Molecular cloning and characterization of a cDNA encoding putative phospholipid hydroperoxide glutathione peroxidase from spinach.
A cDNA encoding spinach putative phospholipid hydroperoxide glutathione peroxidase (PHGPX) was cloned and sequenced. The cDNA included an open reading frame that encoded a polypeptide of 171 amino acid residues. The deduced amino acid sequence showed about 77 and 50% similarity to plant putative PHGPXs and mammalian PHGPXs, respectively. PCR product with the same size as that of the spinach putative PHGPX were obtained from maize, soybeans, and Arabidopsis, suggesting the expression of putative PHGPX genes in other plants.
Sugimoto
M
M
Research Institute for Bioresources, Okayama University, Japan.
Furui
S
S
Suzuki
Y
Y
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000096:biosynthesis* / Q000235:genetics; D005979:Glutathione Peroxidase / Q000096:biosynthesis* / Q000235:genetics; D008969:Molecular Sequence Data; D016366:Open Reading Frames / Q000235:genetics; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D010944:Plants / Q000378:metabolism; D016133:Polymerase Chain Reaction; D013025:Glycine max / Q000201:enzymology; D018724:Spinacia oleracea / Q000201:enzymology*; D003313:Zea mays / Q000201:enzymology
D018076:DNA, Complementary; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D005979:Glutathione Peroxidase