Possible function of two insect phospholipid-hydroperoxide glutathione peroxidases.
We compared the functional properties of two insect members of the phospholipid hydroperoxide glutathione peroxidases (PHGPx) family, VLP1, a major component of virus-like particles from the hymenopteran endoparasitoid Venturia canescens and its closest Drosophila relative, one of the putative PHGPx-proteins predicted from the Berkeley Drosophila genome sequence project. Recombinant Drosophila PHGPx shows enzymatic activity towards a number of PHGPx substrates, while the recombinant PHGPx-like domain of VLP1 lacks a functionally relevant cysteine and enzyme activity. A possible function of a non-enzymatic extracellular PHGPx-like protein is discussed.
Li
D
D
Department of Applied and Molecular Ecology, Waite Campus, Adelaide University, Glen Osmond, SA 5064, Australia.
Blasevich
F
F
Theopold
U
U
Schmidt
O
O
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D017931:DNA Primers; D004330:Drosophila / Q000145:classification / Q000201:enzymology / Q000235:genetics / Q000502:physiology*; D016678:Genome; D005979:Glutathione Peroxidase / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D006927:Hymenoptera / Q000145:classification / Q000201:enzymology / Q000502:physiology; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D010802:Phylogeny; D011994:Recombinant Proteins / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D014158:Transcription, Genetic
D017931:DNA Primers; D011994:Recombinant Proteins; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D005979:Glutathione Peroxidase