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catalase/dental caries
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Influence of main channel structure on H(2)O(2) access to the heme cavity of catalase KatE of Escherichia coli.
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The main channel for H(2)O(2) access to the heme cavity in large subunit catalases is twice as long as in small subunit catalases and is divided into two distinct parts. Like small subunit catalases, the 15Å of the channel adjacent to the heme has a predominantly hydrophobic surface with only weak
Effect of distal cavity mutations on the formation of compound I in catalase-peroxidases.
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Catalase-peroxidases have a predominant catalase activity but differ from monofunctional catalases in exhibiting a substantial peroxidase activity and in having different residues in the heme cavity. We present a kinetic study of the formation of the key intermediate compound I by probing the role
New insights into the heme cavity structure of catalase-peroxidase: a spectroscopic approach to the recombinant synechocystis enzyme and selected distal cavity mutants.
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Catalase-peroxidases (KatGs) are heme peroxidases with homology to yeast cytochrome cperoxidase (CCP) and plant ascorbate peroxidases (APXs). KatGs exhibit a peroxidase activity of broad specificity and a high catalase activity, which strongly depends on the presence of a distal Trp as part of the
Engineering the proximal heme cavity of catalase-peroxidase.
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Catalase-peroxidases (KatGs) are prokaryotic heme peroxidases with homology to yeast cytochrome c peroxidase (CCP) and plant ascorbate peroxidases (APXs). KatGs, CCP and APXs contain identical amino acid triads in the heme pocket (distal Arg/Trp/His and proximal His/Trp/Asp), but differ dramatically
[Catalase activity of fluids isolated from the pleural cavity after surgical intervention].
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Wild-type catalase peroxidase vs G279D mutant type: Molecular basis of Isoniazid drug resistance in Mycobacterium tuberculosis.
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Mycobacterium tuberculosis katG gene is responsible for production of an enzyme catalase peroxidase that peroxidises and activates the prodrug Isoniazid (INH), a first-line antitubercular agent. INH interacts with catalase peroxidase enzyme within its heme pocket and gets converted to an active
Streptococcus ursoris sp. nov., isolated from the oral cavities of bears.
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Three Gram-positive, catalase-negative, coccus-shaped organisms were isolated from the oral cavities of bears. The isolates were tentatively identified as a streptococcal species based on the results of biochemical tests. Comparative 16S rRNA gene sequencing studies confirmed that the organisms were
Transgenic mitochondrial superoxide dismutase and mitochondrially targeted catalase prevent antiretroviral-induced oxidative stress and cardiomyopathy.
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Transgenic mice (TG) were used to define mitochondrial oxidative stress and cardiomyopathy (CM) induced by zidovudine (AZT), an antiretroviral used to treat HIV/AIDS. Genetically engineered mice either depleted or overexpressed mitochondrial superoxide dismutase (SOD2(+/-) KOs and SOD2-OX,
Spectroscopic and Molecular Docking Study on Specific Binding and Inhibition of Isoniazid to Human Serum Albumin and Catalase.
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Isonicotinic acid hydrazide (Isoniazid, INH) is one of the most commonly used first-line anti-tuberculosis drugs, which has been reported that the high concentration of INH in human body can lead to epilepsy, liver function failure, and even death. Therefore, studying the potential binding effects
Eukaryotic Catalase-Peroxidase: The Role of the Trp-Tyr-Met Adduct in Protein Stability, Substrate Accessibility, and Catalysis of Hydrogen Peroxide Dismutation.
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Recently, it was demonstrated that bifunctional catalase-peroxidases (KatGs) are found not only in archaea and bacteria but also in lower eukaryotes. Structural studies and preliminary biochemical data of the secreted KatG from the rice pathogen Magnaporthe grisea (MagKatG2) suggested both similar
Inhibition of adhesion and proliferation of peritoneally disseminated tumor cells by pegylated catalase.
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Hydrogen peroxide may aggravate the peritoneal dissemination of tumor cells by activating the expression of a variety of genes. In this study, we used pegylated catalase (PEG-catalase) to examine whether prolonged retention of catalase activity within the peritoneal cavity is effective in inhibiting
The effect of intraperitoneal catalase on prevention of peritoneal adhesion formation in rats.
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The objective of our study was to investigate the efficacy of catalase in preventing the formation of peritoneal adhesions induced by cecal serosal laceration in rats. A research study was set up using a randomized complete block design. This study was performed in the Experimental Surgical Research
Studies on rat liver catalase. XI. Site of synthesis and segregation by stripped ER membranes.
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We reinvestigated the site of synthesis of rat liver catalase, and it has been reconfirmed that catalase is synthesized not only by free polysomes but also by membrane-bound polysomes. Considerable amounts of nascent catalase on rough microsomes were released from the membrane into the medium upon
Structure of catalase HPII from Escherichia coli at 1.9 A resolution.
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Catalase HPII from Escherichia coli, a homotetramer of subunits with 753 residues, is the largest known catalase. The structure of native HPII has been refined at 1.9 A resolution using X-ray synchrotron data collected from crystals flash-cooled with liquid nitrogen. The crystallographic agreement
Rapid immunoelectrophoretic assay for detection of serum antibodies to Aspergillus fumigatus catalase in patients with pulmonary aspergillosis.
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A rapid immunoelectrophoretic assay was developed to detect antibodies to Aspergillus fumigatus catalase. The method's diagnostic sensitivity for pulmonary aspergillosis was 88% (72-97%, 95% confidence limits) in 33 patients presenting with either aspergilloma or Aspergillus lung infiltrate. The
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