Molecular identification and properties of a light-insensitive rice catalase-B expressed in E. coli

Mondal, Prosenjit; Ray, Mamata; Kar, M.; Sabat, Surendra Ch.

doi:10.1007/s10529-007-9553-9

Cited by 6 publications

(3 citation statements)

References 18 publications

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“…Molecular identification and properties were performed in a light-insensitive Oryza sativa CAT B that was expressed in Escherichia coli (Mondal et al 2008b). The purification and expression of a soluble bioactive Oryza sativa CAT A from recombinant Escherichia coli have also been done (Ray et al 2012).…”

Section: Catalase Genomic Characterization Genes and Isoformsmentioning

confidence: 99%

Catalase and ascorbate peroxidase—representative H2O2-detoxifying heme enzymes in plants

Anjum

Sharma

Gill

et al. 2016

Environ Sci Pollut Res

267

118

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Plants have to counteract unavoidable stress-caused anomalies such as oxidative stress to sustain their lives and serve heterotrophic organisms including humans. Among major enzymatic antioxidants, catalase (CAT; EC 1.11.1.6) and ascorbate peroxidase (APX; EC 1.11.1.11) are representative heme enzymes meant for metabolizing stress-provoked reactive oxygen species (ROS; such as H2O2) and controlling their potential impacts on cellular metabolism and functions. CAT mainly occurs in peroxisomes and catalyzes the dismutation reaction without requiring any reductant; whereas, APX has a higher affinity for H2O2 and utilizes ascorbate (AsA) as specific electron donor for the reduction of H2O2 into H2O in organelles including chloroplasts, cytosol, mitochondria, and peroxisomes. Literature is extensive on the glutathione-associated H2O2-metabolizing systems in plants. However, discussion is meager or scattered in the literature available on the biochemical and genomic characterization as well as techniques for the assays of CAT and APX and their modulation in plants under abiotic stresses. This paper aims (a) to introduce oxidative stress-causative factors and highlights their relationship with abiotic stresses in plants; (b) to overview structure, occurrence, and significance of CAT and APX in plants;

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Section: Catalase Genomic Characterization Genes and Isoformsmentioning

confidence: 99%

Catalase and ascorbate peroxidase—representative H2O2-detoxifying heme enzymes in plants

Anjum

Sharma

Gill

et al. 2016

Environ Sci Pollut Res

267

118

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“…2.1 Determination of the subunit size and comparison of the oligomeric status of WT and mutant IcSOD A mutant plasmid (Ser95Cys) was constructed following in vitro site-specific recombinant PCR and transformed into M15 cells for its overexpression. 20 The recombinant IcSOD proteins (WT and mutant) were purified to their homogeneity using Ni-NTA columns following protocols described earlier. 21 suggested that the sub-unit size of both the WT and mutant IcSOD was B17 kDa (ESI, † Fig.…”

Section: Resultsmentioning

confidence: 99%

S95C substitution in CuZn-SOD of Ipomoea carnea: impact on the structure, function and stability

et al. 2016

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Superoxide dismutase (SOD) in general is a unique homo-dimeric enzyme that can scavenge toxic superoxide radicals by dismutation reaction. In IcSOD (Ipomoea carnea SOD), the presence of cysteine (Cys) plays an essential role in protein behaviour. This study analysed the role of Cys in modulating the stability and kinetic properties of IcSOD. To investigate the significance of the dimeric structure in modulating the structure/function relationship of CuZn-SODs, we have substituted a conserved serine by cysteine (Ser95Cys) in Ipomoea carnea CuZn-SOD. The results demonstrate that this mutation leads to an increase in dimeric strength, as reflected by size exclusion chromatography, differential scanning calorimetry, and high-temperature circular dichroism spectroscopy measurements. The mutant form, as compared to the native enzyme, shows a relatively low tendency to form aggregates but encountered a reduction in both dismutase and peroxidase activities. This study provides new mechanistic insight into the role of free cysteine in CuZn-SODs and such mutation may be used to increase dimeric strength. Protein docking and molecular dynamics simulations further demonstrate that Ser95Cys substitution in Ipomoea carnea CuZn-SOD leads to the creation of a new subunit interface resulting in increased dimeric strength of the protein.

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“…and detoxifies the body, protect against mutagenesis and degenerative diseases [9]. Promising applications of catalases are in wastewater treatment, therapeutics, baking and brewing, pulp and paper industry [7,10]. Peroxidase has a potential for bioremediation of soil and wastewater contaminated with phenols, cresols, chlorinated phenols.…”

Section: Research Articlementioning

confidence: 99%

Assessment of Superoxide Dismutase, Catalase, and Peroxidase Activities in Aspergillus Sp. And Cladosporium Sp.

Alam¹,

Kataria²,

Nethravathy³

2021

JASR

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Antioxidative enzymes are a family of powerful free radical scavenging proteins, naturally synthesized by all aerobic organisms. Family of antioxidant enzymes include superoxide dismutase (SOD), catalase (CAT), peroxidase (PRX), thioredoxins /thioredoxin reductase (TrxR), and glutaredoxins/glutathione reductase (GPx). These oxidative enzymatic machineries, sequentially sequester singlet oxygen (O2 −) and Hydrogen Peroxide, which are the well-known reactive oxygen species. These enzymes can be intracellular as well as extracellular. In the present study, two most common soil fungi namely, Aspergillus Sp. and Cladosporium Sp. were cultivated by submerged cultivation on Potato dextrose broth and pellets were separated by filtration. Pellets were disrupted by detergent lysis method (0.5% Triton X 100, 1% CTAB, 1.5% Tween 80, 5% SDS). Culture media and cellular extracts were analyzed for intracellular and extracellular total proteins and their panel of antioxidative enzymes. Enzyme activity of SOD was carried out by Beauchamp and Fridovich method. Catalase and Peroxidase activities were determined by simple spectrophotometric method. In Aspergillus Sp.1.33 U of superoxide dismutase, 0.115 U catalase, 0.00097 U peroxidase activities per mg of protein was observed. Similarly, in Cladosporium Sp. 1.38 U Superoxide dismutase, 0.1460 U catalase, and 0.00150 U peroxidase activities per mg protein was recorded. Significant amount of antioxidative enzyme activity observed in both the test cultures. And comparatively, Cladosporium Sp has given promising results. Probably, with altered culture conditions and improved extraction procedures, still higher amounts of antioxidative enzymes would be expected.

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Molecular identification and properties of a light-insensitive rice catalase-B expressed in E. coli

Cited by 6 publications

References 18 publications

Catalase and ascorbate peroxidase—representative H2O2-detoxifying heme enzymes in plants

Catalase and ascorbate peroxidase—representative H2O2-detoxifying heme enzymes in plants

S95C substitution in CuZn-SOD of Ipomoea carnea: impact on the structure, function and stability

Assessment of Superoxide Dismutase, Catalase, and Peroxidase Activities in Aspergillus Sp. And Cladosporium Sp.

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