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Cloning and sequencing of the cDNA encoding a human testis phospholipid hydroperoxide glutathione peroxidase.
Department of Medical Oncology, City of Hope National Medical Center, Duarte, CA 9101.
A human cDNA that encodes a polypeptide that has 94% deduced amino-acid sequence identity to porcine phospholipid hydroperoxide glutathione peroxidase was cloned from a testis library. The sequence shows preservation of the UGA selenocysteine codon, putative active-site Trp and Glu residues and a Tyr residue that is phosphorylated in the porcine protein. The 3'-UTR shows some conservation of sequences implicated in the insertion of selenocysteine at an opal codon in human glutathione peroxidase-1.
PMID: 8039723 [PubMed - indexed for MEDLINE]
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Cited by 3 PubMed Central articles
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In vitro evolution of horse heart myoglobin to increase peroxidase activity.
Wan L, Twitchett MB, Eltis LD, Mauk AG, Smith M.
Proc Natl Acad Sci U S A. 1998 Oct 27; 95(22):12825-31.
[Proc Natl Acad Sci U S A. 1998]
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A novel type of glutathione peroxidase: expression and regulation during wound repair.
Munz B, Frank S, Hübner G, Olsen E, Werner S.
Biochem J. 1997 Sep 1; 326 ( Pt 2):579-85.
[Biochem J. 1997]
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An RNA-binding protein recognizes a mammalian selenocysteine insertion sequence element required for cotranslational incorporation of selenocysteine.
Lesoon A, Mehta A, Singh R, Chisolm GM, Driscoll DM.
Mol Cell Biol. 1997 Apr; 17(4):1977-85.
[Mol Cell Biol. 1997]