1.11.1.21: catalase-peroxidase
This is an abbreviated version!
For detailed information about catalase-peroxidase, go to the full flat file.
Word Map on EC 1.11.1.21
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1.11.1.21
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1.11.1.7
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katgs
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mycobacterium
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tuberculosis
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isoniazid
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dismutase
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ascorbate
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heme
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horseradish
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peroxidases
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guaiacol
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ferric
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myeloperoxidase
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catalases
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1.6.4.2
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lignification
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monofunctional
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lactoperoxidase
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peroxidatic
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isonicotinic
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high-spin
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inh-resistant
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isoniazid-resistant
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o-dianisidine
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pseudomallei
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antituberculosis
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soret
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catalatic
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pro-drug
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antitubercular
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medicine
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mycolic
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isoperoxidase
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monodehydroascorbate
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1.8.5.1
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low-spin
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1.10.3.1
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pyrogallol
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3-amino-1,2,4-triazole
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coniferyl
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1.14.18.1
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4.3.1.5
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synthesis
- 1.11.1.21
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1.11.1.7
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katgs
- mycobacterium
- tuberculosis
- isoniazid
- dismutase
- ascorbate
- heme
- horseradish
- peroxidases
- guaiacol
-
ferric
- myeloperoxidase
- catalases
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1.6.4.2
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lignification
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monofunctional
- lactoperoxidase
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peroxidatic
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isonicotinic
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high-spin
-
inh-resistant
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isoniazid-resistant
- o-dianisidine
- pseudomallei
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antituberculosis
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soret
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catalatic
-
pro-drug
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antitubercular
- medicine
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mycolic
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isoperoxidase
- monodehydroascorbate
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1.8.5.1
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low-spin
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1.10.3.1
- pyrogallol
- 3-amino-1,2,4-triazole
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coniferyl
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1.14.18.1
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4.3.1.5
- synthesis
Reaction
Synonyms
AfKatG, BW16_04845, CAT, CAT-2, catalase -peroxidase KatG, catalase peroxidase, catalase-peroxidase, catalase/peroxidase, CP 2, CP01, CP02, CPX, CthediskatG, EC 1.11.1.7, FeSOD A, FvCP01, FvCP02, FVEG_10866, FVEG_12888, HCP, hemoprotein b-590, HPI, hydroperoxidase I, KatG, KatG1, KatG2, KatP, katX2, KpCP, PCP, Rv1908c
ECTree
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General Information
General Information on EC 1.11.1.21 - catalase-peroxidase
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evolution
malfunction
metabolism
physiological function
additional information
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
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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
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evolution
Fusarium verticillioides FGSC 7600
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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
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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
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catalase-peroxidase activity is decreased in a Caulobacter crescentus rho::TN5 mutant
malfunction
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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
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malfunction
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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
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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
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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
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metabolism
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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
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catalase-peroxidase confers isoniazid (isonicotinic acid hydrazide) sensitivity in Mycobacterium tuberculosis
physiological function
catalase-peroxidase has a protective role against environmental H2O2
physiological function
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catalase-peroxidase is involved in isoniazid activation
physiological function
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hemoprotein b-590 plays a role in removal of peroxides generated during respiration
physiological function
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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
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oxidation of isoniazid by KatG in the presence of InhA leads to the inactivation of InhA
physiological function
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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
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
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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
Fusarium verticillioides FGSC 7600
-
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
Fusarium verticillioides FGSC 7600
-
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
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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
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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
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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
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enzyme structure homology modelling using the KtG structure (PDB ID 2CCA) as template, overview
additional information
KatG structure-function analysis, overview
additional information
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KatG structure-function analysis, overview
additional information
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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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additional information
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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
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additional information
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KatG structure-function analysis, overview
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additional information
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enzyme structure homology modelling using the KtG structure (PDB ID 2CCA) as template, overview
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additional information
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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
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additional information
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KatG structure-function analysis, overview
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additional information
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enzyme structure homology modelling using the KtG structure (PDB ID 2CCA) as template, overview
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additional information
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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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additional information
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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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additional information
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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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additional information
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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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