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At least 19 recordsLinked to original sources
PubMed1999

Aspergillus fumigatus catalases: cloning of an Aspergillus nidulans catalase B homologue and evidence for at least three catalases.

The presence of catalases in the water soluble fractions of three Aspergillus fumigatus strains was investigated using non-denaturing and denaturing polyacrylamide gel electrophoresis and Western analysis. Using non-denaturing polyacrylamide gel electrophoresis and staining for catalase activity, three separate catalases were identified. An A. fumigatus catalase gene (catB) was cloned from genomic DNA using the Aspergillus niger catR gene as a probe. Polyclonal antibodies were raised to a glutathione S-transferase-CatB fusion product expressed in Escherichia coli. Western analysis indicated that, under denaturing conditions, the polyclonal antibody recognised a 90-kDa band and under non-denaturing conditions, two separate bands were identified. These results indicate that A. fumigatus in addition to CatB, produces at least two other catalases, one of which is similar in size to CatB. The polyclonal antibody was also used to observe catalase expression in mice, experimentally infected with A. fumigatus. Staining was observed heterogeneously throughout the fungal hyphae. This result indicates that catalase is produced by A. fumigatus during invasive aspergillosis.

Animals↗
PubMed1977

Catalase in salivary gland striated and excretory duct cells. I. The distribution of cytoplasmic and particulate catalase and the presence of catalase-positive rods.

Catalase-positive rods of different dimensions, which frequently appeared crystalline by light microscopy, were found to be concentrated along with microbodies and cytoplasmic enzyme in the cells of the striated and extralobular excretory ducts of mouse salivary glands. When an entire mouse submandibular gland and its ducts were excised, fixed, sectioned and incubated for catalase demonstration, the excretory ducts were intensely stained relative to the remainder of the gland. Light microscopic examination of the stained ductal cells revealed particulate catalase in the form of rods and microbodies as well as reactivity due to non-particulate cytoplasmic enzyme. The cytoplasmic enzyme activity was less intense in some ductal epithelial cells (light cells) which were interspersed in mosaic arrangement among those more intensely stained (dark cells). The rods were somewhat more common in the light cells. Although the rods lack a symmetrical definitive crystal habit, their gross conformation and periodic substructure are reminiscent of crystalline catalase. No rods and relatively few peroxisomes were observed in excretory duct cells of germ-free mice although cytoplasmic catalase was abundant. These observations suggest that the catalase in salivary gland duct cells could be related in some way to the protection of the gland or the oral cavity or both against micro-organisms. Alternatively, the enzyme could be involved in the non-thyroidal biosynthesis of iodinated tyrosine derivatives.

Animals↗
PubMed1976

Catalase biosynthesis in yeast: formation of catalase A and catalase T during oxygen adaptation of Saccharomyces cerevisiae.

Catalase A from Saccharomyces cerevisiae and its biosynthetic precursors can specifically be immunoprecipitated from extracts obtained from yeast cells grown in the presence of L-[3H]leucine or 59FeCl3. The enzyme and its precursors recognized by a specific antiserum are absent from anaerobic cells. During oxygen adaptation of yeast pre-grown on 0.3% glucose under anaerobic conditions catalase A is formed via a heme-less precursor, probably the apomonomer of the protein, and a heme-containing intermediate. When cells are grown in the presence of Tween 80 the amount of catalase A, but not of catalase T, increases 4-fold. Comparison of the mode of synthesis of catalase T and A shows that no precursor-product relationship exists between the two proteins.

Adaptation, Physiological↗
PubMed1996

Molecular evolution of maize catalases and their relationship to other eukaryotic and prokaryotic catalases.

We have compared the nucleotide and protein sequences of the three maize catalase genes with other plant catalases to reconstruct the evolutionary relationship among these catalases. These sequences were also compared with other eukaryotic and prokaryotic catalases. Phylogenies based on distances and parsimony analysis show that all plant catalases derive from a common ancestral catalase gene and can be divided into three distinct groups. The first, and major, group includes maize Cat1, barley Cat1, rice CatB, and most of the dicot catalases. The second group is an apparent dicot-specific catalase group encompassing the tobacco Cat2 and tomato Cat. The third is a monocot-specific catalase class including the maize Cat3, barley Cat2, and rice CatA. The maize Cat2 gene is loosely related to the first group. The distinctive features of monocot-specific catalases are their extreme high codon bias at the third position and low degree of sequence similarity to other plant catalases. Similarities in the intron positions for several plant catalase genes support the conclusion of derivation from a common ancestral gene. The similar intron position between bean catalases and human catalase implies that the animal and plant catalases might have derived from a common progenitor gene sequence.

Catalase↗
PubMed1991

Serum catalase: reversibly formed charge isoform of erythrocyte catalase.

The different electrophoretic mobilities of erythrocyte and serum catalase (EC 1.11.1.6) were confirmed and the causes responsible for their differences were examined. The presence of a catalase-binding protein in serum that could form a complex with erythrocyte catalase was excluded by incubating serum proteins with erythrocyte catalase. No new unequivocal catalase bands representing a catalase-binding protein were detected. The erythrocyte and serum catalase proved to be charge isoforms: their molecular masses, estimated by gel permeation chromatography or polyacrylamide gel electrophoresis in a nondenaturing system, were very similar, whereas their electrophoretic mobilities were different. Assay of serum catalase by gel permeation and hydrophobic chromatography yielded a product with the same electrophoretic mobility as that of erythrocyte catalase. Different dilution of erythrocyte catalase with human sera led to a gradual decrease of its mobility, 20-fold or greater dilution yielding the same results as for serum catalase. Similarly, when serum catalase was diluted 20-fold or more with 60 mmol/L phosphate buffer, it migrated similarly to erythrocyte catalase. I detected no effect of dialyzable serum ligands, NADPH, or protection of SH groups on the electrophoretic mobility of either catalase isoform. I conclude that formation of charge isoforms of catalase is caused by a reversible, conformational modification due to matrix effect of serum.

Carrier Proteins↗
PubMed1981

Biosynthesis of liver catalase in rats treated with allylisopropylacetylcarbamide. III. Occurrence of a possible precursor to catalase.

Inactive catalase [EC 1.11.1.6] occurring in considerable amounts in liver peroxisomal extracts from Sedormid-treated rats was investigated. The antigen-to-enzyme ratio (i.e. the ratio of catalase determined immunochemically to catalase determined enzymatically; 1.0 for purified enzyme) was around 1.7 when peroxisomal extract from Sedormid-treated rats was assayed. After dialysis of the extract against a solution containing 44 mM acetate buffer, pH 4.1, and 22% ethanol, catalase remaining in soluble from showed the same antigen-to-enzyme ratio as the purified enzyme (1.0). Moreover, the total enzymatic activity was not reduced. The results indicated that the catalase precipitated by this treatment was enzymatically inactive. The peroxisomal extract was analyzed by gel filtration, and an enzymatically inactive catalase was detected in the region corresponding to molecules smaller than the enzymatically active catalase (tetramer). When the immunoprecipitates of the inactive catalase were analyzed by polyacrylamide gel electrophoresis in the presence of SDS and urea, only a subunit (monomer) of catalase was detected. At 60 min after injection of [14C]amino acid and delta-[3H]aminolevulinic acid into rats, the specific radioactivity of 14C in this inactive catalase was 6-7 times that of active catalase. On the other hand, the 3H/14C ratio was much lower than that of active catalase. The results suggest that the inactive catalase isolated by gel filtration is an intermediate of maturation, in which apo-catalase monomer binds with heme and assembles to form complete molecules.

Animals↗
PubMed1996

Dinucleotide-binding site of bovine liver catalase mimics a catalase mRNA-binding protein domain.

Rat lung contains protein that interacts with catalase mRNA to form specific, redox-sensitive RNA-protein complexes. The studies in this report were aimed at determining whether catalase protein binds its own RNA. We found that rat catalase RNA binds NADPH-depleted bovine liver catalase (Sigma) but does not bind bovine liver catalase in the presence of NADPH. Complex formation between liver catalase and catalase RNA is competitively eliminated by a CA dinucleotide repeat. These data suggest the dinucleotide binding site of catalase mimics or is homologous to a catalase RNA-binding protein domain. These findings support the hypothesis that a class of RNA-binding proteins may have evolved from (di)nucleotide binding enzymes (M. W. Hentze. Trends Biol. Sci. 19: 101, 1994). When bovine liver catalase from two other commercial sources (Calbiochem and Boehringer) was used, we could not detect binding to catalase RNA. We have not yet been able to identify the basis for this difference. Thus the physiological importance of our observation of the NADPH-sensitive protein binding to catalase RNA cannot be assessed at this time.

Animals↗
PubMed2000

Purification and characterization of a catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1(T) exhibiting high catalase activity.

Catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1(T), which was isolated from an environment exposed to H(2)O(2) and exhibited high catalase activity, was purified and characterized, and its localization in the cell was determined. Its molecular mass was 230 kDa, and the molecule consisted of four identical subunits. The enzyme, which was not apparently reduced by dithionite, showed a Soret peak at 406 nm in a resting state. The catalytic activity was 527,500 U. mg of protein(-1) under standard reaction conditions at 40 degrees C, 1.5 and 4.3 times faster, respectively, than those of the Micrococcus luteus and bovine catalases examined under the same reaction conditions, and showed a broad optimum pH range (pH 6 to 10). The catalase from strain S-1(T) is located not only in the cytoplasmic space but also in the periplasmic space. There is little difference in the activation energy for the activity between strain S-1(T) catalase and M. luteus and bovine liver catalases. The thermoinstability of the activity of the former catalase were significantly higher than those of the latter catalases. The thermoinstability suggests that the catalase from strain S-1(T) should be categorized as a psychrophilic enzyme. Although the catalase from strain S-1(T) is classified as a mammal type catalase, it exhibits the unique enzymatic properties of high intensity of enzymatic activity and thermoinstability. The results obtained suggest that these unique properties of the enzyme are in accordance with the environmental conditions under which the microorganism lives.

Amino Acids↗
PubMed1995

Transcriptional regulation of catalase gene in the fission yeast Schizosaccharomyces pombe: molecular cloning of the catalase gene and northern blot analyses of the transcript.

Exposure of Schizosaccharomyces pombe cells to various stresses including 0.2 mM hydrogen peroxide, 50 microM menadione, 10 J/m2 of UV irradiation at 255 nm, and high osmolarity (0.5 M sorbitol or 0.3 M NaCl) induces catalase [EC 1.11.1.6] activity. A part of the catalase gene of S. pombe was amplified by PCR with oligonucleotide primers designed from amino acid sequences conserved in several species of catalases. The catalase gene including its flanking sequence of S. pombe was cloned from a genomic DNA library of S. pombe, which was constructed on the EMBL3 vector, using the PCR-amplified DNA as a radioactive probe. A 3.5 kb HindIII fragment, which hybridized with the PCR-amplified probe, was subcloned into pUC19 and sequenced. The fragment contains one long open reading frame without any intron. The polypeptide deduced from the nucleotide sequence consists of 512 amino acid residues and is homologous to several other catalases. Amino acid sequences of the proteolytic peptides obtained from the purified catalase of S. pombe coincided with the amino acid sequence predicted from the DNA sequence. Transcription of this gene starts at 370 bases upstream of the initiation methionine codon. Northern blot analyses of the catalase mRNA revealed that the stresses which induce the catalase activity also induce the transcription of the catalase gene. The induction of the catalase mRNA by hydrogen peroxide is not inhibited by cycloheximide or staurosporine.

Alkaloids↗
PubMed1998

A low catalase activity in dog erythrocytes is due to a very low content of catalase protein despite having a normal specific activity.

Catalase was purified to an apparent homogeneity from dog erythrocytes and its properties were compared with those of human erythrocyte catalase. Purification was unsuccessful without the use of glycerol as the stabilizing agent. Molecular weight of the purified dog catalase was estimated to be about 63,000 Da in monomer and about 230,000 Da in native tetramer form. The ratio of A405/A280, the index of hematin content relative to protein, was 1.15. The isoelectric point was in the range of 5.8 to 6.4. These properties of dog catalase were very similar to those of human catalase. Dog catalase also possessed the same partial amino acid sequence as human catalase. However, the specific activity of dog enzyme was about threefold less than that of human enzyme. The amount of catalase protein in dog erythrocytes determined by immunoblotting analysis was about tenfold less than that of human erythrocytes. This was consistent with the fact that the catalase activity in dog hemolysate was about 1/30 of that in human hemolysate.

Amino Acid Sequence↗
PubMed1987

Catalase gene of the yeast Candida tropicalis. Sequence analysis and comparison with peroxisomal and cytosolic catalases from other sources.

A clone harbouring the genomic DNA sequence for the peroxisomal catalase of an n-alkane-utilizable yeast, Candida tropicalis, has been isolated by the hybrid-selection method and confirmed with a probe of catalase partial cDNA. Nucleotide sequence analysis of the cloned DNA disclosed that the gene fragment coding for catalase had a length of 1455 base pairs (corresponding to 485 amino acids; m = 54937 Da), and that the size of this enzyme was the smallest among all catalases reported hitherto. No intervening sequence was found in this coding region and some portions coincided with the amino acid sequences obtained from the analysis of the purified catalase. The comparison with three peroxisomal catalases from rat liver, bovine liver and human kidney, and one cytosolic catalase from Saccharomyces cerevisiae has revealed that catalase from C. tropicalis was more homologous to the peroxisomal enzymes than to the cytosolic one. C. tropicalis used the codons of the high-expression type. Amino acid residues were all conserved at the active and heme-binding sites. In the N and C-terminal regions there was no characteristic signal sequence or consensus sequence. However, a noticeable region, which can be discriminated between peroxisomal and cytosolic catalases, was proposed.

Amino Acid Sequence↗
PubMed1997

The predominant protein in peroxisomal cores of sunflower cotyledons is a catalase that differs in primary structure from the catalase in the peroxisomal matrix.

This paper describes a biochemical study on the protein composition of crystalline inclusions (cores) from plant peroxisomes. By SDS/PAGE and immunoblotting, a catalase of 59 kDa was identified as the predominant protein component in purified cores from sunflower (Helianthus annuus L.) cotyledons. A 55-kDa catalase was the only additional peptide detected. In contrast to in cores, the 55-kDa catalase was the major catalase protein in matrix fractions obtained from lysed peroxisomes. These findings suggested two peroxisomal populations of catalase differing in molecular structure and subperoxisomal compartmentation in sunflower cotyledons. Evidence for different amino acid sequences of the two catalases was found by peptide mapping with endoproteinase Glu-C, by expressing a cDNA encoding matrix catalase in Escherichia coli, and by partial amino acid sequencing of peptide fragments from 59-kDa core catalase. These results contradict the previous view that the formation of cores occurred via condensation of matrix catalase, and indicate that new concepts on the biogenesis and physiological function of plant peroxisomal cores need to be developed.

Amino Acid Sequence↗
PubMed1991

Cloning, characterization, and expression in Escherichia coli of a gene encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous to mammalian catalases.

A gene coding for catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase; EC 1.11.1.6) of the gram-positive bacterium Listeria seeligeri was cloned from a plasmid library of EcoRI-digested chromosomal DNA, with Escherichia coli DH5 alpha as a host. The recombinant catalase was expressed in E. coli to an enzymatic activity approximately 50 times that of the combined E. coli catalases. The nucleotide sequence was determined, and the deduced amino acid sequence revealed 43.2% amino acid sequence identity between bovine liver catalase and L. seeligeri catalase. Most of the amino acid residues which are involved in catalytic activity, the formation of the active center accession channel, and heme binding in bovine liver catalase were also present in L. seeligeri catalase at the corresponding positions. The recombinant protein contained 488 amino acid residues and had a calculated molecular weight of 55,869. The predicted isoelectric point was 5.0. Enzymatic and genetic analyses showed that there is most probably a single catalase of this type in L. seeligeri. A perfect 21-bp inverted repeat, which was highly homologous to previously reported binding sequences of the Fur (ferric uptake regulon) protein of E. coli, was detected next to the putative promoter region of the L. seeligeri catalase gene.

Amino Acid Sequence↗
PubMed2000

Purification and characterization of liver catalase in acatalasemic beagle dog: comparison with normal dog liver catalase.

Catalase from acatalasemic dog liver was purified to homogeneity and its properties were compared with those of normal dog liver catalase. The purified acatalasemic and normal dog liver catalases were found to have the same molecular weight (230,000 Da) and isoelectric point (pI: 6.0-6.2) and both enzymes contained four hematins per molecule. The catalytic activity of catalase from acatalasemic dog was normal. Furthermore, there was no difference between the acatalasemic and normal dog catalases in the binding affinity to NADPH (apparent Kd: 0.11-0.12 microM) and in the sensitivity to oxidative stress by hydrogen peroxide, the normal substrate of catalase. The acatalasemic dog enzyme was stable only in a narrow pH range (pH 6-9) although the normal enzyme was stable in a wide pH range (pH 4-10). Acatalasemic dog liver catalase also showed a slight low thermal stability at 37 degrees C and the heat-lability was remarkable at 45 degrees C, compared to the normal dog enzyme. These results indicated that the acatalasemic dog catalase is catalytically normal although it is associated with an unstable molecular structure.

Acatalasia↗
PubMed2001

Identification of catalase-like activity from Mycobacterium leprae and the relationship between catalase and isonicotinic acid hydrazide (INH).

As Mycobacterium leprae proliferate inside macrophages, it has been speculated that catalase encoded by katG may protect the bacilli from deleterious effects of peroxide generated from the macrophage and may also play a crucial role in the survival of M. leprae in vivo. However, unlike that of M. tuberculosis, the katG of M. leprae has been reported to be a pseudogene, implicating that isoniazid, which is activated to a potent tuberculocidal agent by catalase, is unlikely to be of therapeutic benefit to leprosy patients. These results raise a question as to how M. leprae avoids H202-mediated killing inside macrophages. To understand the survival of M. leprae in macrophages, the present study attempted to detect catalase-like activity in M. leprae. Catalase-like activity was found in M. leprae cell lysate by the diaminobenzidine (DAB) staining method with non-denaturing polyacrylamide gel electrophoresis. An ammonium sulphate precipitation study revealed that the catalase-like activity was precipitable with 80% ammonium sulphate. The effect of isoniazid (INH) on M. leprae growth was also tested by RT-PCR and radiorespirometric assay to examine catalase-like activity in M. leprae, because INH was activated by catalase. It was found that the viability of M. leprae was decreased at a concentration of 20 microg/ml by radiorespirometric assay and it was inhibited at higher concentrations as determined by RT-PCR. These data suggest that a catalase-like activity other than that encoded by katG is present in M. leprae.

Ammonium Sulfate↗
PubMed1993

Differences in the rate of intracellular killing of catalase-negative and catalase-positive Listeria monocytogenes by normal and interferon-gamma-activated macrophages.

Intracellular killing of catalase-positive bacteria by murine resident macrophages requires the presence of extracellular serum, whereas killing of catalase-negative bacteria can occur in the absence of serum. To find out whether the intracellular killing of bacteria by rIFN-gamma-activated macrophages also requires serum stimulation, we investigated the handling of ingested catalase-negative and -positive Listeria monocytogenes by peritoneal macrophages of normal Swiss mice and mice injected i.p. with 1 x 10(4) U rIFN-gamma 18 h earlier. In the absence of extracellular serum, rIFN-gamma-activated macrophages killed ingested catalase-negative Listeria more efficiently (P < 0.01) than normal resident macrophages. Maximal killing of catalase-negative bacteria by rIFN-gamma-activated macrophages required an extracellular serum concentration of only 1.0 to 2.5% compared with the 10% needed by normal macrophages. No differences were observed in the rates of intracellular killing of catalase-positive Listeria by rIFN-gamma-activated and normal resident macrophages: both populations of macrophages required 10% extracellular serum for maximal killing of these bacteria, and killing was minimal in the absence of serum. The rIFN-gamma-activated macrophages displayed enhanced O2-consumption after stimulation with phorbol myristate acetate and heat-killed Listeria compared with macrophages from normal mice. These findings indicate that, under suboptimal stimulation by extracellular serum, rIFN-gamma enhances the intracellular killing of catalase-negative Listeria which lack endogenous catalase acting as a scavenger of reactive oxygen intermediates. The mechanism underlying the enhancement is probably the amplification of the respiratory burst by IFN-gamma.

Animals↗