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PubMed2002

The impact of catalase expression on the replicative lifespan of Saccharomyces cerevisiae.

The role of catalase on Saccharomyces cerevisiae replicative lifespan was investigated using a wild-type haploid laboratory yeast W303a, a catalase A mutant, a catalase T mutant and an acatalasaemic mutant. Lifespan analysis was performed in two different environmental conditions. Under repressing conditions, on glucose media, catalase T activity, but not catalase A activity was necessary to assure longevity. However, under derepressing conditions, on ethanol media, both catalases were required for longevity assurance. Although catalase activity and carbon source influence yeast lifespan, the relationship between oxidative defence and replicative senescence is complex.

Catalase↗
PubMed1994

The damaging effect of UV rays (with the wavelength shorter than 320 nm) on the rabbit anterior eye segment. I. Early changes and their prevention by catalase-aprotinin application.

In experiments carried out in rabbit eyes, UV rays of 254 or 312 nm wavelength damaged the anterior eye segment, whereas those of 365 nm wavelength did not. Two min irradiation with 254 nm UV rays led to a decrease of catalase activity in the corneal epithelium. After 5 min irradiation the catalase activity in the epithelium was not detectable at all. Catalase activity was also diminished in the corneal endothelium and lens epithelium. In this stage the changes were accompanied by decreased activities of Na(+)--K(+)-dependent adenosine triphosphatase, gamma-glutamyl transpeptidase and increased activities of lysosomal enzymes in the corneal and lens epithelium as well as in the corneal endothelium. The transparency of the cornea and lens was decreased. Plasmin activity appeared in the tear fluid. The irradiation with UV rays of 312 nm caused similar disturbances, however, a longer exposure was necessary. In contrast, irradiation with UV rays of 365 nm did not produce any changes. The described corneal disturbances were prevented by dropping of catalase solution on the eye surface during the irradiation or shortly after it. However, after a protracted irradiation aprotinin had to be added to catalase to achieve the healing. The decrease of catalase activity and its prevention by a local application of catalase suggests a key role of oxyradicals in the damage of the eye by UV rays.

Animals↗
PubMed1978

Immunochemical specificity of a benzidine technique proposed to catalases histochemical detection.

As an attempt to test the specificity of an histochemical technique proposed to detect catalases, an investigation was carried out by immunochemical techniques. Purified catalases were used after analysed immunochemically by double immune diffusion test and immunoelectrophoretic technique. These pure catalases induced, after injecting into guinea-pigs, anti-serums that react specifically with catalase and does not give any cross reaction with peroxidases and haemic iron containing compounds. By the direct and indirect immuno-fluorescence techniques it was shown an intense catalase reactivity inside the cytoplasm of adrenal cortex and hepatic cells, that appears as a granular pattern. These results are very similar to those provided by the histochemical technique, either concerning to the reactive cells or to the granular pattern of the positive reaction. In such instances, the immunochemical results suggest the specificity of the histochemical reaction. This specificity is confirmed by the previous treatment of tissue sections by catalases anti-serum. After this treatment either the immunochemical or the histochemical technique to detect catalases provide negative results on cells that before the treatment were strongly reactive.

Adrenal Cortex↗
PubMed1999

Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis.

This review gives an overview about the structural organisation of different evolutionary lines of all enzymes capable of efficient dismutation of hydrogen peroxide. Major potential applications in biotechnology and clinical medicine justify further investigations. According to structural and functional similarities catalases can be divided in three subgroups. Typical catalases are homotetrameric haem proteins. The three-dimensional structure of six representatives has been resolved to atomic resolution. The central core of each subunit reveals a characteristic "catalase fold", extremely well conserved among this group. In the native tetramer structure pairs of subunits tightly interact via exchange of their N-terminal arms. This pseudo-knot structures implies a highly ordered assembly pathway. A minor subgroup ("large catalases") possesses an extra flavodoxin-like C-terminal domain. A > or = 25 A long channel leads from the enzyme surface to the deeply buried active site. It enables rapid and selective diffusion of the substrates to the active center. In several catalases NADPH is tightly bound close to the surface. This cofactor may prevent and reverse the formation of compound II, an inactive reaction intermediate. Bifunctional catalase-peroxidase are haem proteins which probably arose via gene duplication of an ancestral peroxidase gene. No detailed structural information is currently available. Even less is know about manganese catalases. Their di-manganese reaction centers may be evolutionary.

Amino Acid Sequence↗
PubMed2000

Lead acetate potentiates brain catalase activity and enhances ethanol-induced locomotion in mice.

Several reports have demonstrated that acute lead acetate administration enhances brain catalase activity in animals. Other reports have shown a role of brain catalase in ethanol-induced behaviors. In the present study we investigated the effect of acute lead acetate on brain catalase activity and on ethanol-induced locomotion, as well as whether mice treated with different doses of lead acetate, and therefore, with enhanced brain catalase activity, exhibit an increased ethanol-induced locomotor activity. Lead acetate or saline was injected IP in Swiss mice at doses of 50, 100, 150, or 200 mg/kg. At 7 days following this treatment, ethanol (0.0, 1.5, 2.0, 2.5, or 3.0 g/kg) was injected IP, and the animals were placed in the open-field chambers. Results indicated that the locomotor activity induced by ethanol was significantly increased in the groups treated with lead acetate. Maximum ethanol-induced locomotor activity increase was found in animals treated with 100 mg/kg of lead acetate and 2.5 g/kg of ethanol. Total brain catalase activity in lead-pretreated animals also showed a significant induction, which was maximum at 100 mg/kg of lead acetate treatment. No differences in blood ethanol levels were observed among treatment groups. The fact that brain catalase and ethanol-induced locomotor activity followed a similar pattern could suggest a relationship between both lead acetate effects and also a role for brain catalase in ethanol-induced behaviors.

Animals↗
PubMed1998

Primary sequence and activity analyses of a catalase from Ascaris suum.

A complete cDNA encoding the catalase (EC 1.11.1.6) has been isolated from the parasitic nematode Ascaris suum (AsCAT). The active-site residues, the residues involved in ligand interaction, and NADPH-binding residues of the bovine liver catalase-type enzyme are highly conserved in the AsCAT predicted amino acid sequence. To confirm that the AsCAT cDNA encodes a functional enzyme, active recombinant protein (rAsCAT) was produced in a procaryotic expression system. The subunit molecular mass of the purified recombinant protein (rAsCAT) was determined to be approximately 60 kDa. According to gel filtration, the molecular mass of the active enzyme is 240 kDa, indicating that the catalase subunits form a homotetramer in solution. The optical spectrum of rAsCAT shows a typical ferric haem spectrum with a Soret band at 407 nm. Fluorescence spectroscopy demonstrates that rAsCAT binds NADPH. rAsCAT has catalase activity with hydrogen peroxide over a broad pH range, with a specific activity of 37,800 U mg-1. In addition to its catalase activity, rAsCAT displays peroxidase activity using the substrates t-butyl hydroperoxide and o-dianisidine. The haem ligands NaN3 and KCN caused a 50% inhibition of catalase activity at 9 and 19 microM, respectively. In the presence of a H2O2-generating system, catalase activity of rAsCAT was inhibited by 3-aminotriazole, phenolic compounds, and drugs.

Amino Acid Sequence↗
PubMed2000

Common phylogeny of catalase-peroxidases and ascorbate peroxidases.

Catalase-peroxidases belong to Class I of the plant, fungal, bacterial peroxidase superfamily, together with yeast cytochrome c peroxidase and ascorbate peroxidases. Obviously these bifunctional enzymes arose via gene duplication of an ancestral hydroperoxidase. A 230-residues long homologous region exists in all eukaryotic members of Class I, which is present twice in both prokaryotic and archaeal catalase-peroxidases. The overall structure of eukaryotic Class I peroxidases may be retained in both halves of catalase-peroxidases, with major insertions in several loops, some of which may participate in inter-domain or inter-subunit interactions. Interspecies distances in unrooted phylogenetic trees, analysis of sequence similarities in distinct structural regions, as well as hydrophobic cluster analysis (HCA) suggest that one single tandem duplication had already occurred in the common ancestor prior to the segregation of the archaeal and eubacterial lines. The C-terminal halves of extant catalase-peroxidases clearly did not accumulate random changes, so prolonged periods of independent evolution of the duplicates can be ruled out. Fusion of both copies must have occurred still very early or even in the course of the duplication. We suggest that the sparse representatives of eukaryotic catalase-peroxidases go back to lateral gene transfer, and that, except for several fungi, only single copy hydroperoxidases occur in the eukaryotic lineage. The N-terminal halves of catalase-peroxidases, which reveal higher homology with the single-copy members of the superfamily, obviously are catalytically active, whereas the C-terminal halves of the bifunctional enzymes presumably control the access to the haem pocket and facilitate stable folding. The bifunctional nature of catalase-peroxidases can be ascribed to several unique sequence peculiarities conserved among all N-terminal halves, which most likely will affect the properties of both haem ligands.

Amino Acid Motifs↗
PubMed2000

Expression analysis and characterization of the mutant of a growth-phase- and starvation-regulated monofunctional catalase gene from Xanthomonas campestris pv. phaseoli.

Analysis of the Xanthomonas campestris pv. phaseoli (Xp) catalase profile using an activity gel revealed at least two distinct monofunctional catalase isozymes denoted Kat1 and Kat2. Kat1 was expressed throughout growth, whereas Kat2 was expressed only during the stationary phase of growth. The nucleotide sequence of a previously isolated monofunctional catalase gene, Xp katE, was determined. The deduced amino acid sequence of Xp KatE showed a high percentage identity to an atypical group of monofunctional catalases that includes the well-characterized E. coli katE. Expression of Xp katE was growth phase-dependent but was not inducible by oxidants. In addition, growth of Xp in a carbon-starvation medium induced expression of the gene. An Xp katE mutant was constructed, and analysis of its catalase enzyme pattern showed that Xp katE coded for the Kat2 isozyme. Xp katE mutant had resistance levels similar to the parental strain against peroxide and superoxide killing at both exponential and stationary phases of growth. Interestingly, the level of total catalase activity in the mutant was similar to that of the parental strain even in stationary phase. These results suggest the existence of a novel compensatory mechanism for the activity of Xp catalase isozymes.

Catalase↗
PubMed1999

Effects of chronic lead administration on ethanol-induced locomotor and brain catalase activity.

Several reports have demonstrated that chronic lead administration decreases brain catalase activity in animals. Other reports have shown a role of brain catalase on ethanol-induced behaviors. In the present study, we questioned whether mice treated chronically with lead, and therefore functionally devoid of brain catalase activity, exhibit some alterations in ethanol-induced behaviors. Swiss-Webster mice were exposed to drinking fluid containing either 500 ppm lead acetate or sodium acetate (control group) for 0, 15, 30, or 60 days before an acute ethanol administration. Following ethanol injection (2.5 g/kg, i.p.), animals were placed in open field chambers and locomotor activity was measured. Lead exposure had no effect on spontaneous locomotor activity. However, a reduction in ethanol-induced locomotor activity was found at all periods of lead exposure. After 60 days of treatment, the lead group demonstrated 35% less activity than the control group. Brain catalase activity was significantly reduced in the lead group following 60 days of exposure. This reduction in ethanol-induced locomotor activity and in brain catalase activity persisted after 40 days of lead withdrawal. The fact that brain catalase and ethanol-induced locomotor activity followed a similar pattern could suggest a relationship between both lead acetate effects and also a role for brain catalase in ethanol-induced behaviors.

Animals↗
PubMed1986

Immunogenicity of polyethylene glycol-modified superoxide dismutase and catalase.

Modification of proteins with polyethylene glycol (PEG) has been shown to result in a decrease in immunogenicity. Superoxide dismutase (SOD) and catalase were modified with PEG and used to immunize mice. Antibody titers against the antigens were determined by ELISA. Mice immunized with PEG-SOD had antibody titers 0.03%-0.07% of that seen in mice with SOD, while mice immunized with PEG-catalase developed titers 0.02%-0.09% of that seen in mice with catalase. The modified enzymes retained the ability to react with preformed antibodies to the unmodified antigens. Antibodies to SOD reacted equally well with the PEG-SOD or SOD antigen. Antibodies to catalase reacted to PEG-catalase but at only 0.02% of the reaction with catalase antigen. In reciprocal studies, antisera against the PEG-proteins failed to react to an appreciable level with the corresponding unmodified protein. Modification with PEG resulted in a decrease in immunogenicity of both SOD and catalase.

Animals↗
PubMed2000

Levels of DNA damage are unaltered in mice overexpressing human catalase in nuclei.

Two types of transgenic mice were generated to evaluate the role of hydrogen peroxide in the formation of nuclear DNA damage. One set of lines overexpresses wild-type human catalase cDNA, which is localized to peroxisomes. The other set overexpresses a human catalase construct that is targeted to the nucleus. Expression of the wild-type human catalase transgene was found in liver, kidney, skeletal muscle, heart, spleen, and brain with muscle and heart exhibiting the highest levels. Animals containing the nuclear-targeted construct had a similar pattern of expression with the highest levels in muscle and heart, but with lower levels in liver and spleen. In these animals, immunofluorescence detected catalase present in the nuclei of kidney, muscle, heart, and brain. Both types of transgenic animals had significant increases of catalase activities compared to littermate controls in most tissues examined. Despite enhanced activities of catalase, and its presence in the nucleus, there were no changes in levels of 8OHdG, a marker of oxidative damage to DNA. Nor were there differences in mutant frequencies at a Lac Z reporter transgene. This result suggests that in vivo levels of H(2)O(2) may not generate 8OHdG or other types of DNA damage. Alternatively, antioxidant defenses may be optimized such that additional catalase is unable to further protect nuclear DNA against oxidative damage.

8-Hydroxy-2'-Deoxyguanosine↗
PubMed2001

Crystal structure of manganese catalase from Lactobacillus plantarum.

BACKGROUND: Catalases are important antioxidant metalloenzymes that catalyze disproportionation of hydrogen peroxide, forming dioxygen and water. Two families of catalases are known, one having a heme cofactor, and the other, a structurally distinct family containing nonheme manganese. We have solved the structure of the mesophilic manganese catalase from Lactobacillus plantarum and its azide-inhibited complex. RESULTS: The crystal structure of the native enzyme has been solved at 1.8 A resolution by molecular replacement, and the azide complex of the native protein has been solved at 1.4 A resolution. The hexameric structure of the holoenzyme is stabilized by extensive intersubunit contacts, including a beta zipper and a structural calcium ion crosslinking neighboring subunits. Each subunit contains a dimanganese active site, accessed by a single substrate channel lined by charged residues. The manganese ions are linked by a mu1,3-bridging glutamate carboxylate and two mu-bridging solvent oxygens that electronically couple the metal centers. The active site region includes two residues (Arg147 and Glu178) that appear to be unique to the Lactobacillus plantarum catalase. CONCLUSIONS: A comparison of L. plantarum and T. thermophilus catalase structures reveals the existence of two distinct structural classes, differing in monomer design and the organization of their active sites, within the manganese catalase family. These differences have important implications for catalysis and may reflect distinct biological functions for the two enzymes, with the L. plantarum enzyme serving as a catalase, while the T. thermophilus enzyme may function as a catalase/peroxidase.

Azides↗
PubMed1975

Optical and magnetic resonance studies of formate binding to horse liver catalase and sperm whale myoglobin.

The binding of formate ion, a substrate for the peroxidatic reaction of catalase, has been investigated by magnetic resonance techniques. Comparative studies of formate binding to ferric myoglobin have also been performed. The nuclear magnetic relaxation (NMR) rate of formate and water protons is enhanced by the presence of ferric horse liver catalase. The enhancement is not changed significantly by the addition of cyanide, indicating that water and formate are still bound in the presence of cyanide. Formate proton to heme iron distances determined by magnetic resonance techniques indicate that formate does not directly bind to the heme iron of catalase or myoglobin but to the globin, and NMR relaxation occurs as a result of outersphere mechanisms. Evidence that water forms an innersphere complex with the iron atom of the catalase heme is presented. In similar experiments with ferric myoglobin, the addition of cyanide caused a large decrease in the enhancement of the proton relaxation rate of both formate and water, indicating the displacement of water and formate from the heme and the vicinity of the heme, respectively. Broad, high-spin, ferric ion electron paramagnetic resonance absorptions of catalase and myoglobin at room temperature obtained in the presence and absence of formate show that formate does not alter appreciably the heme environment of catalase or myoglobin or the spin state of the heme iron. Studies on the binding of formate to catalase as monitored by changes in the heme absorption spectrum in the visible region show one-to-one stoichiometry with heme concentration. However, the small changes observed in the visible region of the optical spectrum on addition of formate ion are attributed to a secondary effect of formate on the heme environment, rather than direct binding of formate to the heme moiety.

Animals↗
PubMed2001

Potential application of catalase-peroxidase from Comamonas terrigena N3H in the biodegradation of phenolic compounds.

Comamonas terrigena N3H is a gram-negative rod-shaped bacterium that was isolated from contaminated soil in Slovakia. This bacterium showed remarkable biodegradation properties. We investigated the expression and functioning of two catalase isozymes in this bacterium. The typical catalase could be induced by cadmium ions, whereas the catalase-peroxidase enzyme was constitutively expressed. Since C. terrigena lacks the key enzyme for complete degradation of phenols (phenolhydroxylase), we analysed the possible removal of phenol by the two catalases of this bacterium. Addition of phenol to the culture medium led to increased expression of the catalase-peroxidase. Applying oxidative stress prior to phenol administration markedly induced the expression of the typical catalase, irrespective of the nature of the added agent. Thus, the rate of phenol degradation is rather reduced under these conditions, while growth of the cells is not impaired. We concluded that phenol peroxidation in C. terrigena can be largely attributed to the action of a catalase-peroxidase. The potential application of this enzyme in the removal of phenol from the environment is discussed.

Biodegradation, Environmental↗
PubMed2001

Selective sensitization of bacteria to peroxide damage associated with fluoride inhibition of catalase and pseudocatalase.

Fluoride and sulfide are known inhibitors of heme catalases in acid environments. Staphylococcus aureus H cells were found to be sensitized by fluoride or sulfide to H2O2 killing at acid pH values in the range of 3.5 to 4.0, and catalase activity was reduced concomitantly. In contrast, fluoride had little effect on H2O2 killing of Streptococcus mutans GS-5, which has fluoride-insensitive peroxidase activity, but still is more sensitive to H2O2 than is S. aureus in the absence of fluoride. Fluoride but not sulfide was inhibitory also for the Mn-containing, non-heme pseudocatalase of Lactobacillus plantarum ATCC 14431 over a wide pH range, and this inhibitory effect was reflected in enhanced H2O2 killing in the presence of fluoride. In addition, we found that catalase-positive S. aureus or Neisseria sicca could protect catalase-negative S. mutans against killing by H2O2 in mixed suspensions, but protection was compromised by fluoride or sulfide under acid conditions. Thus, catalase-positive organisms could protect a catalase-negative organism against peroxide damage, but inhibition of catalase reduced protection. These findings are pertinent to the widespread use of fluoride and peroxide in oral health care products.

Acids↗
PubMed1988

Purification and biosynthesis of cottonseed (Gossypium hirsutum L.) catalase.

As part of our research on peroxisome biogenesis, catalase was purified from cotyledons of dark-grown cotton (Gossypium hirsutum L.) seedlings and monospecific antibodies were raised in rabbits. Purified catalase appeared as three distinct electrophoretic forms in non-denaturing gels and as a single protein band (with a subunit Mr of 57,000) on silver-stained SDS/polyacrylamide gels. Western blots of crude extracts and isolated peroxisomes from cotton revealed one immunoreactive polypeptide with the same Mr (57,000) as the purified enzyme, indicating that catalase did not undergo any detectable change in Mr during purification. Synthesis in vitro, directed by polyadenylated RNA isolated from either maturing seeds or cotyledons of dark-grown cotton seedlings, revealed a predominant immunoreactive translation product with a subunit Mr of 57,000 and an additional minor immunoreactive product with a subunit Mr of 64000. Labelling studies in vivo revealed newly synthesized monomers of both the 64000- and 57,000-Mr proteins present in the cytosol and incorporation of both proteins into the peroxisome without proteolytic processing. Within the peroxisome, the 57,000-Mr catalase was found as an 11S tetramer; whereas the 64,000-Mr protein was found as a relatively long-lived 20S aggregate (native Mr approx. 600,000-800,000). The results strongly indicate that the 64,000-Mr protein (catalase?) is not a precursor to the 57,000-Mr catalase and that cotton catalase is translated on cytosolic ribosomes without a cleavable transit or signal sequence.

Catalase↗
PubMed1999

Catalase gene is associated with facial eczema disease resistance in sheep.

Facial eczema (FE) is a hepatogenous photosensitization disease of ruminant animals, particularly in sheep which vary widely in their susceptibility to the disease. The liver damage is caused by the mycotoxin, sporidesmin. There is evidence that the toxicity of sporidesmin is due to its ability to generate 'active oxygen' species. We evaluated the catalase gene, which encodes an enzyme with antioxidant functions, as a candidate for determining the susceptibility of sheep to the disease. Two microsatellite markers, OarSHP3 and OarSHP4, which flank the sheep catalase gene, were isolated from a Yeast Artificial Chromosome (YAC) clone. These markers mapped the catalase locus by linkage to ovine chromosome 15. Eleven informative markers spaced throughout chromosome 15, inclusive of the catalase marker OarSHP4, gave no significant linkage with the disease traits when analysed in four outcross resource pedigrees. However, OarSHP3 and OarSHP4 allele frequencies showed significant differences between FE resistant and susceptible selection-lines. Comparison of sequences of catalase cDNAs from sheep of resistant and susceptible lines showed only two silent mutations. A single nucleotide polymorphisms (KP1) in exon 6 of the catalase gene also showed significant differences in allele frequencies between the selection lines. The lack of evidence for linkage in outcross pedigrees, but the significant association in the genetic lines, implies that catalase is involved in determining the susceptibility of sheep to facial eczema, and that the candidate gene's effect is probably recessive or minor.

Alleles↗
PubMed1978

Synthesis of catalase in two cell-free protein-synthesizing systems and in rat liver.

Rat liver polysomal RNA was translated in the rabbit reticulocyte lysate and in the wheat germ cell-free protein-synthesizing systems, using [(35)S]methionine as label. The catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase, EC 1.11.1.6) that was synthesized was isolated by immunoprecipitation and characterized by electrophoresis in sodium dodecyl sulfate/polyacrylamide gels followed by fluorography. The catalase made in both systems migrated more slowly during electrophoresis than did purified peroxisomal catalase. By comparison with standards of known molecular mass, the cell-free products were estimated to be about 4000 daltons larger than the purified enzyme. We also investigated the biosynthesis of catalase in vivo by injecting [(35)S]methionine into rats. The precursor of catalase known to be synthesized in liver and found in the high-speed supernatant 8 min later [Lazarow, P. B. & de Duve, C. (1973) J. Cell Biol. 59, 491-506] was isolated immunochemically. For comparison, 1-day-old completed catalase was immunoprecipitated from peroxisomes. The migrations in sodium dodecyl sulfate gels of the 8-min-old precursor and the subunit of the day-old enzyme were indistinguishable and approximately the same as the migration of the cell-free products. These results indicate that catalase's apparent size does not change when it enters peroxisomes but rather decreases during the chemical purification procedure.

Animals↗