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Primary Structural Characterization of Phospholipid Hydroperoxide Glutathione Peroxidase

Primary Structural Characterization of Phospholipid Hydroperoxide Glutathione Peroxidase
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摘要 More than 20 sequences of phospholipid hydroperoxide glutathione peroxidase (PHGPX) from a sequence database were analyzed. The analyses show that the primary structures of most PHGPX proteins have three highly conserved regions forming a catalytic center and have more than 50% amino acid sequence identity in common. However, two PHGPXs from bovine and swine with the same function have very low similarity with typical PHGPXs and do not have the three highly conserved regions. Thus, the PHGPX proteins are divided into two types: those with the three highly conserved regions, designated as PHGPX I, and the others as PHGPX II. In general, type I proteins are composed of ca.170 amino acid residues; a few of them have an extra signal peptide sequence at the N terminal of the protein. The composition of plant and animal PHGPX amino acids is very different, with most plant PHGPXs being weak acidic, while most animal ones are alkaline. Another specific conservative motif is also found in plant PHGPX proteins. System evolution analysis shows that ortholog and paralog evolution models both exist in PHGPXs, with the plant PHGPX and the animal PHGPX diverging exclusively into two branches in PHGPX I. The information revealed by the evolution tree agrees with the general species evolution process from low to advanced and from simple to complicated. More than 20 sequences of phospholipid hydroperoxide glutathione peroxidase (PHGPX) from a sequence database were analyzed. The analyses show that the primary structures of most PHGPX proteins have three highly conserved regions forming a catalytic center and have more than 50% amino acid sequence identity in common. However, two PHGPXs from bovine and swine with the same function have very low similarity with typical PHGPXs and do not have the three highly conserved regions. Thus, the PHGPX proteins are divided into two types: those with the three highly conserved regions, designated as PHGPX I, and the others as PHGPX II. In general, type I proteins are composed of ca.170 amino acid residues; a few of them have an extra signal peptide sequence at the N terminal of the protein. The composition of plant and animal PHGPX amino acids is very different, with most plant PHGPXs being weak acidic, while most animal ones are alkaline. Another specific conservative motif is also found in plant PHGPX proteins. System evolution analysis shows that ortholog and paralog evolution models both exist in PHGPXs, with the plant PHGPX and the animal PHGPX diverging exclusively into two branches in PHGPX I. The information revealed by the evolution tree agrees with the general species evolution process from low to advanced and from simple to complicated.
出处 《Tsinghua Science and Technology》 SCIE EI CAS 2002年第4期363-368,共6页 清华大学学报(自然科学版(英文版)
基金 Supported by the National Natural Science F oundationof China(Nos. 3 9770 0 78and 3 0 170 0 80 ) the NationalTransgenic Plant Research Project(No.J99-A-041) State Key Basic Research and Development Plan(No.G199980 10 10 0 ) Yunnan Province-Unive
关键词 phospholipid hydroperoxide glutathione peroxidase (PHGPX) isoelectric point and transmembrane region molecular evolution primary structural characterization phospholipid hydroperoxide glutathione peroxidase (PHGPX) isoelectric point and transmembrane region molecular evolution primary structural characterization
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参考文献14

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