM phosphate buffer (pH 7.0), at 25°C
4.8
-
peroxidase specific activity, using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 4.5 and 25°C
43
-
crude enzyme, in 100 mM potassium phosphate buffer (pH 6.8), at 30°C
43.2
-
after 12.7fold purification, catalase activity, in 50 mM potassium phosphate containing 2 M NaCl, pH 6.5, at 25°C
4450
-
catalase specific activity, at pH 7.0 and 37°C
4500
-
catalase activity, in phosphate buffer, pH 7.5, at 25°C
4830
-
catalase specific activity, at pH 7.0 and 37°C
5
-
crude extract, catalatic activity, at 20°C and pH 7.5, in the presence of 1.5 M NaC1
5.5
-
peroxidase specific activity, using o-dianisidine as substrate, at pH 4.3 and 25°C
5280
-
catalase specific activity, at pH 7.0 and 37°C
533
-
after 214fold purification, in 50 mM phosphate buffer, pH 7.0, at 25°C
5420
-
catalase specific activity, at pH 7.0 and 37°C
55784
substrate H2O2, pH 7.0, 37°C
560
-
after 13fold purification, in 100 mM potassium phosphate buffer (pH 6.8), at 30°C
6.1
-
substrate o-dianisidine, mutant W341F
6.4
-
peroxidase specific activity, using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 4.3 and 25°C
6.6
-
substrate pyrogallol, wild-type enzyme
63
-
peroxidase activity, mutant enzyme R102C, at pH 7.0 and 37°C
660
-
peroxidase activity, wild type enzyme, at pH 7.0 and 37°C
6922
catalase activity after 2.91fold purification, in 50 mM potassium phosphate/sodium citrate buffer, pH 6.0, at 70°C
7.3
-
substrate pyrogallol, mutant D152W
743
-
peroxidase activity, pH 7.0, 37°C
7512
-
after 44.7fold purification, peroxidase activity, in 50 mM Tris-HCl buffer (pH 8.5), at 30°C
77
-
peroxidase activity using 2,6-dimethoxyphenol as substrate, at pH 5.4 and 25°C
785
-
after 178fold purification, in 67 mM phosphate buffer (pH 7.0), at 25°C
8.3
-
peroxidase specific activity, using o-dianisidine as substrate, at pH 4.3 and 25°C
8.8
-
peroxidase specific activity, using o-dianisidine as substrate, at pH 4.8 and 25°C
818
-
catalase activity, pH 7.0, 37°C
851
-
after 170fold purification, catalatic activity, at 20°C and pH 7.5, in the presence of 1.5 M NaC1
983
-
after 2.67fold purification, catalase activity, in 67 mM phosphate buffer, pH 7.0, at 30°C
99.4
-
specific peroxidase activity, using 4-phenylendiamine as substrate, purified wild type enzyme, in 50 mM Na2HPO4, pH 5.5, 25°C
additional information
-
isoniazid activation activities of wild-type and mutant enzymes in absence or presence of Mn2+, overview
0.6
-
substrate guajacol, wild-type enzyme
0.6
-
peroxidase activity, using guaiacol as substrate, mutant enzyme N153D, in 50 mM phosphate buffer, pH 7.0, and 30°C
0.6
-
peroxidase activity, using guaiacol as substrate, wild type enzyme, in 50 mM phosphate buffer, pH 7.0, and 30°C
0.95
-
catalase activity, mutant enzyme H267Y, at pH 7.0 and 37°C
0.95
-
peroxidase activity, in 50 mM sodium acetate buffer, pH 5.5, at 25°C
1.9
-
catalase activity, mutant enzyme W105F, at pH 7.0 and 37°C
1.9
-
peroxidase activity, using o-dianisidine as substrate, mutant enzyme N153A, in 50 mM phosphate buffer, pH 7.0, and 30°C
10
-
catalase activity, mutant enzyme R102C, at pH 7.0 and 37°C
10
-
peroxidase specific activity, using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 4.8 and 25°C
11
-
peroxidase activity, mutant enzyme H106C, at pH 7.0 and 37°C
11
-
peroxidase specific activity, using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 4.3 and 25°C
12
-
peroxidase specific activity, using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 4.5 and 25°C
12
-
peroxidase activity, mutant enzyme H267Y, at pH 7.0 and 37°C
1900
-
catalase activity, wild type enzyme, at pH 7.0 and 37°C
1900
-
peroxidase activity, mutant enzyme W105F, at pH 7.0 and 37°C
2.4
-
substrate o-dianisidine, mutant P151A
2.4
-
substrate o-dianisidine, mutant P151A
2.5
-
crude extract, in 50 mM phosphate buffer, pH 7.0, at 25°C
2.5
-
substrate guajacol, mutants D152N and D152S
21.5
-
substrate o-dianisidine, mutant D152W
21.5
-
substrate o-dianisidine, mutant D152W
2200
purified recombinant enzyme, catalase-specific activity
2200
-
catalase specific activity, at pH 7.0 and 37°C
3.2
-
peroxidase specific activity, using o-dianisidine as substrate, at pH 4.5 and 25°C
3.2
-
substrate o-dianisidine, wild-type enzyme
3.2
-
substrate o-dianisidine, wild-type enzyme
4.1
-
substrate guajacol, mutant D152W
4.1
-
substrate pyrogallol, mutant P151A
5.3
-
peroxidase specific activity, using o-dianisidine as substrate, at pH 4.5 and 25°C
5.3
-
peroxidase specific activity, using o-dianisidine as substrate, at pH 4.0 and 25°C
5.9
-
catalase activity, mutant enzyme W105L, at pH 7.0 and 37°C
5.9
-
peroxidase specific activity, using 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate, at pH 4.0 and 25°C
7.5
-
peroxidase activity using guaicol as substrate, at pH 5.4 and 25°C
7.5
-
substrate o-dianisidine, mutant D152N
7.5
-
substrate o-dianisidine, mutant D152N
7.6
-
substrate o-dianisidine, mutant D152S
7.6
-
substrate o-dianisidine, mutant D152S
85
-
peroxidase activity, mutant enzyme R102K, at pH 7.0 and 37°C
85
-
peroxidase activity, mutant enzyme R102L, at pH 7.0 and 37°C
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evolution
catalase-peroxidases (KatGs) are a superfamily of reactive oxygen species (ROS)-degrading enzymes believed to have been horizontally acquired by ancient Ascomycota from bacteria. Subsequent gene duplication resulted in two KatG paralogues in ascomycetes: the widely distributed intracellular KatG1 group and the phytopathogen-dominated extracellular KatG2 group
evolution
Thermochaetoides dissita
catalase-peroxidases represent one important subfamily of ancestral antioxidant enzymes originally evolved in bacteria for the protection against various forms of oxidative stress. KatG genes coding for these bifunctional catalase-peroxidases were during their peculiar evolution transferred from Bacteroidetes to the fungal phylum Ascomycota via a horizontal gene transfer event. Identification of the gene for thermostable bifunctional catalase-peroxidases in Chaetomium thermophilum and their molecular evolution, overview. The gene from Chaetomium thermophilum, CthediskatG, resembling its bacterial counterparts has a typical eukaryotic transcription start site and also contains a conserved eukaryotic polyadenylation signal behind its 3' terminus. PolyA tails are detected in corresponding transcripts of katG from two different mRNA libraries of Chaetomium thermophilum thermophilum var. disstum. Although otherwise highly conserved, a unique 60 bp long deletion leading in the translated product with high probability to a modified loop and thus access to the prosthetic heme group is observed in katG genes of only two Chaetomium thermophilum variants. Molecular phylogeny revealing the evolutionary position of fungal thermostable catalase-peroxidases within a robust phylogenetic tree of the whole KatG subfamily, overview. Molecular phylogeny and phylogenetic tree
evolution
-
catalase-peroxidases (KatGs) are a superfamily of reactive oxygen species (ROS)-degrading enzymes believed to have been horizontally acquired by ancient Ascomycota from bacteria. Subsequent gene duplication resulted in two KatG paralogues in ascomycetes: the widely distributed intracellular KatG1 group and the phytopathogen-dominated extracellular KatG2 group
-
evolution
-
catalase-peroxidases (KatGs) are a superfamily of reactive oxygen species (ROS)-degrading enzymes believed to have been horizontally acquired by ancient Ascomycota from bacteria. Subsequent gene duplication resulted in two KatG paralogues in ascomycetes: the widely distributed intracellular KatG1 group and the phytopathogen-dominated extracellular KatG2 group
-
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
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
-
catalase-peroxidase activity is decreased in a Caulobacter crescentus rho::TN5 mutant
malfunction
-
Mycobacterium tuberculosis isolates with defects in the kutG gene encoding a catalase-peroxidase enzyme exhibit resistance to isoniazid
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
Thermochaetoides dissita
detection of a unique deletion in CthediskatG gene leads to a shortened large loop 1 that can have an impact on a modified accessibility to the heme active site from the protein surface and overall stability of this enzyme
malfunction
mutation at position 315 in the katG gene, encoding the catalase-peroxidase (KatG) enzyme, is the major cause of isoniazid (INH) resistance in Mycobacterium tuberculosis. INH resistance is regarded as a major impediment to the tuberculosis (TB) control programme and contributes to the emergence of multidrug-resistant strains. Analysis of the molecular mechanisms of INH resistance, overview. The five KatG mutations, S315T, S315I, S315R, S315N and S315G , affect enzyme activity in different ways, which can be attributed to conformational changes in mutant KatG that result in altered binding affinity to INH and eventually to INH resistance, docking study. Analysis of molecular dynamics (MD) experiments suggest that fluctuations and deviations are higher at the INH binding residues for the mutants than for the wild-type. Reduction in the hydrogen bond network after MD in all KatG enzymes implies an increase in the flexibility and stability of protein structures. Since KatG is a conjugated protein, docking is first done with heme, and then it is further docked with INH
malfunction
mutations of the katG gene in Mycobacterium tuberculosis (T354I, G421S, R463L, and V721M) are a major INH resistance mechanism. The Mycobacterium tuberculosis clinical isolate R2 shows INH resistance at a high level of 0.01 mg/ml
malfunction
mutations that render the enzyme unable to activate the pro-drug lead to isoniazid (INH) resistance. For two INH resistance variants, W107R and T275P, significant structural disorder relating to heme uptake and retention is the likely cause for INH resistance, dynamics of heme binding are determined by cryo-electronmicroscopy of wild-type and mutant enzymes at 2.7-3.7 A resolution, overview
malfunction
resistance to INH is primarily caused by key mutations of the catalase-peroxidase, KatG, and/or promoter mutations in the inhA gene. The most frequently observed mutation involving an amino acid substitution conferring INH resistance (KatG S315T) is believed to restrict a pathway into a catalytic heme center in the active site. Effects of several mutations on the tertiary structure of KatG, focusing on conformational changes in the three channels in the protein structure, molecular dynamics study. The mutations sufficiently restrict one or more of these access channels, thus potentially preventing INH from reaching the catalytic heme, structure-based origins of INH resistance
malfunction
-
mutation at position 315 in the katG gene, encoding the catalase-peroxidase (KatG) enzyme, is the major cause of isoniazid (INH) resistance in Mycobacterium tuberculosis. INH resistance is regarded as a major impediment to the tuberculosis (TB) control programme and contributes to the emergence of multidrug-resistant strains. Analysis of the molecular mechanisms of INH resistance, overview. The five KatG mutations, S315T, S315I, S315R, S315N and S315G , affect enzyme activity in different ways, which can be attributed to conformational changes in mutant KatG that result in altered binding affinity to INH and eventually to INH resistance, docking study. Analysis of molecular dynamics (MD) experiments suggest that fluctuations and deviations are higher at the INH binding residues for the mutants than for the wild-type. Reduction in the hydrogen bond network after MD in all KatG enzymes implies an increase in the flexibility and stability of protein structures. Since KatG is a conjugated protein, docking is first done with heme, and then it is further docked with INH
-
malfunction
-
mutations of the katG gene in Mycobacterium tuberculosis (T354I, G421S, R463L, and V721M) are a major INH resistance mechanism. The Mycobacterium tuberculosis clinical isolate R2 shows INH resistance at a high level of 0.01 mg/ml
-
malfunction
-
mutations that render the enzyme unable to activate the pro-drug lead to isoniazid (INH) resistance. For two INH resistance variants, W107R and T275P, significant structural disorder relating to heme uptake and retention is the likely cause for INH resistance, dynamics of heme binding are determined by cryo-electronmicroscopy of wild-type and mutant enzymes at 2.7-3.7 A resolution, overview
-
malfunction
-
resistance to INH is primarily caused by key mutations of the catalase-peroxidase, KatG, and/or promoter mutations in the inhA gene. The most frequently observed mutation involving an amino acid substitution conferring INH resistance (KatG S315T) is believed to restrict a pathway into a catalytic heme center in the active site. Effects of several mutations on the tertiary structure of KatG, focusing on conformational changes in the three channels in the protein structure, molecular dynamics study. The mutations sufficiently restrict one or more of these access channels, thus potentially preventing INH from reaching the catalytic heme, structure-based origins of INH resistance
-
malfunction
-
mutation at position 315 in the katG gene, encoding the catalase-peroxidase (KatG) enzyme, is the major cause of isoniazid (INH) resistance in Mycobacterium tuberculosis. INH resistance is regarded as a major impediment to the tuberculosis (TB) control programme and contributes to the emergence of multidrug-resistant strains. Analysis of the molecular mechanisms of INH resistance, overview. The five KatG mutations, S315T, S315I, S315R, S315N and S315G , affect enzyme activity in different ways, which can be attributed to conformational changes in mutant KatG that result in altered binding affinity to INH and eventually to INH resistance, docking study. Analysis of molecular dynamics (MD) experiments suggest that fluctuations and deviations are higher at the INH binding residues for the mutants than for the wild-type. Reduction in the hydrogen bond network after MD in all KatG enzymes implies an increase in the flexibility and stability of protein structures. Since KatG is a conjugated protein, docking is first done with heme, and then it is further docked with INH
-
malfunction
-
mutations of the katG gene in Mycobacterium tuberculosis (T354I, G421S, R463L, and V721M) are a major INH resistance mechanism. The Mycobacterium tuberculosis clinical isolate R2 shows INH resistance at a high level of 0.01 mg/ml
-
malfunction
-
mutations that render the enzyme unable to activate the pro-drug lead to isoniazid (INH) resistance. For two INH resistance variants, W107R and T275P, significant structural disorder relating to heme uptake and retention is the likely cause for INH resistance, dynamics of heme binding are determined by cryo-electronmicroscopy of wild-type and mutant enzymes at 2.7-3.7 A resolution, overview
-
malfunction
-
resistance to INH is primarily caused by key mutations of the catalase-peroxidase, KatG, and/or promoter mutations in the inhA gene. The most frequently observed mutation involving an amino acid substitution conferring INH resistance (KatG S315T) is believed to restrict a pathway into a catalytic heme center in the active site. Effects of several mutations on the tertiary structure of KatG, focusing on conformational changes in the three channels in the protein structure, molecular dynamics study. The mutations sufficiently restrict one or more of these access channels, thus potentially preventing INH from reaching the catalytic heme, structure-based origins of INH resistance
-
metabolism
to function as an antitubercular agent, INH requires activation of enzyme catalase-peroxidase encoded by Mycobacterium tuberculosis gene katG. The INH is bound by catalase-peroxidase in its active site, then converted to an isonicotinoyl acyl radical through the use of a diazene intermediate. The isonicotinoyl acyl radical interacts with the NADH electron donor in the active site of the enoyl ACP reductase (InhA) enzyme. The NAD-INH complex is known as a potent inhibitor of InhA, the enzyme that has an important role in the biosynthesis of mycolic acid, the cell wall component in mycobacteria
metabolism
-
to function as an antitubercular agent, INH requires activation of enzyme catalase-peroxidase encoded by Mycobacterium tuberculosis gene katG. The INH is bound by catalase-peroxidase in its active site, then converted to an isonicotinoyl acyl radical through the use of a diazene intermediate. The isonicotinoyl acyl radical interacts with the NADH electron donor in the active site of the enoyl ACP reductase (InhA) enzyme. The NAD-INH complex is known as a potent inhibitor of InhA, the enzyme that has an important role in the biosynthesis of mycolic acid, the cell wall component in mycobacteria
-
metabolism
-
to function as an antitubercular agent, INH requires activation of enzyme catalase-peroxidase encoded by Mycobacterium tuberculosis gene katG. The INH is bound by catalase-peroxidase in its active site, then converted to an isonicotinoyl acyl radical through the use of a diazene intermediate. The isonicotinoyl acyl radical interacts with the NADH electron donor in the active site of the enoyl ACP reductase (InhA) enzyme. The NAD-INH complex is known as a potent inhibitor of InhA, the enzyme that has an important role in the biosynthesis of mycolic acid, the cell wall component in mycobacteria
-
physiological function
-
catalase-peroxidase confers isoniazid (isonicotinic acid hydrazide) sensitivity in Mycobacterium tuberculosis
physiological function
catalase-peroxidase has a protective role against environmental H2O2
physiological function
-
catalase-peroxidase is involved in isoniazid activation
physiological function
-
hemoprotein b-590 plays a role in removal of peroxides generated during respiration
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
-
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
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
expression in Bacillus subtilis improves its resistance to oxidative stress
physiological function
CAT-2 is a fungal catalase-peroxidase (CP). In contrast to catalases, CPs are bi-functional enzymes having both catalase activity and peroxidase activity. CPs are homodimeric heme-oxidoreductases. CAT-2 is induced during asexual spore formation in Neurospora crassa
physiological function
differing roles of isozymes FvCP01 and FvCP02 in protective responses against H2O2-derived oxidative stress, modeling. Genes FvCP01 and FvCP02 may play a minor role in the virulence of Fusarium verticillioides
physiological function
differing roles of isozymes FvCP01 and FvCP02 in protective responses against H2O2-derived oxidative stress, modeling. In addition, KatG2 genes, because they are mostly limited to fungal phytopathogens, have been inferred to play a potential role in host-pathogen interactions. Genes FvCP01 and FvCP02 may play a minor role in the virulence of Fusarium verticillioides
physiological function
effects of AfKatG addition to growth media of lactic acid bacteria and to growth of food pathogenic bacteria, detailed overview. Significant effect of the catalase addition on the cell viability in Lactobacillus casei (12.7fold) and Lactobacillus lactis (5.3fold) is observed after treatment with hydrogen perxadoxide. The effect on Lactobacillus brevis strains is dual, either there is significantly increased the cells ability to grow (up to 9fold) in the 613 strain, or there is no effect at all with strain 615. The addition of catalase has no significant effect on Lactobacillus paracasei strains (616, 622, 623). The most pronounced survival efficacy of catalase was observed in Lactobacillus fermentum 612, where cell survival was 38.6 times greater than in control samples. Addition of catalase-peroxidase to media on the growth of Leuconostoc spp. strains protects the strains from treatment with H2O2. The food opportunistic and obligate pathogens found in the same environment include Staphylococcus epidermidis and Listeria monocytogenes. The addition of AfKatG to the media proves no effect to the growth of bacteria
physiological function
isoniazid (INH) causes the exclusive lethal action to Mycobacterium tuberculosis cells because of the pathogen's own catalase peroxidase (katG) enzyme that converts INH. Catalase peroxidase (katG) binds and catalyzes the conversion of INH to a very reactive radical. The activated INH, the radical, then reacts with nicotinamide adenine dinucleotide (NAD), a substrate of the enoyl acyl carrier protein reductase (InhA) of the pathogen to form an INH-NAD adduct which irreversibly binds to the InhA. InhA is a crucial protein to produce an important cell wall component of the Mycobacterium tuberculosis cells, thus its inhibition through the irreversible binding of the INH-NAD adduct proves fatal to the pathogen
physiological function
isoniazid (INH) is a drug for the treatment of tuberculosis in patients infected with Mycobacterium tuberculosis. The katG enzyme, a catalase-peroxidase, encoded by gene katG in Mycobacterium tuberculosis activates the pro-drug INH
physiological function
isoniazid (INH) is a pro-drug, that becomes activated by the endogenoous catalase-peroxidase enzyme KAtG in Mycobacterium tuberculosis. Once taken up by Mycobacterium tuberculosis, INH serves as a substrate, along with NAD+, for the KatG-catalyzed formation of nitric oxide (NO) and isonicotinyl-NAD Isonicotinyl-NAD binds to the active site of enoyl acyl carrier protein reductase, blocking fatty acid synthesis in general and the synthesis of mycolic acids, which are components of the Mycobacterium tuberculosis cell wall, in particular
physiological function
KatG from Mycobacterium tuberculosis is a catalase-peroxidase that can utilize and degrade hydrogen peroxide (H2O2) either through functioning as a catalase or as a peroxidase. In Mycobacterium tuberculosis, the multifunctional heme enzyme KatG is indispensable for activation of isoniazid (INH), a first-line pro-drug for treatment of tuberculosis. The activated drug species forms an INH-NAD adduct that subsequently triggers anti-tubercular activity
physiological function
-
effects of AfKatG addition to growth media of lactic acid bacteria and to growth of food pathogenic bacteria, detailed overview. Significant effect of the catalase addition on the cell viability in Lactobacillus casei (12.7fold) and Lactobacillus lactis (5.3fold) is observed after treatment with hydrogen perxadoxide. The effect on Lactobacillus brevis strains is dual, either there is significantly increased the cells ability to grow (up to 9fold) in the 613 strain, or there is no effect at all with strain 615. The addition of catalase has no significant effect on Lactobacillus paracasei strains (616, 622, 623). The most pronounced survival efficacy of catalase was observed in Lactobacillus fermentum 612, where cell survival was 38.6 times greater than in control samples. Addition of catalase-peroxidase to media on the growth of Leuconostoc spp. strains protects the strains from treatment with H2O2. The food opportunistic and obligate pathogens found in the same environment include Staphylococcus epidermidis and Listeria monocytogenes. The addition of AfKatG to the media proves no effect to the growth of bacteria
-
physiological function
-
effects of AfKatG addition to growth media of lactic acid bacteria and to growth of food pathogenic bacteria, detailed overview. Significant effect of the catalase addition on the cell viability in Lactobacillus casei (12.7fold) and Lactobacillus lactis (5.3fold) is observed after treatment with hydrogen perxadoxide. The effect on Lactobacillus brevis strains is dual, either there is significantly increased the cells ability to grow (up to 9fold) in the 613 strain, or there is no effect at all with strain 615. The addition of catalase has no significant effect on Lactobacillus paracasei strains (616, 622, 623). The most pronounced survival efficacy of catalase was observed in Lactobacillus fermentum 612, where cell survival was 38.6 times greater than in control samples. Addition of catalase-peroxidase to media on the growth of Leuconostoc spp. strains protects the strains from treatment with H2O2. The food opportunistic and obligate pathogens found in the same environment include Staphylococcus epidermidis and Listeria monocytogenes. The addition of AfKatG to the media proves no effect to the growth of bacteria
-
physiological function
-
catalase-peroxidase is involved in isoniazid activation
-
physiological function
-
CAT-2 is a fungal catalase-peroxidase (CP). In contrast to catalases, CPs are bi-functional enzymes having both catalase activity and peroxidase activity. CPs are homodimeric heme-oxidoreductases. CAT-2 is induced during asexual spore formation in Neurospora crassa
-
physiological function
-
isoniazid (INH) is a drug for the treatment of tuberculosis in patients infected with Mycobacterium tuberculosis. The katG enzyme, a catalase-peroxidase, encoded by gene katG in Mycobacterium tuberculosis activates the pro-drug INH
-
physiological function
-
KatG from Mycobacterium tuberculosis is a catalase-peroxidase that can utilize and degrade hydrogen peroxide (H2O2) either through functioning as a catalase or as a peroxidase. In Mycobacterium tuberculosis, the multifunctional heme enzyme KatG is indispensable for activation of isoniazid (INH), a first-line pro-drug for treatment of tuberculosis. The activated drug species forms an INH-NAD adduct that subsequently triggers anti-tubercular activity
-
physiological function
-
isoniazid (INH) is a pro-drug, that becomes activated by the endogenoous catalase-peroxidase enzyme KAtG in Mycobacterium tuberculosis. Once taken up by Mycobacterium tuberculosis, INH serves as a substrate, along with NAD+, for the KatG-catalyzed formation of nitric oxide (NO) and isonicotinyl-NAD Isonicotinyl-NAD binds to the active site of enoyl acyl carrier protein reductase, blocking fatty acid synthesis in general and the synthesis of mycolic acids, which are components of the Mycobacterium tuberculosis cell wall, in particular
-
physiological function
-
isoniazid (INH) causes the exclusive lethal action to Mycobacterium tuberculosis cells because of the pathogen's own catalase peroxidase (katG) enzyme that converts INH. Catalase peroxidase (katG) binds and catalyzes the conversion of INH to a very reactive radical. The activated INH, the radical, then reacts with nicotinamide adenine dinucleotide (NAD), a substrate of the enoyl acyl carrier protein reductase (InhA) of the pathogen to form an INH-NAD adduct which irreversibly binds to the InhA. InhA is a crucial protein to produce an important cell wall component of the Mycobacterium tuberculosis cells, thus its inhibition through the irreversible binding of the INH-NAD adduct proves fatal to the pathogen
-
physiological function
-
isoniazid (INH) is a drug for the treatment of tuberculosis in patients infected with Mycobacterium tuberculosis. The katG enzyme, a catalase-peroxidase, encoded by gene katG in Mycobacterium tuberculosis activates the pro-drug INH
-
physiological function
-
KatG from Mycobacterium tuberculosis is a catalase-peroxidase that can utilize and degrade hydrogen peroxide (H2O2) either through functioning as a catalase or as a peroxidase. In Mycobacterium tuberculosis, the multifunctional heme enzyme KatG is indispensable for activation of isoniazid (INH), a first-line pro-drug for treatment of tuberculosis. The activated drug species forms an INH-NAD adduct that subsequently triggers anti-tubercular activity
-
physiological function
-
isoniazid (INH) is a pro-drug, that becomes activated by the endogenoous catalase-peroxidase enzyme KAtG in Mycobacterium tuberculosis. Once taken up by Mycobacterium tuberculosis, INH serves as a substrate, along with NAD+, for the KatG-catalyzed formation of nitric oxide (NO) and isonicotinyl-NAD Isonicotinyl-NAD binds to the active site of enoyl acyl carrier protein reductase, blocking fatty acid synthesis in general and the synthesis of mycolic acids, which are components of the Mycobacterium tuberculosis cell wall, in particular
-
physiological function
-
isoniazid (INH) causes the exclusive lethal action to Mycobacterium tuberculosis cells because of the pathogen's own catalase peroxidase (katG) enzyme that converts INH. Catalase peroxidase (katG) binds and catalyzes the conversion of INH to a very reactive radical. The activated INH, the radical, then reacts with nicotinamide adenine dinucleotide (NAD), a substrate of the enoyl acyl carrier protein reductase (InhA) of the pathogen to form an INH-NAD adduct which irreversibly binds to the InhA. InhA is a crucial protein to produce an important cell wall component of the Mycobacterium tuberculosis cells, thus its inhibition through the irreversible binding of the INH-NAD adduct proves fatal to the pathogen
-
physiological function
-
CAT-2 is a fungal catalase-peroxidase (CP). In contrast to catalases, CPs are bi-functional enzymes having both catalase activity and peroxidase activity. CPs are homodimeric heme-oxidoreductases. CAT-2 is induced during asexual spore formation in Neurospora crassa
-
physiological function
-
differing roles of isozymes FvCP01 and FvCP02 in protective responses against H2O2-derived oxidative stress, modeling. Genes FvCP01 and FvCP02 may play a minor role in the virulence of Fusarium verticillioides
-
physiological function
-
differing roles of isozymes FvCP01 and FvCP02 in protective responses against H2O2-derived oxidative stress, modeling. In addition, KatG2 genes, because they are mostly limited to fungal phytopathogens, have been inferred to play a potential role in host-pathogen interactions. Genes FvCP01 and FvCP02 may play a minor role in the virulence of Fusarium verticillioides
-
physiological function
-
CAT-2 is a fungal catalase-peroxidase (CP). In contrast to catalases, CPs are bi-functional enzymes having both catalase activity and peroxidase activity. CPs are homodimeric heme-oxidoreductases. CAT-2 is induced during asexual spore formation in Neurospora crassa
-
physiological function
-
CAT-2 is a fungal catalase-peroxidase (CP). In contrast to catalases, CPs are bi-functional enzymes having both catalase activity and peroxidase activity. CPs are homodimeric heme-oxidoreductases. CAT-2 is induced during asexual spore formation in Neurospora crassa
-
physiological function
-
effects of AfKatG addition to growth media of lactic acid bacteria and to growth of food pathogenic bacteria, detailed overview. Significant effect of the catalase addition on the cell viability in Lactobacillus casei (12.7fold) and Lactobacillus lactis (5.3fold) is observed after treatment with hydrogen perxadoxide. The effect on Lactobacillus brevis strains is dual, either there is significantly increased the cells ability to grow (up to 9fold) in the 613 strain, or there is no effect at all with strain 615. The addition of catalase has no significant effect on Lactobacillus paracasei strains (616, 622, 623). The most pronounced survival efficacy of catalase was observed in Lactobacillus fermentum 612, where cell survival was 38.6 times greater than in control samples. Addition of catalase-peroxidase to media on the growth of Leuconostoc spp. strains protects the strains from treatment with H2O2. The food opportunistic and obligate pathogens found in the same environment include Staphylococcus epidermidis and Listeria monocytogenes. The addition of AfKatG to the media proves no effect to the growth of bacteria
-
physiological function
-
differing roles of isozymes FvCP01 and FvCP02 in protective responses against H2O2-derived oxidative stress, modeling. Genes FvCP01 and FvCP02 may play a minor role in the virulence of Fusarium verticillioides
-
physiological function
-
differing roles of isozymes FvCP01 and FvCP02 in protective responses against H2O2-derived oxidative stress, modeling. In addition, KatG2 genes, because they are mostly limited to fungal phytopathogens, have been inferred to play a potential role in host-pathogen interactions. Genes FvCP01 and FvCP02 may play a minor role in the virulence of Fusarium verticillioides
-
physiological function
-
CAT-2 is a fungal catalase-peroxidase (CP). In contrast to catalases, CPs are bi-functional enzymes having both catalase activity and peroxidase activity. CPs are homodimeric heme-oxidoreductases. CAT-2 is induced during asexual spore formation in Neurospora crassa
-
physiological function
-
hemoprotein b-590 plays a role in removal of peroxides generated during respiration
-
physiological function
-
effects of AfKatG addition to growth media of lactic acid bacteria and to growth of food pathogenic bacteria, detailed overview. Significant effect of the catalase addition on the cell viability in Lactobacillus casei (12.7fold) and Lactobacillus lactis (5.3fold) is observed after treatment with hydrogen perxadoxide. The effect on Lactobacillus brevis strains is dual, either there is significantly increased the cells ability to grow (up to 9fold) in the 613 strain, or there is no effect at all with strain 615. The addition of catalase has no significant effect on Lactobacillus paracasei strains (616, 622, 623). The most pronounced survival efficacy of catalase was observed in Lactobacillus fermentum 612, where cell survival was 38.6 times greater than in control samples. Addition of catalase-peroxidase to media on the growth of Leuconostoc spp. strains protects the strains from treatment with H2O2. The food opportunistic and obligate pathogens found in the same environment include Staphylococcus epidermidis and Listeria monocytogenes. The addition of AfKatG to the media proves no effect to the growth of bacteria
-
physiological function
-
expression in Bacillus subtilis improves its resistance to oxidative stress
-
additional information
CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. A perhydroxy modification of the indole nitrogen of Trp90 is oriented toward the catalytic His91. In contrast to cytochrome c peroxidase and ascorbate peroxidase, the catalase-peroxidase heme propionates are not exposed to the solvent. Together with other Nueorspora crassa enzymes that utilize H2O2 as a substrate, CAT-2 has many tryptophan and proline residues at its surface, probably related to H2O2 selection in water. Potentiometric titration of CAT-2 metalloenzyme sample in phosphate buffer, pH 7.0, at 25°C, CAT-2 is reduced with sodium dithionite and reoxidized with potassium ferricyanide following the changes with a spectrophotometer. 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. Structure comparisons, overview
additional information
-
CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. A perhydroxy modification of the indole nitrogen of Trp90 is oriented toward the catalytic His91. In contrast to cytochrome c peroxidase and ascorbate peroxidase, the catalase-peroxidase heme propionates are not exposed to the solvent. Together with other Nueorspora crassa enzymes that utilize H2O2 as a substrate, CAT-2 has many tryptophan and proline residues at its surface, probably related to H2O2 selection in water. Potentiometric titration of CAT-2 metalloenzyme sample in phosphate buffer, pH 7.0, at 25°C, CAT-2 is reduced with sodium dithionite and reoxidized with potassium ferricyanide following the changes with a spectrophotometer. 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. Structure comparisons, overview
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. The heme is surrounded by six residues which are Arg104, Trp107 and His108 in the distal pocket, and His270, Trp321 and Asp381 in the proximal pocket. In the heme, the Trp107 residue is connected to Tyr229 and Met255 residues to form an adduct triad complex. The adduct triad is likely conserved in many catalase-peroxidase structures and it is involved in the catalase activity [9]. The binding of INH to katG takes place at the edges of the ?-meso heme. In the region, the residues of the distal pocket, i.e., Arg104, Trp107 and His108, are involved in the interactions with INH. The adduct triad complex (Trp107-Tyr229-Met255) is a part of the active site of the catalase-peroxidase enzyme
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. The heme is surrounded by six residues which are Arg104, Trp107 and His108 in the distal pocket, and His270, Trp321 and Asp381 in the proximal pocket. In the heme, the Trp107 residue is connected to Tyr229 and Met255 residues to form an adduct triad complex. The adduct triad is likely conserved in many catalase-peroxidase structures and it is involved in the catalase activity [9]. The binding of INH to katG takes place at the edges of the ?-meso heme. In the region, the residues of the distal pocket, i.e., Arg104, Trp107 and His108, are involved in the interactions with INH. The adduct triad complex (Trp107-Tyr229-Met255) is a part of the active site of the catalase-peroxidase enzyme
additional information
enzyme structure homology modelling using the KtG structure (PDB ID 2CCA) as template, overview
additional information
-
enzyme structure homology modelling using the KtG structure (PDB ID 2CCA) as template, overview
additional information
KatG structure-function analysis, overview
additional information
-
KatG structure-function analysis, overview
additional information
-
CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. A perhydroxy modification of the indole nitrogen of Trp90 is oriented toward the catalytic His91. In contrast to cytochrome c peroxidase and ascorbate peroxidase, the catalase-peroxidase heme propionates are not exposed to the solvent. Together with other Nueorspora crassa enzymes that utilize H2O2 as a substrate, CAT-2 has many tryptophan and proline residues at its surface, probably related to H2O2 selection in water. Potentiometric titration of CAT-2 metalloenzyme sample in phosphate buffer, pH 7.0, at 25°C, CAT-2 is reduced with sodium dithionite and reoxidized with potassium ferricyanide following the changes with a spectrophotometer. 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. Structure comparisons, overview
-
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. The heme is surrounded by six residues which are Arg104, Trp107 and His108 in the distal pocket, and His270, Trp321 and Asp381 in the proximal pocket. In the heme, the Trp107 residue is connected to Tyr229 and Met255 residues to form an adduct triad complex. The adduct triad is likely conserved in many catalase-peroxidase structures and it is involved in the catalase activity [9]. The binding of INH to katG takes place at the edges of the ?-meso heme. In the region, the residues of the distal pocket, i.e., Arg104, Trp107 and His108, are involved in the interactions with INH. The adduct triad complex (Trp107-Tyr229-Met255) is a part of the active site of the catalase-peroxidase enzyme
-
additional information
-
KatG structure-function analysis, overview
-
additional information
-
enzyme structure homology modelling using the KtG structure (PDB ID 2CCA) as template, overview
-
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. The heme is surrounded by six residues which are Arg104, Trp107 and His108 in the distal pocket, and His270, Trp321 and Asp381 in the proximal pocket. In the heme, the Trp107 residue is connected to Tyr229 and Met255 residues to form an adduct triad complex. The adduct triad is likely conserved in many catalase-peroxidase structures and it is involved in the catalase activity [9]. The binding of INH to katG takes place at the edges of the ?-meso heme. In the region, the residues of the distal pocket, i.e., Arg104, Trp107 and His108, are involved in the interactions with INH. The adduct triad complex (Trp107-Tyr229-Met255) is a part of the active site of the catalase-peroxidase enzyme
-
additional information
-
KatG structure-function analysis, overview
-
additional information
-
enzyme structure homology modelling using the KtG structure (PDB ID 2CCA) as template, overview
-
additional information
-
CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. A perhydroxy modification of the indole nitrogen of Trp90 is oriented toward the catalytic His91. In contrast to cytochrome c peroxidase and ascorbate peroxidase, the catalase-peroxidase heme propionates are not exposed to the solvent. Together with other Nueorspora crassa enzymes that utilize H2O2 as a substrate, CAT-2 has many tryptophan and proline residues at its surface, probably related to H2O2 selection in water. Potentiometric titration of CAT-2 metalloenzyme sample in phosphate buffer, pH 7.0, at 25°C, CAT-2 is reduced with sodium dithionite and reoxidized with potassium ferricyanide following the changes with a spectrophotometer. 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. Structure comparisons, overview
-
additional information
-
CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. A perhydroxy modification of the indole nitrogen of Trp90 is oriented toward the catalytic His91. In contrast to cytochrome c peroxidase and ascorbate peroxidase, the catalase-peroxidase heme propionates are not exposed to the solvent. Together with other Nueorspora crassa enzymes that utilize H2O2 as a substrate, CAT-2 has many tryptophan and proline residues at its surface, probably related to H2O2 selection in water. Potentiometric titration of CAT-2 metalloenzyme sample in phosphate buffer, pH 7.0, at 25°C, CAT-2 is reduced with sodium dithionite and reoxidized with potassium ferricyanide following the changes with a spectrophotometer. 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. Structure comparisons, overview
-
additional information
-
CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. A perhydroxy modification of the indole nitrogen of Trp90 is oriented toward the catalytic His91. In contrast to cytochrome c peroxidase and ascorbate peroxidase, the catalase-peroxidase heme propionates are not exposed to the solvent. Together with other Nueorspora crassa enzymes that utilize H2O2 as a substrate, CAT-2 has many tryptophan and proline residues at its surface, probably related to H2O2 selection in water. Potentiometric titration of CAT-2 metalloenzyme sample in phosphate buffer, pH 7.0, at 25°C, CAT-2 is reduced with sodium dithionite and reoxidized with potassium ferricyanide following the changes with a spectrophotometer. 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. Structure comparisons, overview
-
additional information
-
CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. A perhydroxy modification of the indole nitrogen of Trp90 is oriented toward the catalytic His91. In contrast to cytochrome c peroxidase and ascorbate peroxidase, the catalase-peroxidase heme propionates are not exposed to the solvent. Together with other Nueorspora crassa enzymes that utilize H2O2 as a substrate, CAT-2 has many tryptophan and proline residues at its surface, probably related to H2O2 selection in water. Potentiometric titration of CAT-2 metalloenzyme sample in phosphate buffer, pH 7.0, at 25°C, CAT-2 is reduced with sodium dithionite and reoxidized with potassium ferricyanide following the changes with a spectrophotometer. 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. Structure comparisons, overview
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A143Q
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
A143V
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
A290Q
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
A290Y
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
D141A/R108A
-
the reaction with peroxyacetic acid is clearly slower than for mutant D141A
E242Q
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
H112A
the mutant shows 0.02% of wild type catalase activity and 2.3% of wild type peroxidase activity
H112N
the mutant shows 0.05% of wild type catalase activity and 2.3% of wild type peroxidase activity
L209D
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
L236D
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
M264A
the mutant shows 0.15% of wild type catalase activity and 160% of wild type peroxidase activity
M264L
the mutant shows 0.02% of wild type catalase activity and 140% of wild type peroxidase activity
Q233E
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
R108A/W111F
the mutant shows stronglydecreased catalase and peroxidase activities
R108A/W111F/D141A
the mutant shows strongly decreased catalase and peroxidase activities
R426A
the mutant shows 4.3% of wild type catalase activity and 99% of wild type peroxidase activity
R426K
the mutant shows 70% of wild type catalase activity and 97% of wild type peroxidase activity
S324T
the mutant shows 109% of wild type catalase activity and 94% of wild type peroxidase activity
W309F
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
W330F
-
the mutant exhibits slightly reduced catalase- and peroxidase-specific activities but a faster peroxidase turnover rate compared to the wild type enzyme
Y238A
the mutant shows 0.05% of wild type catalase activity and 140% of wild type peroxidase activity
Y238F
the mutant shows 0.15% of wild type catalase activity and 64% of wild type peroxidase activity
A143Q
-
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
-
A143V
-
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
-
D141A
-
the mutant shows reduced catalase and peroxidase activities compared to the wild type enzyme
-
E242Q
-
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
-
W309F
-
the mutant shows unchanged catalase and peroxidase activities compared to the wild type enzyme
-
DELTA200-214
-
mutation eliminates catalase activity, but variant is substantially more active as peroxidase
DELTA209-228
-
variant is substantially more active as peroxidase
DELTAL193-N228
-
mutant lacking Large Loop1, mutation eliminates catalase activity, but variant is substantially more active as peroxidase
H257Y
-
the mutant shows 0.05% of wild type catalase activity and 1.8% of wild type peroxidase activity
H267Y
-
the peroxidatic-to-catalatic ratio of the mutant is increased 36fold, the heme content of the mutant is reduced relative to the wild type enzyme
Y111A
-
the mutation leads to a 5fold reduction in the apparent kcat for catalase activity and an 8fold decrease in the apparent second-order rate constant. For peroxidase activity, the H2O2- and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)-dependent peroxidatic apparent kcat are reduced by 66% and 40%, respectively. Preparations of this variant yield a mixture of high- and low-spin heme states, thus creating the appearance of a transition between wild type (high-spin) and C-terminal lacking (low-spin) KatG
Y226F
-
mutation eliminates catalase activity, but variant is substantially more active as peroxidase
H106Y
-
the peroxidatic-to-catalatic ratio of the mutant is increased 321fold, the heme content of the mutant is reduced relative to the wild type enzyme
-
R102C
-
the peroxidatic-to-catalatic ratio of the mutant is increased 18fold, the heme content of the mutant is reduced relative to the wild type enzyme
-
R102K
-
the peroxidatic-to-catalatic ratio of the mutant is increased 7fold, the heme content of the mutant is reduced relative to the wild type enzyme
-
R102L
-
the peroxidatic-to-catalatic ratio of the mutant is increased 13fold, the heme content of the mutant is reduced relative to the wild type enzyme
-
W105F
-
the peroxidatic-to-catalatic ratio of the mutant is increased 2800fold, the heme content of the mutant is reduced relative to the wild type enzyme
-
A139P
-
site-directed mutagenesis, 76% decreased activity with and activation of isoniazid compared to the wild-type enzyme
A350T
-
the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
D137S
-
in the presence of H2O2, the adduct radical formed from covalently linked side chains of conserved amino acids Met255, Tyr229, and Trp107 is formed normally, but mutant is defective in forming dioxyheme and lacks catalase activity. Mutant exhibits a coincidence between adduct radical persistence and H2O2 consumption as a function of time, and enhanced subunit oligomerization during turnover
D381G
-
the mutant shows no catalase activity
D387G
naturally occuring mutation in KatG which causes INH resistance to a very high level
D735A
-
site-directed mutagenesis, 73% decreased activity with and activation of isoniazid compared to the wild-type enzyme
E291A
-
the mutant shows 89% peroxidase activity and 139% catalase activity compared to the wild type enzyme
E291K
-
the mutant shows 200% peroxidase activity and 79% catalase activity compared to the wild type enzyme
E291K/E292A
-
the mutant shows 222% peroxidase activity and 102% catalase activity compared to the wild type enzyme
E695A
-
only subtle variations in spectroscopic and catalytic properties of the enzyme, substantial decrease in the rate and extent of KatG N-terminal domain reactivation
E695A/Y697A
-
substantial increase in hexa-coordinate low-spin heme and diminished enzyme activity, complete loss of the capacity for the reactivation of the N-terminal domain
G273C
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
G316S
naturally occuring mutation in KatG which does not cause INH resistance
G421S
site-directed mutagenesis, of amino acids alteration in the mutant, substitution of T354I and G421S create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis
H108E
-
isoniazid-resistant clinical mutant
H270Q
-
the mutant shows no catalase activity
H52L
-
isoniazid-resistant clinical mutant
H97R/L200Q
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
I290A
-
the mutant shows 31% peroxidase activity and 93% catalase activity compared to the wild type enzyme
I290A/Q293A
-
the mutant shows 56% peroxidase activity and 64% catalase activity compared to the wild type enzyme
I290V
-
the mutant shows 35% peroxidase activity and 67% catalase activity compared to the wild type enzyme
I290V/Q293V
-
the mutant shows 44% peroxidase activity and 47% catalase activity compared to the wild type enzyme
L148R
-
the mutant shows no catalase activity
L499M
naturally occuring mutation in KatG which does not cause INH resistance
L587P
naturally occuring mutation in KatG which does not cause INH resistance
L619P
-
site-directed mutagenesis, no remaining activity with and activation of isoniazid
L634F
-
site-directed mutagenesis, 36% decreased activity with and activation of isoniazid compared to the wild-type enzyme
L690A/R691A
-
substantial increase in hexa-coordinate low-spin heme and diminished enzyme activity, complete loss of the capacity for the reactivation of the N-terminal domain
L690A/R691A/E695A/Y697A
-
substantial increase in hexa-coordinate low-spin heme and diminished enzyme activity, complete loss of the capacity for the reactivation of the N-terminal domain
M255A
the mutant exhibits severely reduced catalase activity compared to the wild type enzyme
N138S
-
the KatG level of the mutant is 30% of wild type level, the mutant shows a 90% reduction in peroxidase activity
N238S
the catalytic efficiency (Kcat/KM) of the mutant decreases to 41 and 52% for catalase and peroxidase, respectively, compared to the wild type enzyme
Q293A
-
the mutant shows 59% peroxidase activity and 102% catalase activity compared to the wild type enzyme
Q293E
-
the mutant shows 62% peroxidase activity and 80% catalase activity compared to the wild type enzyme
Q293V
-
the mutant shows 25% peroxidase activity and 44% catalase activity compared to the wild type enzyme
R385W
naturally occuring mutation in KatG which causes INH resistance to a very high level
R463G
-
the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
R691A
-
only subtle variations in spectroscopic and catalytic properties of the enzyme, substantial decrease in the rate and extent of KatG N-terminal domain reactivation
S140N
-
the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
S140N/A350T/R463L/R463G/L587M
the mutant katG has catalase-peroxidase activities higher than wild-type katG and exhibits INH sensitivity
T354I
site-directed mutagenesis, of amino acids alteration in the mutant, substitution of T354I and G421S create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis
T354I/G421S/R463L/V721M
naturally occuring mutation. The Mycobacterium tubeculsosis clinical isolate R2 contains four mutations, i.e. C1061T, G1261A, G1388T, G2161A, which correspond to the amino acid substitutions T354I, G421S, R463L, and V721M, respectively, leading to high level isoniazid (INH) resistance. The mutant enzyme showed 86.5% of catalase and 45% of peroxidase activities in comparison to the wild-type enzyme. Substitutions of T354I and G421S in mutant katG R2 create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis. Mutant phenotype and stability, overview
W107F/W321F
-
the mutant shows decreased catalase catalytic efficiency compared to the wild type enzyme
W107R
site-directed mutagenesis of the catalytic residue, the mutant displays only one heme bound per homodimer of protein. The heme is absent from protomer A and displays significant structural disorder in the vicinity of the heme binding site. Several areas surrounding the heme pocket are difficult to model in protomer A, either displaying minimal or fragmented density. The mutant C-terminal domain of both protomers remains similar to wild-type KatG. The mutant's Arg residue results in disruption of the covalently linked catalytic triad. The loop containing Tyr229, which is part of the MYW catalytic triad is disordered in both protomers, presumably as a consequence of the mutation
W321G
-
the KatG level of the mutant is 40% of wild type level, the mutant shows a 70% reduction in peroxidase and catalase activities
Y697A
-
only subtle variations in spectroscopic and catalytic properties of the enzyme, substantial decrease in the rate and extent of KatG N-terminal domain reactivation
A110V
-
naturally occuring mutation in KatG which does not cause INH resistance
-
G421S
-
site-directed mutagenesis, of amino acids alteration in the mutant, substitution of T354I and G421S create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis
-
S140N/A350T/R463L/R463G/L587M
-
the mutant katG has catalase-peroxidase activities higher than wild-type katG and exhibits INH sensitivity
-
S315G
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
S315I
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
S315R
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
T275P
-
site-directed mutagenesis of the residue from the loop close to the heme binding site. The structure of mutant T275P displays significant areas of disorder compared with the wild-type KatG. Several loops surrounding the heme pocket contain little or no density in either protomer A or B. These disordered regions are identical to those in protomer A of the W107R variant. The loop containing the Thr275 residue (residues 274-329) displays no density and therefore cannot be modeled
-
T354I/G421S/R463L/V721M
-
naturally occuring mutation. The Mycobacterium tubeculsosis clinical isolate R2 contains four mutations, i.e. C1061T, G1261A, G1388T, G2161A, which correspond to the amino acid substitutions T354I, G421S, R463L, and V721M, respectively, leading to high level isoniazid (INH) resistance. The mutant enzyme showed 86.5% of catalase and 45% of peroxidase activities in comparison to the wild-type enzyme. Substitutions of T354I and G421S in mutant katG R2 create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis. Mutant phenotype and stability, overview
-
W107R
-
site-directed mutagenesis of the catalytic residue, the mutant displays only one heme bound per homodimer of protein. The heme is absent from protomer A and displays significant structural disorder in the vicinity of the heme binding site. Several areas surrounding the heme pocket are difficult to model in protomer A, either displaying minimal or fragmented density. The mutant C-terminal domain of both protomers remains similar to wild-type KatG. The mutant's Arg residue results in disruption of the covalently linked catalytic triad. The loop containing Tyr229, which is part of the MYW catalytic triad is disordered in both protomers, presumably as a consequence of the mutation
-
A110V
-
naturally occuring mutation in KatG which does not cause INH resistance
-
G421S
-
site-directed mutagenesis, of amino acids alteration in the mutant, substitution of T354I and G421S create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis
-
L148R
-
the mutant shows no catalase activity
-
L587M
-
the mutant has wild type-like strong catalase and peroxidase activities
-
M255A
-
the mutant exhibits severely reduced catalase activity compared to the wild type enzyme
-
N238S
-
the catalytic efficiency (Kcat/KM) of the mutant decreases to 41 and 52% for catalase and peroxidase, respectively, compared to the wild type enzyme
-
R418L
-
the mutant shows 0.6% of wild type catalase activity and 192% of wild type peroxidase activity
-
S140N
-
the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
-
S140N/A350T/R463L/R463G/L587M
-
the mutant katG has catalase-peroxidase activities higher than wild-type katG and exhibits INH sensitivity
-
S315G
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
S315I
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
S315R
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
T354I/G421S/R463L/V721M
-
naturally occuring mutation. The Mycobacterium tubeculsosis clinical isolate R2 contains four mutations, i.e. C1061T, G1261A, G1388T, G2161A, which correspond to the amino acid substitutions T354I, G421S, R463L, and V721M, respectively, leading to high level isoniazid (INH) resistance. The mutant enzyme showed 86.5% of catalase and 45% of peroxidase activities in comparison to the wild-type enzyme. Substitutions of T354I and G421S in mutant katG R2 create significant instability in the adduct triad complex (Trp107-Tyr229-Met255), a part of the active site of the catalase-peroxidase enzyme in the model structure analysis. Mutant phenotype and stability, overview
-
W107F
-
the mutant exhibits severely reduced catalase activity yet normal peroxidase activity and contains more abundant 6-coordinate heme in high spin and low spin forms compared to the wild type enzyme
-
W107R
-
site-directed mutagenesis of the catalytic residue, the mutant displays only one heme bound per homodimer of protein. The heme is absent from protomer A and displays significant structural disorder in the vicinity of the heme binding site. Several areas surrounding the heme pocket are difficult to model in protomer A, either displaying minimal or fragmented density. The mutant C-terminal domain of both protomers remains similar to wild-type KatG. The mutant's Arg residue results in disruption of the covalently linked catalytic triad. The loop containing Tyr229, which is part of the MYW catalytic triad is disordered in both protomers, presumably as a consequence of the mutation
-
W321F
-
the mutant shows 38% of wild type catalase activity and 18% of wild type peroxidase activity
-
C26A/C74A
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
C55A
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
C55A/C74A
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
C74A
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
C26A/C74A
-
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
-
C55A
-
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
-
C55A/C74A
-
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
-
C74A
-
kinetic constants similar to wild-type, decrease in melting temperature due to loss of disulfide bridge
-
D152N
the mutant shows 2.7% of wild type catalase activity and 234% of wild type peroxidase activity
D152S
the mutant shows 5.7% of wild type catalase activity and 237% of wild type peroxidase activity
D152W
the mutant shows 0.6% of wild type catalase activity and 672% of wild type peroxidase activity
D402E
the mutant shows 0.6% of wild type catalase activity and 65% of wild type peroxidase activity
D402N
the mutant shows 0.5% of wild type catalase activity and 56% of wild type peroxidase activity
E253D
the mutant shows 42% of wild type catalase activity and 280% of wild type peroxidase activity
E253Q
the mutant shows 25% of wild type catalase activity and 96% of wild type peroxidase activity
H123E
the mutant shows 0.03% of wild type catalase activity and 13% of wild type peroxidase activity
H123Q
the mutant shows 0.02% of wild type catalase activity and 7.4% of wild type peroxidase activity
H290Q
the mutant shows 0.09% of wild type catalase activity and 5.6% of wild type peroxidase activity
I248F
the mutant shows 12% of wild type catalase activity and 124% of wild type peroxidase activity
M275I
the mutant shows 0.6% of wild type catalase activity and 640% of wild type peroxidase activity
N153A
the mutant shows 6% of wild type catalase activity and 60% of wild type peroxidase activity
N153D
the mutant shows 17% of wild type catalase activity and 130% of wild type peroxidase activity
N251L
the mutant shows 33% of wild type catalase activity and 415% of wild type peroxidase activity
P252A
the mutant shows 110% of wild type catalase activity and 97% of wild type peroxidase activity
R119A
the mutant shows 15% of wild type catalase activity and 12% of wild type peroxidase activity
R119N
the mutant shows 0.5% of wild type catalase activity and 5% of wild type peroxidase activity
R439A
the mutant shows 4.9% of wild type catalase activity and 12% of wild type peroxidase activity
R439N
the mutant shows 3.1% of wild type catalase activity and 100% wild type peroxidase activity
S335T
the mutant shows 99% of wild type catalase activity and 103% of wild type peroxidase activity
W122A
the mutant shows no catalase activity and 100% wild type peroxidase activity
W122F
the mutant shows no catalase activity and 90% of wild type peroxidase activity
W341A
the mutant shows 0.5% of wild type catalase activity and 25% of wild type peroxidase activity
W341F
the mutant shows 42% of wild type catalase activity and 190% of wild type peroxidase activity
Y249F
the mutant shows 0.17% of wild type catalase activity and 121% of wild type peroxidase activity
D152N
-
the mutant shows 2.7% of wild type catalase activity and 234% of wild type peroxidase activity
-
D402E
-
the mutant shows 0.6% of wild type catalase activity and 65% of wild type peroxidase activity
-
D402N
-
the mutant shows 0.5% of wild type catalase activity and 56% of wild type peroxidase activity
-
H290Q
-
the mutant shows 0.09% of wild type catalase activity and 5.6% of wild type peroxidase activity
-
R119A
-
the mutant shows 15% of wild type catalase activity and 12% of wild type peroxidase activity
-
D152N
-
site-directed mutagenesis, 2.7% remaining catalase activity and 2-7times higher peroxidase activity compared to the wild-type enzyme, highly altered pH profile
D152W
-
site-directed mutagenesis, 0.6% remaining catalase activity and 2-7times higher peroxidase activity compared to the wild-type enzyme, highly altered pH profile
E253Q
-
the mutant shows strongly reduced catalase activity
H123E
-
mutant with very low catalase activity
N153A
-
the mutant shows 6% of wild type catalase activity and exhibits an overall peroxidase activity similar with wild type KatG
N153D
-
the mutant shows 16.5% of wild type catalase activity and exhibits an overall peroxidase activity similar with wild type KatG
P151A
-
site-directed mutagenesis, slightly increased catalase activity compared to the wild-type enzyme
R439A
-
mutant with very low catalase activity
D152N
-
site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction, reduced catalase activity and increased peroxidase activity compared to the wild-type enzyme
D152S
-
site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction, reduced catalase activity and increased peroxidase activity compared to the wild-type enzyme
D152W
-
site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction, highly reduced catalase activity and highly increased peroxidase activity compared to the wild-type enzyme
D402E
-
site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, reduced catalase and peroxidase activity compared to the wild-type enzyme
D402N
-
site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, reduced catalase and peroxidase activity compared to the wild-type enzyme
H290Q
-
site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, highly reduced catalase and peroxidase activity compared to the wild-type enzyme
N153A
-
site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction
N153D
-
site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction
P151A
-
site-directed mutagenesis, residue of the heme binding pocket distal side, mutation effect on heme structure and residue interaction, slightly reduced catalase and peroxidase activity compared to the wild-type enzyme
W341A
-
site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, highly reduced catalase and peroxidase activity compared to the wild-type enzyme
W341F
-
site-directed mutagenesis, residue of the heme binding pocket proximal side, mutation effect on heme structure and residue interaction, 50% reduced catalase activity and 50% increased peroxidase activity compared to the wild-type enzyme, binds completely to NaF
D141A
-
mutant with reduced catalase activity
D141A
-
the mutant lacks an aspartate at the entrance to the heme cavity. The reaction with peroxyacetic acid proceeds much faster than for the wild type enzyme
D141A
the mutant shows 1.5% of wild type catalase activity and 132% of wild type peroxidase activity
D141A
the mutant shows decreased catalase and peroxidase activities
D141A
the mutant shows reduced catalase and peroxidase activities compared to the wild type enzyme
D141E
-
mutant with normal catalase activity but with modified kinetics
D141E
the mutant retains normal catalase activity and decreased peroxidase activity
D141E
the mutant shows 80% of wild type catalase activity and 143% of wild type peroxidase activity
D141N
the mutant shows 10% of wild type catalase activity and 123% of wild type peroxidase activity
D141N
the mutant shows decreased catalase and peroxidase activities
R108A
-
mutant with reduced catalase activity
R108A
the mutant shows 31% of wild type catalase activity and 23% of wild type peroxidase activity
R108A
the mutation causes a reduction in catalase activity to 35% of native levels and a decrease in peroxidase activity
R108A
-
the reaction with peroxyacetic acid is clearly slower than for mutant D141A
R108A/D141A
-
activity is 18% lower than wild-type activity
R108A/D141A
the mutant exhibits near normal catalase activity (82% of native) and decreased peroxidase activity
R108K
the mutant shows 8% of wild type catalase activity and 21% of wild type peroxidase activity
R108K
the mutant shows decreased catalase and peroxidase activities
W111F
-
site-directed mutagenesis, active site structure analysis
W111F
the mutant shows 0.05% of wild type catalase activity and 75% of wild type peroxidase activity
H106C
-
the mutant shows 0.01% of wild type catalase activity and 1.7% of wild type peroxidase activity
H106C
-
the peroxidatic-to-catalatic ratio of the mutant is increased 125fold, the heme content of the mutant is reduced relative to the wild type enzyme
H106Y
-
the mutant shows 0.008% of wild type catalase activity and 2.7% of wild type peroxidase activity
H106Y
-
the peroxidatic-to-catalatic ratio of the mutant is increased 321fold, the heme content of the mutant is reduced relative to the wild type enzyme
R102C
-
the mutant shows 0.5% of wild type catalase activity and 10% of wild type peroxidase activity
R102C
-
the peroxidatic-to-catalatic ratio of the mutant is increased 18fold, the heme content of the mutant is reduced relative to the wild type enzyme
R102K
-
the mutant shows 1.8% of wild type catalase activity and 13% of wild type peroxidase activity
R102K
-
the peroxidatic-to-catalatic ratio of the mutant is increased 7fold, the heme content of the mutant is reduced relative to the wild type enzyme
R102L
-
the mutant shows 1% of wild type catalase activity and 13% of wild type peroxidase activity
R102L
-
the peroxidatic-to-catalatic ratio of the mutant is increased 13fold, the heme content of the mutant is reduced relative to the wild type enzyme
W105F
-
the mutant shows 0.1% of wild type catalase activity and 288% of wild type peroxidase activity
W105F
-
the peroxidatic-to-catalatic ratio of the mutant is increased 2800fold, the heme content of the mutant is reduced relative to the wild type enzyme
W105L
-
the mutant shows 0.3% of wild type catalase activity and 197% of wild type peroxidase activity
W105L
-
the peroxidatic-to-catalatic ratio of the mutant is increased 612fold, the heme content of the mutant is reduced relative to the wild type enzyme
A110V
-
site-directed mutagenesis, catalytic efficiency with and activation of isoniazid similar to the wild-type enzyme, reduced Km and increased kcat compared to the wild-type
A110V
naturally occuring mutation in KatG which does not cause INH resistance
H108L
-
the mutant has lost both peroxidatic and catalatic activities
H108L
-
the mutant shows decreased catalase catalytic efficiency compared to the wild type enzyme
H108Q
the mutant shows 0.03% of wild type catalase activity and 47% of wild type peroxidase activity
H108Q
-
the mutant shows no catalase activity
L587M
-
the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
L587M
-
the mutant has wild type-like strong catalase and peroxidase activities
R104L
-
mutant with reduced enzymatic activity
R104L
the mutant shows 0.06% of wild type catalase activity and 200% of wild type peroxidase activity
R418L
the mutant shows 0.6% of wild type catalase activity and 192% of wild type peroxidase activity
R418L
-
mutant is catalase deficient but exhibits normal formation of the adduct radical formed from covalently linked side chains of conserved amino acids Met255, Tyr229, and Trp107 and dioxyheme. Mutant exhibits a coincidence between adduct radical persistence and H2O2 consumption as a function of time, and enhanced subunit oligomerization during turnover
R463L
-
isoniazid-resistant clinical mutant, which has retained peroxidatic and catalatic activities
R463L
-
the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
R463L
-
the mutant has wild type-like strong catalase and peroxidase activities
R463L
-
the mutation is found in isoniazid-resistant strains and does not lead to a loss of peroxidase or catalase activity
R463L
naturally occuring mutation in KatG which does not cause INH resistance
S315G
-
the mutation leads to isoniazid resistance
S315G
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
S315G
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
S315I
-
the mutation leads to isoniazid resistance
S315I
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
S315I
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
S315N
-
site-directed mutagenesis, no remaining activity with and activation of isoniazid
S315N
-
the mutation leads to isoniazid resistance
S315N
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
S315N
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
S315R
-
the mutation leads to isoniazid resistance
S315R
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
S315R
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
S315T
-
most prevalent isonazid-resistant mutant, determination of Fe2+-binding/interaction structure, minimal alterations compared to the wild-type enzyme, mutant enzyme retains all active site properties for proper catalytic function
S315T
-
isoniazid-resistant, mutant catalase-peroxidase retains all active site properties for proper catalytic function
S315T
-
isoniazid resistant mutant
S315T
-
the KatG level of the mutant is 90% of wild type level, the mutant shows 60% peroxidase and 40% catalase activity compared to the wild type enzyme
S315T
-
the mutant has weak catalase and barely detectable peroxidase activities
S315T
-
the mutant is a competent catalase-peroxidase with reduced activity toward isoniazid. The catalase activity is reduced 6fold and the peroxidase activity is decreased less than 2fold compared with the activities for the wild type enzyme
S315T
the mutant shows 52% of wild type catalase activity and 50% of wild type peroxidase activity
S315T
-
the mutation leads to isoniazid resistance
S315T
naturally occuring mutant, the mutant katG retains peroxidase and catalase activity as 60% and 40%, respectively, from wild-type activity, the mutant develops INH inhibitory levels to the transformant BCG corresponding to the decline of its protein activity
S315T
naturally occuring mutation in KatG which restricts a pathway into a catalytic heme center in the active site causing INH resistance
S315T
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
S315T
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
T275P
-
the mutant has very low catalase activity
T275P
-
the mutant shows no catalase activity
T275P
site-directed mutagenesis of the residue from the loop close to the heme binding site. The structure of mutant T275P displays significant areas of disorder compared with the wild-type KatG. Several loops surrounding the heme pocket contain little or no density in either protomer A or B. These disordered regions are identical to those in protomer A of the W107R variant. The loop containing the Thr275 residue (residues 274-329) displays no density and therefore cannot be modeled
W107F
the mutant exhibits severely reduced catalase activity yet normal peroxidase activity and contains more abundant 6-coordinate heme in high spin and low spin forms compared to the wild type enzyme
W107F
-
the mutant shows decreased catalase catalytic efficiency compared to the wild type enzyme
W321F
the mutant shows 38% of wild type catalase activity and 18% of wild type peroxidase activity
W321F
-
the mutant shows decreased catalase catalytic efficiency compared to the wild type enzyme
Y229F
the mutant exhibits severely reduced catalase activity compared to the wild type enzyme
Y229F
the mutant shows 0.002% of wild type catalase activity and 1360% of wild type peroxidase activity
S315N
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
S315N
-
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
-
S315T
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
S315T
-
naturally occuring mutant, the mutant katG retains peroxidase and catalase activity as 60% and 40%, respectively, from wild-type activity, the mutant develops INH inhibitory levels to the transformant BCG corresponding to the decline of its protein activity
-
S315T
-
naturally occuring mutation in KatG which restricts a pathway into a catalytic heme center in the active site causing INH resistance
-
S315T
-
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
-
R104L
-
mutant with reduced enzymatic activity
-
R104L
-
the mutant shows 0.06% of wild type catalase activity and 200% of wild type peroxidase activity
-
R463L
-
the mutant has wild type-like strong catalase and peroxidase activities
-
R463L
-
the catalase and peroxidase activities and isoniazid sensitivity is similar to the wild type enzyme
-
S315N
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
S315N
-
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
-
S315T
-
the mutant has weak catalase and barely detectable peroxidase activities
-
S315T
-
the KatG level of the mutant is 90% of wild type level, the mutant shows 60% peroxidase and 40% catalase activity compared to the wild type enzyme
-
S315T
-
the mutant shows 52% of wild type catalase activity and 50% of wild type peroxidase activity
-
S315T
-
site-directed mutagenesis, modelling and docking and interaction analysis with isoniazid, comparison to wild-type
-
S315T
-
naturally occuring mutant, the mutant katG retains peroxidase and catalase activity as 60% and 40%, respectively, from wild-type activity, the mutant develops INH inhibitory levels to the transformant BCG corresponding to the decline of its protein activity
-
S315T
-
naturally occuring mutation in KatG which restricts a pathway into a catalytic heme center in the active site causing INH resistance
-
S315T
-
site-directed mutagenesis near the heme center, the mutation causes a decrease in the the volume of the catalytic center
-
T275P
-
the mutant has very low catalase activity
-
T275P
-
site-directed mutagenesis of the residue from the loop close to the heme binding site. The structure of mutant T275P displays significant areas of disorder compared with the wild-type KatG. Several loops surrounding the heme pocket contain little or no density in either protomer A or B. These disordered regions are identical to those in protomer A of the W107R variant. The loop containing the Thr275 residue (residues 274-329) displays no density and therefore cannot be modeled
-
Y229F
-
the mutant exhibits severely reduced catalase activity compared to the wild type enzyme
-
Y229F
-
the mutant shows 0.002% of wild type catalase activity and 1360% of wild type peroxidase activity
-
R461A
the mutation slightly increases the thermal stability but does not alter the active site architecture or the kinetics of cyanide binding. However, the variant loses the wild type-typical optimum of catalase activity at pH 5.3 but exhibits a broad plateau between pH 4.5 and 7.5
R461A
-
the mutation slightly increases the thermal stability but does not alter the active site architecture or the kinetics of cyanide binding. However, the variant loses the wild type-typical optimum of catalase activity at pH 5.3 but exhibits a broad plateau between pH 4.5 and 7.5
-
S308T
the mutant shows strongly reduced activity compared to the wild type enzyme
S308T
-
the mutant shows strongly reduced activity compared to the wild type enzyme
-
D152S
-
site-directed mutagenesis, 5.7% remaining catalase activity and 2-7times higher peroxidase activity compared to the wild-type enzyme, highly altered pH profile
D152S
-
mutant with very low catalase activity
D152S
-
the mutant shows strongly reduced catalase activity
W122F
-
inactive
W122F
-
mutant without catalase activity
Y249F
-
the bimolecular rate constants of dioxygen binding to ferrous Y249F is 1.3fold higher than the wild-type value. The dissociation constants of the ferrous-dioxygen is 1.5fold higher than wild-type value
Y249F
-
mutant with very low catalase activity
additional information
-
the heme environment of mutant KatGDELTAFG (lacking its FG insertion) is highly similar to wild type KatG, but the variant retains only 0.2% catalase activity. In contrast, the deletion reduces peroxidase activity by only 50%
additional information
generation of single and double gene deletion mutants of genes FvCP01 and FvCP02 encoding isozyme in KatG1 and KatG2, respectively, in the maize pathogen Fusarium verticillioides. Both mutants DELTAFvCP01 and DELTAFvCP02 are more sensitive to H2O2 than the wild-type in vitro, although their sensitivity differ depending on the type of inoculum. Inoculations using mycelial agar plugs demonstrate an additive effect of the mutants, with the DELTAFvCP01/DELTAFvCP02 double deletion being the most sensitive to H2O2. In general, conidia are much more sensitive than agar plugs to H2O2, and conidial inoculations indicate that FvCP01 confers more H2O2 tolerance than FvCP02. Phenotypes, detailed overview
additional information
generation of single and double gene deletion mutants of genes FvCP01 and FvCP02 encoding isozyme in KatG1 and KatG2, respectively, in the maize pathogen Fusarium verticillioides. Both mutants DELTAFvCP01 and DELTAFvCP02 are more sensitive to H2O2 than the wild-type in vitro, although their sensitivity differ depending on the type of inoculum. Inoculations using mycelial agar plugs demonstrate an additive effect of the mutants, with the DELTAFvCP01/DELTAFvCP02 double deletion being the most sensitive to H2O2. In general, conidia are much more sensitive than agar plugs to H2O2, and conidial inoculations indicate that FvCP01 confers more H2O2 tolerance than FvCP02. Phenotypes, detailed overview
additional information
-
generation of single and double gene deletion mutants of genes FvCP01 and FvCP02 encoding isozyme in KatG1 and KatG2, respectively, in the maize pathogen Fusarium verticillioides. Both mutants DELTAFvCP01 and DELTAFvCP02 are more sensitive to H2O2 than the wild-type in vitro, although their sensitivity differ depending on the type of inoculum. Inoculations using mycelial agar plugs demonstrate an additive effect of the mutants, with the DELTAFvCP01/DELTAFvCP02 double deletion being the most sensitive to H2O2. In general, conidia are much more sensitive than agar plugs to H2O2, and conidial inoculations indicate that FvCP01 confers more H2O2 tolerance than FvCP02. Phenotypes, detailed overview
additional information
-
generation of single and double gene deletion mutants of genes FvCP01 and FvCP02 encoding isozyme in KatG1 and KatG2, respectively, in the maize pathogen Fusarium verticillioides. Both mutants DELTAFvCP01 and DELTAFvCP02 are more sensitive to H2O2 than the wild-type in vitro, although their sensitivity differ depending on the type of inoculum. Inoculations using mycelial agar plugs demonstrate an additive effect of the mutants, with the DELTAFvCP01/DELTAFvCP02 double deletion being the most sensitive to H2O2. In general, conidia are much more sensitive than agar plugs to H2O2, and conidial inoculations indicate that FvCP01 confers more H2O2 tolerance than FvCP02. Phenotypes, detailed overview
-
additional information
-
generation of single and double gene deletion mutants of genes FvCP01 and FvCP02 encoding isozyme in KatG1 and KatG2, respectively, in the maize pathogen Fusarium verticillioides. Both mutants DELTAFvCP01 and DELTAFvCP02 are more sensitive to H2O2 than the wild-type in vitro, although their sensitivity differ depending on the type of inoculum. Inoculations using mycelial agar plugs demonstrate an additive effect of the mutants, with the DELTAFvCP01/DELTAFvCP02 double deletion being the most sensitive to H2O2. In general, conidia are much more sensitive than agar plugs to H2O2, and conidial inoculations indicate that FvCP01 confers more H2O2 tolerance than FvCP02. Phenotypes, detailed overview
-
additional information
dynamic simulations of enzyme mutants bound to isoniazid (INH)
additional information
-
dynamic simulations of enzyme mutants bound to isoniazid (INH)
additional information
enzyme mutants' tertiary structures analysis, detailed overview
additional information
-
enzyme mutants' tertiary structures analysis, detailed overview
additional information
-
dynamic simulations of enzyme mutants bound to isoniazid (INH)
-
additional information
-
enzyme mutants' tertiary structures analysis, detailed overview
-
additional information
-
dynamic simulations of enzyme mutants bound to isoniazid (INH)
-
additional information
-
enzyme mutants' tertiary structures analysis, detailed overview
-
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