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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A catalase-negative mutant of the yeast Hansenula polymorpha consumed methanol in the presence of glucose when the organism was grown in carbon-limited chemostat cultures. The organism was apparently able to decompose the H(2)O(2) generated in the oxidation of methanol by alcohol oxidase. Not only H(2)O(2) generated intracellularly but also H(2)O(2) added extracellularly was effectively destroyed by the catalase-negative mutant. From the rate of H(2)O(2) consumption during growth in chemostat cultures on mixtures of glucose and H(2)O(2), it appeared that the mutant was capable of decomposing H(2)O(2) at a rate as high as 8 mmol . g of cells . h. Glutathione peroxidase (EC 1.11.1.9) was absent under all growth conditions. However, cytochrome c peroxidase (CCP; EC 1.11.1.5) increased to very high levels in cells which decomposed H(2)O(2). When wild-type H. polymorpha was grown on mixtures of glucose and methanol, the CCP level was independent of the rate of methanol utilization, whereas the level of catalase increased with increasing amounts of methanol in the substrate feed. Also, the wild type decomposed H(2)O(2) at a high rate when cells were grown on mixtures of glucose and H(2)O(2). In this case, an increase of both CCP and catalase was observed. When Saccharomyces cerevisiae was grown on mixtures of glucose and H(2)O(2), the level of catalase remained low, but CCP increased with increasing rates of H(2)O(2) utilization. From these observations and an analysis of cell yields under the various conditions, two conclusions can be drawn. (i) CCP is a key enzyme of H(2)O(2) detoxification in yeasts. (ii) Catalase can effectively compete with mitochondrial CCP for hydrogen peroxide only if hydrogen peroxide is generated at the site where catalase is located, namely in the peroxisomes.
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PMID:Hydrogen peroxide metabolism in yeasts. 1634 19

Catalase (EC 1.11.1.6) is an enzyme which is present mainly in the peroxisomes of mammalian cells. It is a tetrameric enzyme consisting of four identical, tetrahedrally arranged subunits of 60 kDa, each containing in its active center a heme group and NADPH. Catalase has two enzymatic activities depending on the concentration of H2O2. If the concentration of H2O2 is high, catalase acts catalytically, i.e. removes H2O2 by forming H2O and O2 (catalatic reaction). However, at a low concentration of H2O2 and in the presence of a suitable hydrogen donor, e.g. ethanol, methanol, phenol, and others, catalase acts peroxidically, removing H2O2, but oxidizing its substrate (peroxidatic reaction). The review article presents current knowledge about the structure, properties, and functions of catalase in living organisms.
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PMID:[Catalase: structure, properties, functions]. 1661 87

Effect of six organic solvents-methanol, ethanol, propanol, dimethyl sulphoxide (DMSO), N,N-dimethyl formamide (DMF), and glycerol on the conformation and interaction of catalase and anticatalase antibodies were studied with the aim of identifying the solvents in which antigen-antibody interactions are strong. The antigen binding activity of the antibodies in the various organic solvents increased in the following order: ethanol<methanol<no organic solvent<propanol<DMSO<DMF<glycerol. The structure of both the antibody and the antigen molecule was affected significantly in 40% concentration of the organic solvents used in this study. Catalase activity was inhibited in DMSO. However, the enzyme was activated in DMF upto about 50% of its concentration.
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PMID:Effect of organic solvents on the conformation and interaction of catalase and anticatalase antibodies. 1667 2

A strictly anaerobic, mesophilic, sulfate-reducing bacterial strain (MSL86(T)) isolated from an estuarine sediment in the Sea of Japan (around the Japanese islands) was characterized phenotypically and phylogenetically. The cells were found to be Gram-negative, motile, non-spore-forming rods. Catalase was not detected. The optimum NaCl concentration for growth was 1.0 % (w/v) and the optimum temperature was 35 degrees C. Strain MSL86(T) was slightly alkaliphilic, with optimum growth at pH 7.5-7.6. Organic electron donors were incompletely oxidized to (mainly) acetate. Strain MSL86(T) utilized formate, pyruvate, lactate, fumarate, ethanol, propanol, butanol and glycerol as electron donors for sulfate reduction and did not use acetate, propionate, butyrate, succinate, malate, methanol, glycine, alanine, serine, aspartate, glutamate or H(2). Sulfite, thiosulfate and fumarate were used as electron acceptors with lactate as an electron donor. Without electron acceptors, the strain fermented pyruvate and fumarate. The genomic DNA G+C content was 54.4 mol%. Menaquinone MK-8(H(4)) was the major respiratory quinone. The major cellular fatty acids were C(16 : 0), C(16 : 1)omega7, C(16 : 1)omega5 and C(17 : 1)omega6. A phylogenetic analysis based on the 16S rRNA gene sequence placed the strain in the class Deltaproteobacteria. The recognized bacterium most closely related to strain MSL86(T) was [Desulfobacterium] catecholicum DSM 3882(T) (sequence similarity 94.4 %), and the next most closely related recognized species were Desulfotalea psychrophila (94.2 % sequence similarity with the type strain) and Desulfotalea arctica (93.7 %). As the physiological and chemotaxonomic characteristics of MSL86(T) were distinctly different from those of any related species, a novel genus and species Desulfopila aestuarii gen. nov., sp. nov. are proposed to accommodate the strain. The type strain of Desulfopila aestuarii is MSL86(T) (=JCM 14042(T)=DSM 18488(T)).
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PMID:Desulfopila aestuarii gen. nov., sp. nov., a Gram-negative, rod-like, sulfate-reducing bacterium isolated from an estuarine sediment in Japan. 1732 77

Two strictly anaerobic, mesophilic, sulfate-reducing bacterial strains, Pro1(T) and Pro16, were isolated from an estuarine sediment in the Sea of Japan of the Japanese islands and were characterized by phenotypic and phylogenetic methods. Strains Pro1(T) and Pro16 had almost the same physiological and chemotaxonomic characteristics. Cells of both strains were Gram-negative, motile, non-spore-forming rods. Catalase activity was not detected. The optimum NaCl concentration for growth was 3.0 % (w/v). The optimum temperature for growth was 35 degrees C and the optimum pH was 6.7. Both strains used formate, propionate, pyruvate, lactate, fumarate, malate, ethanol, propanol, butanol, glycerol, alanine, glucose, fructose and H(2) as electron donors for sulfate reduction and did not use acetate, butyrate, succinate, methanol, glycine, serine, aspartate, glutamate, cellobiose or sucrose. Organic electron donors were incompletely oxidized mainly to acetate. Both strains also used thiosulfate as an electron acceptor. Without electron acceptors, both strains fermented pyruvate and lactate. The genomic DNA G+C contents of strains Pro1(T) and Pro16 were 48.6 and 46.0 mol%, respectively. The major respiratory quinone of both strains was menaquinone MK-5(H(2)). Major cellular fatty acids of both strains were C(15 : 0), C(16 : 0), C(17 : 1)omega6 and C(18 : 1)omega7. Phylogenetic analysis based on 16S rRNA gene sequences placed both strains in the class Deltaproteobacteria. The closest recognized relative of strains Pro1(T) and Pro16 was Desulfobulbus mediterraneus with sequence similarities of 95.2 and 94.8 %, respectively. Based on phylogenetic, physiological and chemotaxonomic characteristics, strains Pro1(T) and Pro16 represent a novel species of the genus Desulfobulbus, for which the name Desulfobulbus japonicus is proposed. The type strain is Pro1(T)(=JCM 14043(T)=DSM 18378(T)) and strain Pro16 (=JCM 14044=DSM 18379) is a reference strain.
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PMID:Desulfobulbus japonicus sp. nov., a novel Gram-negative propionate-oxidizing, sulfate-reducing bacterium isolated from an estuarine sediment in Japan. 1739 18

A strictly anaerobic, mesophilic, sulfate-reducing bacterial strain, designated MSL71T, was isolated from an estuarine sediment from the Sea of Japan bordering the Japanese islands and was characterized phenotypically and phylogenetically. The cells were found to be Gram-negative, motile, non-spore-forming, slightly curved rods. Catalase and oxidase activities were not detected. The optimum NaCl concentration for growth was 2.0 % (w/v), the optimum temperature was 30 degrees C and the optimum pH was 6.3. Strain MSL71T utilized formate, butyrate, pyruvate, lactate, malate, ethanol, propanol, butanol, glycerol and H2 as electron donors for sulfate reduction. The organic electron donors used were incompletely oxidized, mainly to acetate. The strain did not use acetate, propionate, fumarate, succinate, methanol, glycine, alanine, serine, aspartate or glutamate. Sulfite and thiosulfate were used as electron acceptors with lactate as an electron donor, but fumarate was not utilized. Without electron acceptors, pyruvate and malate, but not lactate or fumarate, were fermented. The genomic DNA G+C content was 62.0 mol%. Menaquinone MK-8(H4) was the major respiratory quinone. The major cellular fatty acids were C14 : 0, C16 : 0, C16 : 1 omega 7, C18 : 1 omega 9, C18 : 1 omega 7 and C14 : 0 3-OH. A phylogenetic analysis based on the 16S rRNA gene sequence placed the strain in the class Deltaproteobacteria. The closest recognized relative of strain MSL71T was Desulfofrigus fragile (93.9 % sequence similarity) and the next closest recognized species was Desulfofrigus oceanense (93.5 %). On the basis of the significant differences in the 16S rRNA gene sequence and phenotypic characteristics between strain MSL71T and each of the related species, a novel genus and species, Desulfoluna butyratoxydans gen. nov., sp. nov., are proposed to accommodate strain MSL71T. The type strain is MSL71T (=JCM 14721T=DSM 19427T).
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PMID:Desulfoluna butyratoxydans gen. nov., sp. nov., a novel Gram-negative, butyrate-oxidizing, sulfate-reducing bacterium isolated from an estuarine sediment in Japan. 1839 77

The modeling of growth and production of methanol oxidase (MOX) by Hansenula polymorpha CBS 4732 has been studied to provide a mathematical description of such production processes. Two kinds of mathematical models were constructed for growth on methanol and on mixtures of methanol and glucose. The model for growth on methanol as the sole carbon source consists of kinetics expressions, a limited number of key steps incorporating substrate and production inhibition. This model was used to predict and simulate the culture dynamics at the start-up, the most critical step in continuous cultivation. The growth on mixtures of methanol and glucose was modeled assuming virtually independent metabolic pathways. The induction and production of MOX could be described by adaptation of various repression equations for various data from the literature. The models describe both experimental data and literature data on growth of H. polymorpha CBS 4732 on glucose-methanol mixtures satisfactorily. All parameters for the induction-repression model for growth of H. polymorpha CBS 4732 on glucose-methanol mixtures yielded evidence that a similar induction-repression pattern is involved in MOX production. Catalase, however, is repressed by a different mechanism.
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PMID:Mathematical modeling of growth and production of alcohol oxidase by Hansenula polymorpha grown on methanol-glucose mixtures. 1858 47

Sunflower plants were treated with (14)C-chlorpyrifos under conditions simulating local agricultural practice. Residues present in the oil, methanol extract and cake of the treated sunflower seeds were 7.2, 2.8, and 12 ppm, respectively. When rats fed on sunflower cake containing bound residues for three days, the animals eliminated 46 % of the radioactivity in urine, 25 % in feces and 10 % in the expired air. A further bioavailable amount of 8 % was found in selected organs indicating that the bound residues were highly bioavailable. Chromatographic analysis of urine extract revealed the presence of the parent compound, its oxon, desethyl chlorpyrifos and desethyl chlorpyrifos oxon as free metabolites in addition to a conjugated metabolite. It was liberated by acid hydrolysis and identified as 3,5,6-trichloro-2-hydroxypyridine. Bound residues were found to have biological effects such as inhibition of rat plasma ChE, elevations of liver parameters (ALT, AST, and ALP), decrease in total protein and albumin content suggesting a hepatotoxic potential. A significant increase in the values of creatinine, urea, cholesterol, triglycerides and significant decrease in Catalase and Glutathion-S-Transfrase were observed in treated rats.
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PMID:Bioavailability and toxicological potential of sunflower-bound residues of (14)C-chlorpyrifos insecticide in rats. 2186 39

Catalase is sorted to peroxisomes via a C-terminal peroxisomal targeting signal 1 (PTS1), which binds to the receptor protein Pex5. Analysis of the C-terminal sequences of peroxisomal catalases from various species indicated that catalase never contains the typical C-terminal PTS1 tripeptide-SKL, but invariably is sorted to peroxisomes via a non-canonical sorting sequence. We analyzed the relevance of the non-canonical PTS1 of catalase of the yeast Hansenula polymorpha (-SKI). Using isothermal titration microcalorimetry, we show that the affinity of H. polymorpha Pex5 for a peptide containing -SKI at the C-terminus is 8-fold lower relative to a peptide that has a C-terminal -SKL. Fluorescence microscopy indicated that green fluorescent protein containing the -SKI tripeptide (GFP-SKI) has a prolonged residence time in the cytosol compared to GFP containing -SKL. Replacing the -SKI sequence of catalase into -SKL resulted in reduced levels of enzymatically active catalase in whole cell lysates together with the occurrence of catalase protein aggregates in the peroxisomal matrix. Moreover, the cultures showed a reduced growth yield in methanol-limited chemostats. Finally, we show that a mutant catalase variant that is unable to properly fold mislocalizes in protein aggregates in the cytosol. However, by replacing the PTS1 into -SKL the mutant variant accumulates in protein aggregates inside peroxisomes. Based on our findings we propose that the relatively weak PTS1 of catalase is important to allow proper folding of the enzyme prior to import into peroxisomes, thereby preventing the accumulation of catalase protein aggregates in the organelle matrix.
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PMID:The relevance of the non-canonical PTS1 of peroxisomal catalase. 2254 6

Laboratories around the world have produced tens of thousands of mutant and transgenic zebrafish lines. As with mice, maintaining all of these valuable zebrafish genotypes is expensive, risky, and beyond the capacity of even the largest stock centers. Because reducing oxidative stress has become an important aspect of reducing the variability in mouse sperm cryopreservation, we examined whether antioxidants might improve cryopreservation of zebrafish sperm. Four experiments were conducted in this study. First, we used the xanthine-xanthine oxidase (X-XO) system to generate reactive oxygen species (ROS). The X-XO system was capable of producing a stress reaction in zebrafish sperm reducing its sperm motility in a concentration dependent manner (P<0.05). Second, we examined X-XO and the impact of antioxidants on sperm viability, ROS and motility. Catalase (CAT) mitigated stress and maintained viability and sperm motility (P>0.05), whereas superoxide dismutase (SOD) and vitamin E did not (P<0.05). Third, we evaluated ROS in zebrafish spermatozoa during cryopreservation and its effect on viability and motility. Methanol (8%) reduced viability and sperm motility (P<0.05), but the addition of CAT mitigated these effects (P>0.05), producing a mean 2.0 to 2.9-fold increase in post-thaw motility. Fourth, we examined the effect of additional cryoprotectants and CAT on fresh sperm motility. Cryoprotectants, 8% methanol and 10% dimethylacetamide (DMA), reduced the motility over the control value (P<0.5), whereas 10% dimethylformamide (DMF) with or without CAT did not (P>0.05). Zebrafish sperm protocols should be modified to improve the reliability of the cryopreservation process, perhaps using a different cryoprotectant. Regardless, the simple addition of CAT to present-day procedures will significantly improve this process, assuring increased and less variable fertilization success and allowing resource managers to dependably plan how many straws are needed to safely cryopreserve a genetic line.
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PMID:Oxidative stress in zebrafish (Danio rerio) sperm. 2272 13


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