Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.11.1.6 (catalase)
 55,569 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Three strains of Escherichia coli differing only in the catalase locus mutated by transposon Tn10 were constructed. These strains produced only catalase HPI (katE::Tn10 and katF::Tn10 strains) or catalase HPII (katG::Tn10). HPI levels increased gradually about twofold during logarithmic growth but did not increase during growth into stationary phase in rich medium. HPII levels, which were initially threefold lower than HPI levels, did not change during logarithmic growth but did increase tenfold during growth into stationary phase. HPI levels increased in response to ascorbate or H2O2 being added to the medium but HPII levels did not. In minimal medium, any carbon source derived from the tricarboxylic acid cycle caused five- to tenfold higher HPII levels during logarithmic growth but had very little effect on HPI levels. Active electron transport did not affect either HPI or HPII levels.
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PMID:Catalases HPI and HPII in Escherichia coli are induced independently. 390 30

A class of catalase-deficient mutants that was unlinked to katE was localized between mutS and cys at 59.0 min on the Escherichia coli genome. This locus was named katF. Transposon Tn10 insertions were isolated that mapped in both katE and katF loci. The catalase species present in katE+ and katF+ recombinants was found to be different from the main catalase activities, HPI and HPII, in several respects. It did not have an associated peroxidase activity; it was electrophoretically slower on native polyacrylamide gels; it eluted from DEAE-Sephadex A50 at a higher salt concentration; its Km for H2O2 was 30.9 mM as compared with 3.7 mM for HPI and HPII; its synthesis was not induced by ascorbate; and it did not cross react with HPI-HPII antisera. This new catalase was labeled HPIII.
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PMID:Genetic mapping of katF, a locus that with katE affects the synthesis of a second catalase species in Escherichia coli. 609 82

The phytophathogenic, gram-negative bacterium Pseudomonas syringae pv. syringae 61 contains three isozymes of catalase (EC 1.11.1.6), which have been proposed to play a role in the bacterium's responses to various environmental stresses. To study the role of individual isozymes, the gene coding for the catalytic subunit of one catalase isozyme was cloned from a cosmid library hosted in Escherichia coli DH5 alpha by using a designed catalase-specific DNA probe for the screening. One out of four clones with a catalase-positive genotype was subcloned and a pUC19-based 2.7 x 10(3)-base (2.7-kb) insert subclone, pMK3E5, was used to transform catalase-deficient E. coli strain UM255 (HPI-, HPII-). The transformants contained a single isozyme of catalase that had electrophoretic and enzymic properties similar to catalase isozyme CatF from P. syringae pv. syringae 61. Analysis of the sequenced 2.7-kb insert DNA revealed six putative open-reading frames (ORF). The 1542-base-pair DNA sequence of ORF2, called catF, encodes a peptide of 513 amino acid residues with a calculated molecular mass of 66.6 kDa. The amino acid sequence deduced from catF had homology to the primary structure of true catalases from mammals, plants, yeasts and bacteria. The activity of the recombinant catalase was inhibited by 3-amino-1,2,4-triazole and azide and stimulated by chloramphenicol. The N terminus contained a signal sequence of 26 amino acids necessary for secretion into the periplasm, a so-far unique property of Pseudomonas catalases.
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PMID:Cloning, characterization and phenotypic expression in Escherichia coli of catF, which encodes the catalytic subunit of catalase isozyme CatF of Pseudomonas syringae. 754 3

Sophisticated biochemical networks allow organisms such as bacteria and insects to switch from very rapid growth and development in ideal environments to dormancy during severely unfavorable conditions. These switches may be accompanied by abrupt changes in oxidation/reduction involving reactive oxygen species (ROS). ROS have the potential of damaging nucleic acids, proteins, and membranes. In Escherichia coli, certain genetically regulated circuits (regulons) turn on synthesis of anti-oxidant enzymes to protect against distinct ROS excesses (superoxide, hydrogen peroxide, organic or lipid peroxides, etc.). As examples, the soxRS regulon controls synthesis of Mn-superoxide dismutase, oxyR controls catalase HPI, rpoS positively regulates HPII, and fur regulates several oxidative reactions that involve iron uptake. Our studies have focused on the regulatory role of rpoS, known to be a sigma factor (sigma 38) that combines with RNA polymerase and is a regulator of those gene products needed to protect cells during dormancy. Since insect cells, during both active growth and dormancy, endure severe environments, analogous protective gene products may be induced. Examples are presented of insect anti-oxidant metabolism, including those involved in the aging process. In addition, we searched several DNA and protein sequence data banks to compare resemblances between anti-oxidant gene products of bacteria and insects.
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PMID:Genetic mechanisms involved in cellular recovery from oxidative stress. 760 42

Pathogenic microorganisms possess antioxidant defense mechanisms for protection from reactive oxygen metabolites such as hydrogen peroxide (H2O2), which are generated during the respiratory burst of phagocytic cells. These defense mechanisms include enzymes such as catalase, which detoxify reactive oxygen species, and DNA repair systems which repair damage resulting from oxidative stress. To determine the relative importance of these two potentially protective defense mechanisms against oxidative stress encountered by Salmonella during infection of the host, a Salmonella typhimurium double mutant unable to produce either the HPI or HPII catalase was constructed, and compared with an isogenic recA mutant deficient in DNA repair. The recA mutant was hypersusceptible to H2O2 at low cell densities in vitro, while the catalase mutant was more susceptible to high H2O2 concentrations at high cell densities. The catalase mutant was found to be resistant to macrophages and retained full murine virulence, in contrast to the recA mutant which previously was shown to be macrophage-sensitive and attenuated in mice. These observations suggest that Salmonella is subjected to low concentrations of H2O2 while at relatively low cell density during infection, conditions requiring an intact DNA repair system but not functional catalase activity.
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PMID:DNA repair is more important than catalase for Salmonella virulence in mice. 788 91

We present evidence showing that rpoS (katF) is a regulator of katG gene transcription in an oxyR-independent manner. Mutation of the rpoS gene in several different Escherichia coli strains caused a significant reduction in catalase HPI activity. In rpoS-delta oxyR double mutants, the level of HPI was considerably lower compared to the delta oxyR parent strain, and was restored when transformed with an rpoS+ plasmid. Overproduction of HPI in oxyR- suppressor strains was greatly diminished after inactivation of the rpoS gene and was accompanied by a substantial increase in sensitivity to menadione. Beta-galactosidase expression from a katG::lacZ promoter was lower in rpoS strains compared to rpoS+ isogenic parents. Several delta oxyR strains had detectable levels of katG transcription that was significantly diminished after rpoS gene inactivation.
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PMID:Role of rpoS (katF) in oxyR-independent regulation of hydroperoxidase I in Escherichia coli. 793 80

The effects of near ultraviolet (NUV) light on a NUV chromophore-containing oxidant-sensitive enzyme, dihydroxyacid dehydratase (DHAD), were measured in seven strains of Escherichia coli. The strains differed in production of the oxidant-defense enzymes, superoxide dismutases (Fe-SOD and Mn-SOD), and catalases HPI and HPII. With the stress of aerobic growth but without NUV exposure, the strains lacking either Fe or Mn SOD or both SODs had 57%, 25%, and 12%, respectively, of the DHAD-specific activity of the parent (K12) strain. Under the same conditions, the catalase strains that were wild type, overproducing, and deficient had comparable DHAD-specific activities. When aerobic cultures were exposed for 30 min to NUV with a fluence of 216 J/m2/s at 310-400 nm, the percentage decreases in DHAD-specific activities were similar (ranging from 75% to 89%) in strains with none, either, or both SODs missing, and in the catalase-overproducing strain. However, the decreases were only 58% and 52% in the strain with catalase missing and in its parent, respectively. The NUV-induced loss of DHAD enzyme activity was not accompanied by any detectable loss of the DHAD protein as measured by polyclonal antibody to DHAD.
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PMID:Near ultraviolet light inactivation of dihydroxyacid dehydratase in Escherichia coli. 839 20

Disseminated Mycobacterium avium-Mycobacterium intracellulare disease is a prevalent opportunistic infection in patients with acquired immune deficiency syndrome (AIDS). These pathogens are generally resistant to isoniazid (INH), a powerful antituberculosis drug. It is now generally accepted that the INH susceptibility of Mycobacterium tuberculosis results from the transformation of the drug into a toxic derivative, as a result of the action of the enzyme catalase-peroxidase (HPI), encoded by the katG gene. It has been speculated that the presence of a second catalase (HPII) in some mycobacterial species, but lacking in M. tuberculosis, may impair the action of INH. In this report, the nucleotide sequence of the M. avium katE gene, encoding catalase HPII, is described. This enzyme shows strong similarity to Escherichia coli catalase HPII and eukaryotic catalases. All amino acids previously postulated as participating directly in catalysis by liver catalase and most of the amino acids binding the prosthetic group are conserved in M. avium catalase HPII. The enzyme is expressed in E. coli and is inhibited by 3-amino-1,2,4-triazole (AT). Furthermore, Southern blot hybridizations and polymerase chain reaction experiments demonstrate the distribution of katE gene in several mycobacterial species. To evaluate the potentially antagonistic effect of HPII catalase on INH susceptibility, the katE gene was transformed into M. tuberculosis H37Rv and the minimum inhibitory concentration (MIC) for INH was determined. Despite strong expression of the katE gene, no change in MIC was observed, thus ruling out a possible contribution of this enzyme to the natural resistance of M. avium to the drug. The availability of the gene probe, encoding the second mycobacterial catalase HPII, should open the way for the development of new drugs and diagnostic tests to combat drug-resistant pathogen strains.
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PMID:The katE gene, which encodes the catalase HPII of Mycobacterium avium. 882 41

Escherichia coli produces two catalases or hydroperoxidases, HPI and HPII. HPI is a bifunctional catalase-peroxidase active as a tetramer of identical 80049-Da subunits encoded by katG. The expression of katG is controlled at the basal level by sigma s (KatF), and its induction by H2O2 is regulated by OxyR. HPII is a monofunctional catalase active as a tetramer of identical 84118-Da subunits encoded by katE. The induction of katE expression in the stationary phase is controlled by sigma s. The core of HPII is similar in sequence to other catalases including the conservation of several residues that have been implicated as playing a catalytic role, His128, Asn201, Ser167 and Tyr415. These residues have served as targets for site-directed mutagenesis in a study that has demonstrated their role in the catalytic mechanism of HPII. In addition, the two Cys residues in HPII have been targeted in a similar study revealing that they do not have a catalytic role, but that Cys438 is blocked by a novel modification. Despite many structural similarities to bovine liver catalase, the heme component of HPII has proved to be quite different. The presence of a cis heme d was determined spectrally and chromatographically, and the inability of certain mutants to generate the modified heme revealed that it was HPII itself that was catalysing the oxidation of heme b to heme d. The recent solution of the crystal structure of HPII and mass spectrometry have revealed that the heme d bound to HPII is a spirolactone structure with a cis orientation of the oxygens on the proximal side of the heme. This has created the problem of explaining how the oxidation of the heme can occur on the opposite side of the heme ring, remote from the catalytic residues.
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PMID:Probing the structure of catalase HPII of Escherichia coli--a review. 895 27

It has long been known that almost all isoniazid (INH) resistant mycobacteria lose the catalase and peroxidase activities along with reduced or no virulence for guinea pigs. Recently resistance to INH has become known to be associated with mutations of katG gene encoding the HPI (Hydroperoxidase I) type catalase and peroxidase. Among these mutations, the point mutation of codon 463 of katG gene is found frequently, and is suggested as being associated with INH resistance. Therefore we performed this study in order to confirm the correlation between the point mutation of codon 463 of the katG gene and INH resistance of M. tuberculosis in Korea. Fifty isolates, 32 of which were resistant to INH, and 18 of which were sensitive to INH, were selected for this study. We used PCR-SSCP and RFLP analysis to detect the point mutation of the codon 463 of katG gene and confirmed the CGG (arginine) to CTG (leucine) mutation by direct sequencing analysis. Among 32 resistant isolates, 7 isolates (22%) had the same restriction pattern compared with that of the reference strain (H37Rv), and 25 isolates (78%) showed a different restriction pattern. Among 18 sensitive isolates, 7 isolates (39%) had the same restriction pattern compared with that of H37Rv, and 11 isolates (61%) showed a different restriction pattern. These results suggest that the CGG to CTG change of codon 463 of katG gene of M. tuberculosis may be a polymorphism not related with INH resistance.
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PMID:Isoniazid resistance and the point mutation of codon 463 of katG gene of Mycobacterium tuberculosis. 917 12


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