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

The reactions of steroid hormone biosynthesis are accompanied by formation of oxygen radicals. We determined the levels of some antioxidants and antioxidative enzymes at different developmental stages of bovine corpora lutea to examine their correlation with steroidogenic status. Plasma progesterone concentrations of estrous cycle synchronized cows increased until day 16, and then decreased rapidly during luteal regression. The levels of steroidogenic cytochrome P450scc and adrenodoxin paralleled the changes in plasma progesterone. Among the antioxidative enzymes examined, the SOD and catalase activities showed patterns most similar to plasma progesterone. Catalase and SOD activities increased 6-8 fold from day 6 to 16 of the estrous cycle and then decreased during the luteal regression. Ascorbate and beta-carotene showed low but significant correlation with P450scc and plasma progesterone levels. The profiles of two lipophilic antioxidants in corpora lutea were very different. beta-carotene concentration increased by approximately 6 fold from day 6 to 16, and decreased in regressive tissue. alpha-tocopherol showed a 3 fold increase between days 6 and 9 followed by a rapid decrease. Thus, at the peak of steroidogenesis at mid-luteal phase alpha-tocopherol levels decreased, but beta-carotene levels increased. The correlation between the levels of some antioxidant enzymes and compounds with progesterone levels indicates that antioxidative mechanisms are activated to cope with steroidogenesis dependent oxyradical formation in the bovine corpus luteum.
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PMID:Antioxidant capacity is correlated with steroidogenic status of the corpus luteum during the bovine estrous cycle. 954 62

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 conserved amino acid triad Arg-Trp-His. By contrast, both CCP and APX do not have a substantial catalase activity despite the presence of the same triad. Thus, to elucidate structure-function relationships of catalase-peroxidases (for which no crystal structure is available at the moment), we performed UV-Vis and resonance Raman studies of recombinant wild-type KatG from the cyanobacterium SynechocystisPCC 6803 and the distal side variants (His123-->Gln, Glu; Arg119-->Ala, Asn; Trp122-->Phe, Ala). The distal cavity of KatG is very similar to that of the other class I peroxidases. A H-bond network involving water molecules and the distal Trp, Arg, and His is present, which connects the distal and proximal sides of the heme pocket. However, distal mutation not only affects the heme Fe coordination state and perturbs the proximal Fe-Im bond, as previously observed for other peroxidases, but also alters the stability of the heme architecture. The charge of the distal residues appears particularly important for maintaining the heme architecture. Moreover, the Trp plays a significant role in the distal H-bonding, much more pronounced than in CCP. The relevance of these findings for the catalase activity of KatG is discussed in light of the complete loss of catalase activity in the distal Trp mutants.
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PMID:New insights into the heme cavity structure of catalase-peroxidase: a spectroscopic approach to the recombinant synechocystis enzyme and selected distal cavity mutants. 1211 39

Enterococcus faecalis cells cannot synthesize porphyrins and do not rely on heme for growth but can take up heme and use it to synthesize heme proteins. We recently described a cytochrome bd in E. faecalis strain V583 and here report the identification of a chromosomal gene, katA, encoding a heme-containing cytoplasmic catalase. The 54-kDa KatA polypeptide shows sequence similarity to members of the family of monofunctional catalases. A hexahistidyl-tagged version of the catalase was purified, and major characteristics of the enzyme were determined. It contains one protoheme IX group per KatA polypeptide. Catalase activity was detected only in E. faecalis cells grown in the presence of heme in the medium; about 2 and 10 micro M hemin was required for half-maximal and maximal production of catalase, respectively. Our finding of a catalase whose synthesis is dependent on the acquisition of heme in the opportunistic pathogen E. faecalis might be of clinical importance. Studies of cellular heme transport and heme protein assembly and in vivo synthesis of metalloprotein analogs for biotechnological applications are impeded by the lack of experimental systems. We conclude that the E. faecalis cell potentially provides such a desired system.
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PMID:Enterococcus faecalis heme-dependent catalase. 1239 5

White, D. C. (Rockefeller Institute, New York, N.Y.). Respiratory systems in hemin-requiring Haemophilus species. J. Bacteriol. 85:84-96. 1963.-If grown in Levinthal's medium or in proteose peptone medium with excess hemin, Haemophilus influenzae, H. aegyptius, and H. canis (H. haemoglobinophilus) form an electron-transport system consisting of six cytochromes and two respiratory flavoproteins. In proteose peptone, these species can greatly modify the composition of their electron-transport complex. With anaerobic incubation in the presence of nitrate, they produce increased amounts of cytochrome c(1) and the cytochrome oxidases a(1) and o. This anaerobic pattern is greatly exaggerated by growth under carbon monoxide, in which case large concentrations of cytochrome oxidase are produced. In the presence of the inhibitor secobarbital or of growth-limiting amounts of hemin, intermediate amounts of cytochromes and respiratory flavoproteins are formed. When only small amounts of hemin are present, these species grow but form no detectable cytochrome system. Catalase is the only hemoprotein found. Under these conditions, the addition of glucose induces the formation of a lactate oxidase flavoprotein if the system is incubated aerobically. This cytochromeless state also occurs when these species are grown in KCN or anaerobically without nitrate and with excess hemin. The ability of these species to modify the composition of the electron-transport system strongly suggests that this function unit is formed from individual components. Hemin-requiring Haemophilus species have a hemin-sparing compensatory mechanism that allows growth under conditions under which hemin-independent Haemophilus species will not grow.
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PMID:Respiratory systems in the hemin-requiring Haemophilus species. 1400 Feb 93

Gene expression in frontal, occipital, and hippocampal regions of rat brains at 15 min of ischemic injury was studied in a rat model by producing focal cerebral ischemia through middle cerebral artery (MCA) occlusion without reperfusion. Catalase, epithelial glycoprotein (EGP-314), cytochrome C oxidase-subunit 1, ribosomal L31 protein, and ceruloplasmin were found to be differentially expressed. Specific primers were designed to study this newly reported brain EGP-314, a cellular adhesion molecule involved in cell-cell and cell-extracellular matrix interactions and related with cytoskeletal organization, differentiation, and proliferation. In the frontal and occipital lobes, EGP-314 expression was low in control and ischemic conditions and increased in sham injured conditions, whereas in the hippocampal region its expression was induced only by ischemia. In situ hybridization and immunohistochemistry revealed that EGP-314 mRNA and the protein were present in the ischemic hippocampus pyramidal neurons. DNA fragmentation was demonstrated by TUNEL and LM-PCR analysis in hippocampus region. TUNEL positive pyramidal neurons were observed at 15 min of ischemia. DNA ladder was found at 12 and 15 min of ischemia.
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PMID:EGP-314 is expressed differentially in three brain zones at an early time in an experimentally induced ischemia rat model. 1595 Jul 61

The present study was undertaken to investigate the involvement of nitric oxide in the augmentation of benzo(a)pyrene induced cellular injury in polymorphonuclear leukocytes (PMNs). Polymorphs were isolated from the blood collected from Wistar rats treated with and without benzo(a)pyrene (50mg/kg, i.p.) through cardiac puncture. Catalase, superoxide dismutase (SOD), glutathione-s-transferase (GST), myeloperoxidase (MPO) and nitrite content were estimated in PMNs using standard procedures. Inducible nitric oxide synthase (iNOS) and cytochrome P-4501A1 (CYP1A1) expression in PMNs were also analyzed in presence or absence of nitric oxide synthase (NOS) inhibitors, aminoguanidine (AG, 5mM) and L-NG nitro L-arginine methyl ester (L-NAME, 1mM). A significant augmentation was observed in the nitrite content, activities of superoxide dismutase, MPO and GST and the expressions of iNOS and CYP1A1, however, catalase activity was attenuated in PMNs of benzo(a)pyrene treated rats as compared with their respective controls. AG and L-NAME resulted in a significant attenuation in nitrite content, MPO activity and iNOS expression; however, no significant alteration was observed in CYP1A1 expression. CYP1A1 inhibitor alpha-naphthoflavone inhibited the expression of iNOS in PMNs of benzo(a)pyrene treated animals significantly. The results obtained thus suggest that CYP1A1 induces iNOS expression leading to the generation of endogenous nitric oxide (NO) that could be responsible for the augmentation of myeloperoxidase-mediated benzo(a)pyrene-induced injury in PMNs.
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PMID:Involvement of endogenous nitric oxide in myeloperoxidase mediated benzo(a)pyrene induced polymorphonuclear leukocytes injury. 1654 Nov 99

Medroxyprogesterone acetate was studied at three different concentrations (1, 5 and 10 microM), for its genotoxic effects in human peripheral blood lymphocyte culture using chromosomal aberrations and sister chromatid exchanges as parameters. Duplicate peripheral blood cultures were treated with three different concentrations (1, 5 and 10 microM) of medroxyprogesterone acetate. The study was carried out both in the absence as well as in the presence of metabolic activation (S9 mix) with and without NADP. Medroxyprogesterone acetate was found genotoxic at 5 and 10 microM in the presence of S9 mix with NADP. To study the possible mechanism of the genotoxicity of medroxyprogesterone acetate, superoxide dismutase and catalase at different doses were used separately and in combination with 10 microM of medroxyprogesterone at different doses in the presence of S9 mix with NADP. Superoxide dismutase treatment results in an increase of the genotoxic damage but catalase treatment reduce the genotoxic damage of medroxyprogesterone acetate. Catalase treatment in combination with superoxide dismutase also results in the further reduction of the genotoxic damage. The results of the present study reveal that medroxyprogesterone acetate is genotoxic only in the presence of metabolic activation (S9 mix) with NADP. Treatments with superoxide dismutase and catalase suggests the possible generation of reactive oxygen species by redox cycling of various forms of quinones, similar to estrogens, that are the results of aromatic hydroxylation by cytochrome P450s.
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PMID:Genotoxic potential of medroxyprogesterone acetate in cultured human peripheral blood lymphocytes. 1702 4

Fungal lignin-degrading systems likely include membrane-associated proteins that participate in diverse processes such as uptake and oxidation of lignin fragments, production of ligninolytic secondary metabolites, and defense of the mycelium against ligninolytic oxidants. Little is known about the nature or regulation of these membrane-associated components. We grew the white rot basidiomycete Phanerochaete chrysosporium on cellulose or glucose as the carbon source and monitored the mineralization of a (14)C-labeled synthetic lignin by these cultures to assess their ligninolytic competence. The results showed that the cellulose-grown cultures were ligninolytic, whereas the glucose-grown ones were not. We isolated microsomal membrane fractions from both types of culture and analyzed tryptic digests of their proteins by shotgun liquid chromatography-tandem mass spectrometry. Comparison of the results against the predicted P. chrysosporium proteome showed that a catalase (Joint Genome Institute P. chrysosporium protein identification number [I.D.] 124398), an alcohol oxidase (126879), two transporters (137220 and 132234), and two cytochrome P450s (5011 and 8912) were upregulated under ligninolytic conditions. Quantitative reverse transcription-PCR assays showed that RNA transcripts encoding all of these proteins were also more abundant in ligninolytic cultures. Catalase 124398, alcohol oxidase 126879, and transporter 137220 were found in a proteomic analysis of partially purified plasma membranes from ligninolytic P. chrysosporium and are therefore most likely associated with the outer envelope of the fungus.
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PMID:Differential expression in Phanerochaete chrysosporium of membrane-associated proteins relevant to lignin degradation. 1884 59

A strictly anaerobic, mesophilic, sulfate-reducing bacterial strain (MSL79T) isolated from an estuarine sediment in the Sea of Japan of the Japanese islands was characterized phenotypically and phylogenetically. Cells were Gram-negative, motile with a polar flagellum, non-spore-forming, curved rods. Cells had desulfoviridin and c-type cytochrome. Catalase and oxidase activities were not detected. The optimum NaCl concentration for growth was 2.0% (wt/vol). The optimum temperature was 35 degrees C and the optimum pH was 6.5. Strain MSL79T utilized H2, formate, pyruvate, lactate, fumarate, malate, succinate, ethanol, propanol and butanol as electron donors for sulfate reduction. The organic electron donors were incompletely oxidized to mainly acetate. Sulfite and thiosulfate were used as electron acceptors with lactate as an electron donor. Without electron acceptors, pyruvate, fumarate and malate supported the growth. The genomic DNA G+C content was 62.1 mol%. Menaquinone MK-6(H2) was the major respiratory quinone. Major cellular fatty acids were C16:0, iso-C15:0, anteiso-C15:0, iso-C17:0, anteiso-C17:0 and iso-C17:1omega9. Phylogenetic analysis based on the 16S rRNA gene sequence as well as the alpha-subunit of dissimilatory sulfite reductase gene sequence assigned the strain to the family Desulfovibrionaceae within the class Deltaproteobacteria. The closest validly described species based on the 16S rRNA gene sequences were Desulfovibrio aespoeensis (sequence similarity; 95.0%) and Desulfovibrio profundus (94.3%). On the basis of the significant differences in the 16S rRNA gene sequences and the phenotypic characteristics between strain MSL79T and each of the most closely related species, Desulfovibrio portus sp. nov. is proposed. The type strain is MSL79T (=JCM 14722T=DSM 19338T).
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PMID:Desulfovibrio portus sp. nov., a novel sulfate-reducing bacterium in the class Deltaproteobacteria isolated from an estuarine sediment. 1943 29

Strictly anaerobic, mesophilic, sulfate-reducing bacterial strains were isolated from two anaerobic municipal sewage sludge digesters. One representative strain (BSY(T)) was characterized phenotypically and phylogenetically. Cells were Gram-negative, motile by means of a single polar flagellum, non-spore-forming, curved rods. Cells had desulfoviridin and cytochrome type c. Catalase and oxidase activities were not detected. The optimum NaCl concentration for growth was 0.5 % (w/v). The optimum temperature was 35 degrees C and the optimum pH was 7.1. Strain BSY(T) utilized butyrate, 2-methylbutyrate, valerate, pyruvate, lactate, ethanol, 1-propanol, butanol and H(2) as electron donors for sulfate reduction. This strain grew lithoautotrophically with H(2)/CO(2) under sulfate-reducing conditions. Most organic electron donors were incompletely oxidized to mainly acetate, whereas 2-methylbutyrate and valerate were oxidized to equivalent amounts of acetate and propionate. Strain BSY(T) utilized thiosulfate as an electron acceptor, and grew with pyruvate in the absence of electron acceptors. The genomic DNA G+C content of strain BSY(T) was 63.3 mol%. Menaquinone MK-6(H(2)) was the major respiratory quinone. Major cellular fatty acids were C(14 : 0), C(16 : 0), C(16 : 1) omega7 and C(18 : 1)omega7. Phylogenetic analyses based on 16S rRNA and dissimilatory sulfite-reductase beta-subunit gene sequences assigned strain BSY(T) to the genus Desulfovibrio in the family Desulfovibrionaceae within the class Deltaproteobacteria . Its closest recognized relative based on 16S rRNA gene sequences was the type strain of Desulfovibrio putealis (95.3 % similarity). On the basis of significant differences in 16S rRNA gene sequences and phenotypic characteristics, the sewage sludge strains are considered to represent a single novel species of the genus Desulfovibrio, for which the name Desulfovibrio butyratiphilus sp. nov. is proposed. The type strain is BSY(T) (=JCM 15519(T)=DSM 21556(T)).
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PMID:Desulfovibrio butyratiphilus sp. nov., a Gram-negative, butyrate-oxidizing, sulfate-reducing bacterium isolated from an anaerobic municipal sewage sludge digester. 1965 41


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