Phospholipid hydroperoxide glutathione peroxidase is a selenoenzyme distinct from the classical glutathione peroxidase as evident from cDNA and amino acid sequencing

Free Radic Res Commun. 1991;14(5-6):343-61. doi: 10.3109/10715769109093424.

Abstract

The primary structure of phospholipid hydroperoxide glutathione peroxidase (PHGPx) was partially elucidated by sequencing peptides obtained by cyanogen bromide cleavage and tryptic digestion and by isolating and sequencing corresponding cDNA fragments covering about 75% of the total sequence. Based on these data PHGPx can be rated as a selenoprotein homologous, but poorly related to classical glutathione peroxidase (GPx). Peptide loops constituting the active site in GPx are, however, strongly conserved in PHGPx. This suggests that the mechanism of action involving an oxidation/reduction cycle of a selenocysteine residue is essentially identical in PHGPx and GPx.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • DNA / genetics
  • Glutathione Peroxidase / chemistry*
  • Glutathione Peroxidase / genetics
  • Humans
  • Mammals / genetics
  • Molecular Sequence Data
  • Myocardium / enzymology
  • Peptide Mapping
  • Phospholipid Hydroperoxide Glutathione Peroxidase
  • Polymerase Chain Reaction
  • Protein Conformation
  • Sequence Alignment
  • Sequence Homology, Nucleic Acid
  • Species Specificity
  • Swine

Substances

  • DNA
  • Phospholipid Hydroperoxide Glutathione Peroxidase
  • Glutathione Peroxidase

Associated data

  • GENBANK/S70107
  • GENBANK/S70109
  • GENBANK/S70115
  • GENBANK/S70117
  • GENBANK/S70121
  • GENBANK/S70125
  • GENBANK/S70128
  • GENBANK/S70130
  • GENBANK/S76128
  • GENBANK/S80257