Cloning, Overexpression, and Characterization of Peroxiredoxin and NADH Peroxiredoxin Reductase from Thermus aquaticus
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چکیده
منابع مشابه
Molecular cloning and characterization of a peroxiredoxin from Phanerochaete chrysosporium.
Peroxiredoxins (Prxs) are a ubiquitous family of peroxidases widely distributed among prokaryotes and eukaryotes. Here, we report on the cloning and functional characterization of a cDNA designated PcPrx-1, encoding peroxiredoxin from the white-rot fungus Phanerochaete chrysosporium. The full-length PcPrx-1 cDNA (932 bp) contains an open reading frame of 200 amino acid residues with a molecular...
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The NADH oxidase-peroxiredoxin (Prx) system of Amphibacillus xylanus reduces hydroperoxides with the highest turnover rate among the known hydroperoxide-scavenging enzymes. The high electron transfer rate suggests that there exists close interaction between NADH oxidase and Prx. Variant enzyme experiments indicated that the electrons from β-NADH passed through the secondary disulfide, Cys128-Cy...
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DNA polymerase gene from Thermus aquaticus strain YT1 was amplified using VENTTM DNA po-lymerase and cloned under the control of X.PR promoter and expression was induced by a shift in tern perature. The culture was then sonicated, and after centrifugation the lysate was treated with polyethyleneimine followed by a salting-out step. Finally the protein was precipitated with ammonium sulfate and...
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A cDNA sequence coding for a pea (Pisum sativum L.) 2-Cys peroxiredoxin (2-Cys Prx) has been cloned. The deduced amino acid sequence showed a high sequence homology to the 2-Cys Prx enzymes of Phaseolus vulgaris (86%), Arabidopsis thaliana (75%), and Spinacia oleracea (75%), and contained a chloroplast target sequence at its N-terminus. The mature enzyme, without the transit peptide, has a mole...
متن کاملCloning and Characterization of a 2-Cys Peroxiredoxin from Babesia gibsoni
Peroxiredoxins (Prxs) are a family of antioxidant enzymes. Here, we cloned a 2-Cys Prx, BgTPx-1, from the canine Babesia parasite B. gibsoni. Sequence identity between BgTPx-1 and 2-Cys Prx of B. bovis was 81% at the amino acid level. Enzyme activity assay by using recombinant BgTPx-1 (rBgTPx-1) indicated that BgTPx-1 has antioxidant activity. Antiserum from a mouse immunized with rBgTPx-1 reac...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2000
ISSN: 0021-9258
DOI: 10.1074/jbc.m004161200