Q4AEI3 · GPX1_PONPY

Function

function

Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis. Can reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide, as well as several fatty acid-derived hydroperoxides. In platelets catalyzes the reduction of 12-hydroperoxyeicosatetraenoic acid, the primary product of the arachidonate 12-lipoxygenase pathway.

Catalytic activity

  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
    This reaction proceeds in the forward direction.
    EC:1.11.1.9 (UniProtKB | ENZYME | Rhea)
  • a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
    EC:1.11.1.12 (UniProtKB | ENZYME | Rhea)
  • 2 glutathione + tert-butyl hydroperoxide = glutathione disulfide + H2O + tert-butanol
    This reaction proceeds in the forward direction.
  • cumene hydroperoxide + 2 glutathione = 2-phenylpropan-2-ol + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione = (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (9S)-hydroperoxy-(10E,12Z)-octadecadienoate + 2 glutathione = (9S)-hydroxy-(10E,12Z)-octadecadienoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2 glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2 glutathione = (12R)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + 2 glutathione = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (5S)-hydroperoxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (12S)-hydroperoxy-(5Z,8Z,10E,14Z,17Z)-eicosapentaenoate + 2 glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z,17Z)-eicosapentaenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (15S)-hydroperoxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + 2 glutathione = (15S)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (15S)-hydroperoxy-(11Z,13E)-eicosadienoate + 2 glutathione = (15S)-hydroxy-(11Z,13E)-eicosadienoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (17S)-hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + 2 glutathione = (17S)-hydroxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.

Features

Showing features for active site, site.

TypeIDPosition(s)Description
Active site47
Site47Subject to oxidation and hydroselenide loss to dehydroalanine

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrion
Molecular Functionglutathione peroxidase activity
Molecular Functionphospholipid-hydroperoxide glutathione peroxidase activity
Biological Processarachidonic acid metabolic process
Biological Processglutathione metabolic process
Biological Processhydrogen peroxide catabolic process
Biological Processlipoxygenase pathway
Biological Processresponse to hydrogen peroxide
Biological Processresponse to selenium ion

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutathione peroxidase 1
  • EC number
  • Short names
    GPx-1; GSHPx-1
  • Alternative names
    • Cellular glutathione peroxidase
    • Phospholipid-hydroperoxide glutathione peroxidase GPX1 (EC:1.11.1.12
      ) . EC:1.11.1.12 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      GPX1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pongo

Accessions

  • Primary accession
    Q4AEI3

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000666151-201Glutathione peroxidase 1
Modified residue32Phosphoserine
Modified residue86N6-acetyllysine; alternate
Modified residue86N6-succinyllysine; alternate
Modified residue112N6-acetyllysine; alternate
Modified residue112N6-succinyllysine; alternate
Modified residue146N6-acetyllysine; alternate
Modified residue146N6-succinyllysine; alternate
Modified residue195Phosphoserine
Modified residue199Phosphoserine

Post-translational modification

During periods of oxidative stress, Sec-47 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine.

Keywords

Interaction

Subunit

Homotetramer. Interacts with MIEN1 (By similarity).

Family & Domains

Sequence similarities

Belongs to the glutathione peroxidase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    201
  • Mass (Da)
    21,990
  • Last updated
    2008-02-26 v2
  • Checksum
    EB34A11CFC1A759A
MCAARLVAAAAQSVYSFSARPLAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRRFQTIDIEPDIEALLSQGPSCA

Features

Showing features for non-standard residue.

TypeIDPosition(s)Description
Non-standard residue47Selenocysteine

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB120997
EMBL· GenBank· DDBJ
BAE17007.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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