P36014 · GPX1_YEAST

Function

function

Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress (PubMed:10480913, PubMed:11445588).
Has peroxidase activity using thioredoxin or glutathione as a reducing power (PubMed:20572871, PubMed:22659048).
Involved in peroxisome formation (PubMed:22659048).

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide.

Caution

Was originally thought to be a glutathione peroxidase (PubMed:10480913) or a phospholipid hydroperoxide glutathione peroxidase (PubMed:11445588), but functions as an atypical 2-Cys peroxiredoxin using both glutathione and thioredoxin almost equally as reducing power instead (PubMed:20572871).

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
141 μMH2O2using glutathione as electron donor
75 μMtert-butyl hydroperoxideusing glutathione as electron donor
120 μMH2O2using thioredoxin as electron donor
223 μMtert-butyl hydroperoxideusing glutathione as electron donor
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
2.98 μmol/min/mgfor H2O2 (using glutathione as electron donor)
0.579 μmol/min/mgfor tert-butyl hydroperoxide (using glutathione as electron donor)
0.739 μmol/min/mgfor H2O2 (using thioredoxin as electron donor)
1.25 μmol/min/mgfor tert-butyl hydroperoxide (using thioredoxin as electron donor)

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site36Cysteine sulfenic acid (-SOH) intermediate

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrial outer membrane
Cellular Componentperoxisomal matrix
Molecular Functionglutathione peroxidase activity
Molecular Functionphospholipid-hydroperoxide glutathione peroxidase activity
Molecular Functionthioredoxin-dependent peroxiredoxin activity
Biological Processcellular response to oxidative stress
Biological Processperoxisome organization

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutathione peroxidase-like peroxiredoxin 1
  • EC number
  • Alternative names
    • Glutathione peroxidase homolog 1
      (GPx 1)

Gene names

    • Name
      GPX1
    • Ordered locus names
      YKL026C

Organism names

Accessions

  • Primary accession
    P36014
  • Secondary accessions
    • D6VXQ8

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Disruption phenotype

Impairs growth and peroxisome formation in oleic acid medium.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis36Prevents oxidation of the protein.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 7 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00000666411-167Glutathione peroxidase-like peroxiredoxin 1
Disulfide bond36↔82Redox-active

Keywords

Proteomic databases

Expression

Induction

By glucose starvation.

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Belongs to the glutathione peroxidase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    167
  • Mass (Da)
    19,485
  • Last updated
    1994-06-01 v1
  • Checksum
    8C421FFF813391DD
MQEFYSFSPIDENGNPFPFNSLRNKVVLIVNVASHCAFTPQYKELEYLYEKYKSHGLVIVAFPCGQFGNQEFEKDKEINKFCQDKYGVTFPILHKIRCNGQKQDPVYKFLKNSVSGKSGIKMIKWNFEKFVVDRNGKVVKRFSCMTRPLELCPIIEELLNQPPEEQI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z28026
EMBL· GenBank· DDBJ
CAA81861.1
EMBL· GenBank· DDBJ
Genomic DNA
AY557895
EMBL· GenBank· DDBJ
AAS56221.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006944
EMBL· GenBank· DDBJ
DAA09128.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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