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

Although the nonfermentative, asaccharolytic, putative anaerobes Wolinella curva, Wolinella recta, Bacteroides ureolyticus, and Bacteroides gracilis are phylogenetically related to the true campylobacters, the type strains of these species exhibited O2-dependent microaerophilic growth in brucella broth and on brucella agar. The optimum O2 levels for growth of these strains ranged from 4 to 14% in brucella broth and from 2 to 8% on brucella agar, when H2 was provided as the electron donor. No growth occurred under 21% O2, and scant or no growth occurred under anaerobic conditions unless fumarate or nitrate was provided as a terminal electron acceptor. Aspartate, asparagine, and malate also served as apparent electron acceptors. The organisms were catalase negative and, except for B. gracilis, oxidase positive. Catalase added to brucella broth enhanced growth. O2 uptake by all species was inhibited by cyanide and 2-heptyl-4-hydroxyquinoline N-oxide. We concluded that these organisms are not anaerobes but instead are microaerophiles, like their campylobacter relatives.
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PMID:Wolinella recta, Wolinella curva, Bacteroides ureolyticus, and Bacteroides gracilis are microaerophiles, not anaerobes. 185 36

The presence of peroxisomes and peroxisomal enzyme activities were investigated in the oleaginous yeast Apiotrichum curvatum ATCC 20509 (formerly Candida curvata D.) Catalase, a marker enzyme for peroxisomes, was measured in cell-free extracts prepared by sonication. The nature of the carbon and nitrogen sources in the growth medium greatly affected catalase activity. Cells grown on corn oil had high specific activity of catalase, but those grown on glucose, sucrose, or maltose had low specific activity. High specific activity of catalase was measured in cultures grown on media that supported poor growth (with soluble starch as carbon source or with methylamine, urea, or asparagine as nitrogen source). Peroxisomes from cells grown on corn oil were separated from other subcellular fractions in a discontinuous sucrose gradient. Major peaks of activity of fatty acid beta-oxidation and of two key enzymes in the glyoxylate cycle were found in fractions containing peroxisomes, but not in fractions corresponding to the mitochondria. Peroxisomal beta-oxidation showed equivalent activity with palmitoyl CoA or n-octanoyl CoA as substrate. Mitochondria did not seem to contain NAD-linked glutamate dehydrogenase. Peroxisomes with a homogeneous matrix and core surrounded by a single-layer membrane were observed with an electron microscope in cells grown on corn oil, but not in those grown on glucose. Staining with 3,3'-diaminobenzidine revealed that catalase activity was located in peroxisomes. Peroxisomes in this oleaginous yeast play important roles in lipid metabolism.
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PMID:Evidence of peroxisomes and peroxisomal enzyme activities in the oleaginous yeast Apiotrichum curvatum. 187 14

A nocardioform bacterium was isolated from the spleen tissue of an armadillo infected with M. leprae and easily propagated in pure culture in mineral salt medium supplemented with only simple C and N sources (e.g., liquid paraffin, tetradecane, ammonium salts, urea, asparagine, gelatin, xanthin, hypoxanthin etc.). Complex organic substances, e.g., tyrosin, casein, peptone, meat extract, egg proteins, serum, blood, yeast extract as well as medium 199, did not support the growth of this organism. Microscopically, the organism consisted of acid-fast, long, slender rods which originated from long, fragmented hyphae, or sporulating mycelial tufts; it was acid-fast (at less than 4.0% H2SO4) which was pyridine-susceptible. It produced DOPA-oxidase and Catalase and was lysozyme resistant; this grew best under reduced O2 tension, at pH 7.0 to 8.0 and 28 degrees C. Serologically, it appeared to be only weakly related to the prototype human multibacillary leprosy-derived (reference) nocardioform strain, Nocardia brasiliensis and N. caviae, but was variably related to several mycobacteria strains.
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PMID:Cultivation of a nocardioform acid-fast chemoautotrophic bacterium from armadillo tissues infected with Mycobacterium leprae. 218 9

Apiotrichum curvatum ATCC 20509, an oleaginous yeast that can accumulate up to 60% of its cellular dry weight as intracellular lipid when grown with excess carbon, was grown in nitrogen-limited, balanced, and lactose-free medium with asparagine as nitrogen source and lactose as carbon source. Biomass and lipid accumulation were measured, cell composition was analyzed, and catalase activity was followed as marker enzyme for peroxisomes. The organism accumulated 54% of its dry weight as total cellular lipid when grown under nitrogen limitation and accumulated only 20-25% of its dry weight as lipid when grown in balanced medium. When starved for carbon, cells utilized endogenous lipid and carbohydrate as carbon and energy sources; the intracellular contents of lipid and carbohydrate decreased by 31 and 26%, respectively. Intracellular carbohydrates also seemed to be used as intermediates for lipid accumulation and lipid turnover. Catalase activity was strongly induced (over 10-fold increase in specific activity) when cells metabolized endogenous lipid. The lipid content of cells was inversely related to catalase activity and to intracellular protein or total nitrogen content. Lipid content showed no correlation with intracellular carbohydrate content.
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PMID:Lipid metabolism and cell composition of the oleaginous yeast Apiotrichum curvatum grown at different carbon to nitrogen ratios. 239 Jul 44

Aerobic degradation of dimethyl sulfide (DMS), previously described for thiobacilli and hyphomicrobia, involves catabolism to sulfide via methanethiol (CH3SH). Methyl groups are sequentially eliminated as HCHO by incorporation of O2 catalyzed by DMS monooxygenase and methanethiol oxidase. H2O2 formed during CH3SH oxidation is destroyed by catalase. We recently isolated Thiobacillus strain ASN-1, which grows either aerobically or anaerobically with denitrification on DMS. Comparative experiments with Thiobacillus thioparus T5, which grows only aerobically on DMS, indicate a novel mechanism for aerobic DMS catabolism by Thiobacillus strain ASN-1. Evidence that both organisms initially attacked the methyl group, rather than the sulfur atom, in DMS was their conversion of ethyl methyl sulfide to ethanethiol. HCHO transiently accumulated during the aerobic use of DMS by T. thioparus but not with Thiobacillus strain ASN-1. Catalase levels in cells grown aerobically on DMS were about 100-fold lower in Thiobacillus strain ASN-1 than in T. thioparus T5, suggesting the absence of H2O2 formation during DMS catabolism. Also, aerobic growth of T. thioparus T5 on DMS was blocked by the catalase inhibitor 3-amino-1,2,4-triazole whereas that of Thiobacillus strain ASN-1 was not. Methyl butyl ether, but not CHCl3, blocked DMS catabolism by T. thioparus T5, presumably by inhibiting DMS monooxygenase and perhaps methanethiol oxidase. In contrast, DMS metabolism by Thiobacillus strain ASN-1 was unaffected by methyl butyl ether but inhibited by CHCl3. DMS catabolism by Thiobacillus strain ASN-1 probably involves methyl transfer to a cobalamin carrier and subsequent oxidation as folate-bound intermediates.
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PMID:A new mechanism for the aerobic catabolism of dimethyl sulfide. 828 84

Catalase-peroxidases (KatGs) are unique in exhibiting an overwhelming catalase activity and a peroxidase activity of broad specificity. Similar to other peroxidases the distal histidine in KatGs forms a hydrogen bond with an adjacent conserved asparagine. To investigate the catalytic role(s) of this potential hydrogen bond in the bifunctional activity of KatGs, Asn153 in Synechocystis KatG was replaced with either Ala (Asn153-->Ala) or Asp (Asn153-->Asp). Both variants exhibit an overall peroxidase activity similar with wild-type KatG. Cyanide binding is monophasic, however, the second-order binding rates are reduced to 5.4% (Asn153-->Ala) and 9.5% (Asn153-->Asp) of the value of native KatG [(4.8 +/- 0.4) x 105 m-1.s-1 at pH 7 and 15 degrees C]. The turnover number of catalase activity of Asn153-->Ala is 6% and that of Asn153-->Asp is 16.5% of wild-type activity. Stopped-flow analysis of the reaction of the ferric forms with H2O2 suggest that exchange of Asn did not shift significantly the ratio of rates of H2O2-mediated compound I formation and reduction. Both rates seem to be reduced most probably because (a) the lower basicity of His123 hampers its function as acid-base catalyst and (b) Asn153 is part of an extended KatG-typical H-bond network, the integrity of which seems to be essential to provide optimal conditions for binding and oxidation of the second H2O2 molecule necessary in the catalase reaction.
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PMID:The catalytic role of the distal site asparagine-histidine couple in catalase-peroxidases. 1260 34

The results of this study of the effect of temperature on the respiratory mechanism of five stenothermophilic bacteria may be summarized as follows:- 1. The respiratory mechanism and its various components of the stenothermophilic bacteria were found to function at temperatures below the minimum temperature for growth of these organisms. In every case the rates of the individual reactions involved in the respiratory chain increased exponentially with temperature until the temperature at which inactivation became apparent was reached. 2. The mean activation energies, calculated from the "best" value for the slope of the straight lines resulting from a plot of log rate against the reciprocal of the absolute temperature were: Dehydrogenases: 28,000 to 28,500 calories per gram molecule. Glucose, fructose, galactose, mannose, xylose, arabinose, maltose, lactose, sucrose, glycine, beta-alanine, monosodium glutamate, (asparagine). 19,500 to 20,500 calories per gram molecule. Ethyl alcohol, succinate, pyruvate, lactate, acetate. 19,500 to 20,500 calories per gram molecule. Ethyl alcohol, succinate, pyruvate, lactate, acetate. 15,000 calories per gram molecule. Formate. Cytochrome oxidase and cytochrome b and c (substrate: p-phenylenediamine): 16,800 calories per gram molecule. Cytochrome oxidase and cytochrome c (substrate: hydroquinone): 20,200 calories per gram molecule. Catalase: 4,100 calories per gram molecule. Complete aerobic respiratory system (plus added glucose): 29,500 calories per gram molecule. 3. The identity of the energies of activation of the respiratory system and its enzymic components at temperatures above and below the minimum temperature for growth of the stenothermophilic bacteria was demonstrated. 4. An attempt has been made to indicate a relationship between the nature of the substrate and the activation energy by grouping substrates on the basis of common micro values obtained for their dehydrogenation by resting cell preparations of stenothermophilic bacteria. The dehydrogenation reactions have been found to be the rate-controlling reactions in the aerobic respiratory system of these bacteria.
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PMID:Temperature activation of certain respiratory enzymes of stenothermophilic bacteria. 1810 98

Disulfide bond formation during protein folding of nascent proteins is associated with the generation of H2O2 in the endoplasmic reticulum (ER). Approaches to quantifying H2O2 directly within the ER failed because of the oxidative environment in the ER lumen, and ER-specific catalase expression to detoxify high H2O2 concentrations resulted in an inactive protein owing to N-glycosylation. Therefore, the N-glycosylation motifs at asparagine-244 and -439 of the human catalase protein were deleted by site-directed mutagenesis. The ER-targeted expression of these variants revealed that the deletion of the N-glycosylation motif only at asparagine-244 (N244) was associated with the maintenance of full enzymatic activity in the ER. Expression of catalase N244 in the ER (ER-Catalase N244) was ER-specific and protected the cells significantly against exogenously added H2O2. With the expression of ER-Catalase N244, a highly effective H2O2 inactivation within the ER was achieved for the first time. Catalase has a high H2O2-inactivation capacity without the need of reducing cofactors, which might interfere with the ER redox homeostasis, and is not involved in protein folding. With these characteristics ER-Catalase N244 is an ideal tool to explore the impact of ER-generated H2O2 on the generation of disulfide bonds or to study the induction of ER-stress pathways through protein folding overload and accumulation of H2O2.
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PMID:N-glycosylation-negative catalase: a useful tool for exploring the role of hydrogen peroxide in the endoplasmic reticulum. 2549 53