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Characterization of six types of thiol peroxidase from the Anabaena sp. (strain PCC7120)
Author(s) -
Cha MeeKyung,
Hong SeungKeun,
Kim IlHan
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.a902-c
Subject(s) - peroxiredoxin , biochemistry , peroxidase , anabaena , shuttle vector , escherichia coli , chemistry , recombinant dna , homology (biology) , thioredoxin , cyanobacteria , enzyme , biology , bacteria , amino acid , gene , genetics , vector (molecular biology)
Thiol peroxidase (TPx), named alternatively peroxiredoxin (Prx), constitutes a large family of enzymes found in microorganisms, animals, and plants. They are assumed to reduce toxic peroxides to their corresponding alcohols with rather broad substrate specificity. The Anabaena sp. (strain PCC7120) genome contains six open reading frames with homology to members of the TSA/AhpC (TPx) family excluding one TPx‐Grx hybrid. A sequences coding for six TPx proteins were inserted into an expression plasmid. The recombinant protein were produced in Escherichia coli cells and purified to homogeneity. We performed the physico‐chemical studies on the six type proteins. It was shown that the there are one dimeric TPx and five monomeric TPx in the cyanobacteria. All of the 2‐Cys TPx proteins (typical and atypical subtypes) degrade preferencially lipid hydroperoxides in the presence of thioredoxin (Trx)/Trx reductaser/NADPH system. In contrast, the 1‐Cys TPx with homology to yeast mitochondrial TPx (ymTPx) showed the Trx‐supported H2O2 peroxidase. The other 1‐Cys TPx reduces preferencially lipid peroxide with the use of DTT not Trx system. Based on this finding, we demonstrated that there are two 1‐Cys‐TPx, one typical 2‐Cys‐TPx, and three atypical 2‐Cys‐TPx in the Anabaena sp. (strain PCC7120).