Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The present study tested the hypothesis that BCG-activated macrophages become injured when they phagocytose certain particulates. The data indicate that alveolar macrophages obtained from Mycobacterium bovis BCG-sensitized animals were more susceptible to cell death after in vitro incubation with BCG or zymosan than were macrophages from normal animals. Increased susceptibility was dependent on phagocytosis, since incubation with cytochalasin B, a phagocytosis inhibitor, abrogated the effect. Catalase, cytochrome c, and ascorbic acid offered partial protection to the macrophage, suggesting the involvement of free radicals in the generation of cytotoxicity. Not all of the cells from the alveolar populations were equally susceptible to cell death, thus suggesting either heterogeneity in the cell population or a requirement of more than one cell type in the induction of necrosis or both.
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PMID:Phagocytosis-induced injury of normal and activated alveolar macrophages. 23 Oct 11

Mycobacterium phlei contains two catalase activities and a single peroxidase activity. The latter is associated with one of the catalases. The single catalase-peroxidase enzyme accounted for 75% of the total catalase activity and was lost upon acquisition of resistance to the antitubercular drug isoniazid (INH). Heat-treated (68 degrees C) wild-type cells showed similar decreases in catalase activity as well as complete loss of peroxidase activity. Catalase activity in the INH-resistant strain of M. phlei (Inh(r)) was unaffected by heating. The heat-sensitive catalase of the wild-type M. phlei was completely inhibited by 0.1 M INH, and Cu(2+) enhanced this inhibitory effect by 100-fold. No inhibition of activity was found with the heat-stable enzyme. Equivalent inhibition of catalase was also observed with nicotinic acid hydrazide and benzoic acid hydrazide. Peroxidase activity was also completely inhibited by any one of the three hydrazides, either INH, benzoic acid hydrazide, or nicotinic acid hydrazide at 10(-3) M. The presence of two catalase activities and the loss of one (catalase-peroxidase) on acquiring INH resistance or heating wild-type cells was confirmed by acrylamide gel electrophoresis of the cell-free extracts.
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PMID:Differentiation of catalases in Mycobacterium phlei on the basis of susceptibility to isoniazid: association with peroxidase and acquired resistance to isoniazid. 92 Dec 49

A rapid growing acid-fast organism was isolated from the blood of a borderline leprosy patient. The isolate appeared to be close to Mycobacterium cheloni group of organisms but showed globi, cigar shaped bundles and was positive for DOPA-oxidase. Catalase, iron uptake, sodium chloride tolerance, tellurite reduction, Tween 80 hydrolysis and pyridine extraction tests were also positive. The 3-days arylsulphatase test and nitrate reduction test were negative.
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PMID:Isolation of a DOPA positive rapid growing mycobacterium from blood of a leprosy patient. 157 5

A case of cutaneous atypical mycobacteriosis due to Mycobacterium (M.) kansasii is reported. A 41-year-old man, who had lived in Kawasaki city, was seen in April 1988 because of sores on the dorsum of left forefinger which had been present for one month. Physical examination revealed an erythematous, edematous plaque approximately 2 and 4 cm overlying proximal and middle phalanx of left index finger. Otherwise his physical findings were normal. Laboratory studies including X-ray examinations of the chest and left hand were normal. The histopathology revealed a mixed cellular infiltration consists of mononuclear cells and neutrophils with necrosis in the dermis. No granuloma formation was observed. In the deep dermis, some acid fast bacilli (AFB) were demonstrated. The culture for AFB was positive with the following characteristics: Acidfastness (+), Niacin (-), Photochromogenecity (+), Growth at 37 degrees C (+), at 42 degrees C (+), at 45 degrees C (-), Nitrate reduction (+), Catalase (+). These tests were diagnostic of Group I photochromogen, M. kansasii. We reviewed 19 cases of cutaneous atypical mycobacteriosis due to M. kansasii in the world literature including our case and found that there were three types of the disease: (1) Cutaneous chronic granulomatous type, (2) Disseminated acute pyogenic type and (3) Cutaneous pyogenic type.
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PMID:[Cutaneous atypical mycobacteriosis due to Mycobacterium kansasii--a case report and a review of the literature]. 221 38

A virulent Mycobacterium avium strain, LR25, which carries three plasmids (18, 28, and 165 kilobases) and grows at 43 degrees C was compared with its plasmid-free, avirulent segregant, strain LR163, to identify the basis for the latter's inability to grow at 43 degrees C. The failure of mid-log-phase cultures of strain LR163 to grow at 43 degrees C was dependent on the presence of high levels of culture aeration. In addition, highly aerated cultures of strain LR163 failed to grow at 37 degrees C. Mid-log-phase cultures of strain LR163 had 30% of the catalase activity of strain LR25 and were more hydrogen peroxide (0.08%, wt/vol) susceptible. Catalase activity of strain LR25 was higher in cultures grown with high aeration than in those grown with almost no aeration. These data support the contention that plasmid-encoded genes influence M. avium catalase activity.
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PMID:Plasmid-influenced changes in Mycobacterium avium catalase activity. 272 36

Fairly pure leprosy bacilli were easily collected from nude mouse foot pad lepromas by the Ficoll density gradient centrifugation and alkali treatment methods. The yield of bacilli available for biochemical study was 42.6%. The density of Mycobacterium leprae was very heterogeneous. The percent of solid bacilli in the light bacilli fraction was 23%; that in the heavy bacilli fraction was 40%. The endogenous respiration activity in the heavy bacilli was greater than that in light bacilli. The average coefficient of respiration in M. leprae was 1 microliter O2/mg X hr. In the whole cells of M. leprae, a cytochrome b1 absorption peak and its Soret peak were detected at wavelengths of 560 nm and 426 nm, respectively. However, a cytochrome a2-like peak (which was observed in M. lepraemurium), and a cyt c and cyt a were not detected. Catalase activity was not found in whole cells, the cell-free extract, or particle fractions of M. leprae. Any catalase activity associated with M. leprae suspensions is a tissue contaminant. NAD-peroxidase activity was also not detected in the cell-free extract of the leprosy bacillus. These results would indicate that leprosy bacilli cannot degrade hydrogen peroxide.
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PMID:Respiration in Mycobacterium leprae. 300 14

Xanthine oxidase with acetaldehyde as substrate (the XOA system) generated superoxide anion and hydrogen peroxide, but this system had only weak bactericidal activity. Addition of Fe2+ and EDTA to the XOA system (XOA-Fe-EDTA system) increased bactericidal activity against Staphylococcus aureus, Escherichia coli, Listeria monocytogenes and Salmonella typhimurium, although both Mycobacterium tuberculosis and Candida albicans remained highly resistant. Catalase (H2O2 scavenger) and mannitol (.OH scavenger) almost completely inhibited the bactericidal activity of the XOA-Fe-EDTA system whereas SOD (O2- scavenger) was less inhibitory. Azide (1O2 scavenger) caused no such inhibition. The results suggest the possible role of .OH, H2O2 and O2- in the XOA-Fe-EDTA-mediated antimicrobial system, as effector molecules. There was no correlation between resistance of a given bacterium to active oxygen and the level of endogenous active oxygen-scavengers.
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PMID:Susceptibility of micro-organisms to active oxygen species: sensitivity to the xanthine-oxidase-mediated antimicrobial system. 312 35

The five mycobacteria Mycobacterium lepraemurium, M. leprae, M. bovis BCG, M. smegmatis, and M. intracellulare were studied. Catalase and peroxidase activities were demonstrated in polyacrylamide and crossed immunoelectrophoresis gels for M. lepraemurium, M. intracellulare, and BCG, but not for M. leprae. Peroxidase and catalase activities were associated with the same precipitate line in crossed immunoelectrophoresis for M. lepraemurium, M. intracellulare, and BCG, showing that in these mycobacteria the two enzyme activities resided in the same molecule. M. smegmatis peroxidase and catalase activities were closely associated on polyacrylamide gel electrophoresis, but on the crossed immunoelectrophoresis catalase and peroxidase activities were associated with two different precipitate lines. Catalases without peroxidase activity were demonstrated in crossed immunoelectrophoresis and polyacrylamide gel electrophoresis in M. intracellulare and M. smegmatis. The catalase without peroxidase activity in M. intracellulare was heat resistant and therefore classified as an m-catalase. In M. smegmatis the catalase without peroxidase activity was only partially heat resistant. All of the catalases with peroxidase activity were heat-sensitive t-catalases. Superoxide dismutase activity in the crossed immunoelectrophoresis was associated with the M. leprae antigen no. 4 and with cross-reacting antigens in the other mycobacteria studied. Several superoxide dismutases were demonstrated in Mycobacterium duvalii. They were antigenically different from the other superoxide dismutases in this study, as shown by lack of reactivity with a monospecific antibody to M. lepraemurium superoxide dismutase. Molecular weights were estimated for all the enzymes in this study by sodium dodecyl sulfate-polyacrylamide gels.
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PMID:Catalases, peroxidases, and superoxide dismutases in Mycobacterium leprae and other mycobacteria studied by crossed immunoelectrophoresis and polyacrylamide gel electrophoresis. 353 45

Superoxide dismutase has been identified and peroxidatic activity demonstrated in Mycobacterium leprae. The superoxide dismutase, shown indirectly to be a manganese-containing enzyme, was present at low activity in the cell-free extract. Peroxidatic activity was detected in a haemoprotein on polyacrylamide gels, but quantitative assay was not possible. Catalase, although present in a cell-free extract, appeared to be a host-derived enzyme, thus emphasizing the importance of establishing the authenticity of enzyme activities in host-derived M. leprae. The implications for the growth of M. leprae in vivo and its non-cultivability are discussed in the light of these findings.
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PMID:Superoxide dismutase, peroxidatic activity and catalase in Mycobacterium leprae purified from armadillo liver. 702 67

Catalase-peroxidases have a predominant catalatic activity but differ from monofunctional catalases in exhibiting a substantial peroxidatic reaction which has been implicated in the activation of the antitubercular drug isoniazid in Mycobacterium tuberculosis. Hydroperoxidase I of Escherichia coli encoded by katG is a catalase-peroxidase, and residues in its putative active site have been the target of a site directed-mutagenesis study. Variants of residues R102 and H106, on the distal side of the heme, and H267, the proximal side ligand, were constructed, all of which substantially reduced the catalatic activity and, to a lesser extent, the peroxidatic activity. In addition, the heme content of the variants was reduced relative to the wild-type enzyme. The relative ease of heme loss from HPI and a mixture of tetrameric enzymes with 2, 3, and 4 hemes was revealed by mass spectrometry analysis. Conversion of W105 to either an aromatic (F) or aliphatic (I) residue caused a 4-5-fold increase in peroxidatic activity, coupled with a >99% inhibition of catalatic activity. The peroxidatic-to-catalatic ratio of the W105F variant was increased 2800-fold such that compound I could be identified by both electronic and EPR spectroscopy as being similar to the porphyrin cation radical formed in other catalases and peroxidases. Compound I, when generated by a single addition of H(2)O(2), decayed back to the native or resting state within 1 min. When H(2)O(2) was generated enzymatically in situ at low levels, active compound I was evident for up to 2 h. However, such prolonged treatment resulted in conversion of compound I to a reversibly inactivated and, eventually, to an irreversibly inactivated species, both of which were spectrally similar to compound I.
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PMID:Modulation of the activities of catalase-peroxidase HPI of Escherichia coli by site-directed mutagenesis. 1080 38


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