ER oxidoreductin (original) (raw)
ER oxidoreductin 1 (Ero1) is an oxidoreductase enzyme that catalyses the formation and isomerization of protein disulfide bonds in the endoplasmic reticulum (ER) of eukaryotes. ER Oxidoreductin 1 (Ero1) is a conserved, luminal, glycoprotein that is tightly associated with the ER membrane, and is essential for the oxidation of protein dithiols. Since disulfide bond formation is an oxidative process, the major pathway of its catalysis has evolved to utilise oxidoreductases, which become reduced during the thiol-disulfide exchange reactions that oxidise the cysteine thiol groups of nascent polypeptides. Ero1 is required for the introduction of oxidising equivalents into the ER and their direct transfer to protein disulfide isomerase (PDI), thereby ensuring the correct folding and assembly of
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| dbo:abstract | ER oxidoreductin 1 (Ero1) is an oxidoreductase enzyme that catalyses the formation and isomerization of protein disulfide bonds in the endoplasmic reticulum (ER) of eukaryotes. ER Oxidoreductin 1 (Ero1) is a conserved, luminal, glycoprotein that is tightly associated with the ER membrane, and is essential for the oxidation of protein dithiols. Since disulfide bond formation is an oxidative process, the major pathway of its catalysis has evolved to utilise oxidoreductases, which become reduced during the thiol-disulfide exchange reactions that oxidise the cysteine thiol groups of nascent polypeptides. Ero1 is required for the introduction of oxidising equivalents into the ER and their direct transfer to protein disulfide isomerase (PDI), thereby ensuring the correct folding and assembly of proteins that contain disulfide bonds in their native state. Ero1 exists in two isoforms: Ero1-α and Ero1-β. Ero1-α is mainly induced by hypoxia (HIF-1), whereas Ero1-β is mainly induced by the unfolded protein response (UPR). During endoplasmic reticulum stress (such as occurs in beta cells of the pancreas or in macrophages causing atherosclerosis), CHOP can induce activation of Ero1, causing calcium release from the endoplasmic reticulum into the cytoplasm, resulting in apoptosis. Homologues of the Saccharomyces cerevisiae Ero1 proteins have been found in all eukaryotic organisms examined, and contain seven cysteine residues that are absolutely conserved, including three that form the sequence Cys–X–X–Cys–X–X–Cys (where X can be any residue). (en) |
| dbo:symbol | ERO1 |
| dbo:thumbnail | wiki-commons:Special:FilePath/PDB_1rp4_EBI.jpg?width=300 |
| dbo:wikiPageID | 7023098 (xsd:integer) |
| dbo:wikiPageLength | 4969 (xsd:nonNegativeInteger) |
| dbo:wikiPageRevisionID | 1032198712 (xsd:integer) |
| dbo:wikiPageWikiLink | dbr:Endoplasmic_reticulum dbr:Endoplasmic_reticulum_stress_in_beta_cells dbr:Cytoplasm dbr:DNA_damage-inducible_transcript_3 dbr:Saccharomyces_cerevisiae dbr:Protein_isoform dbc:Biomolecules dbc:Enzymes dbr:Enzyme dbr:Apoptosis dbr:Protein_disulfide_isomerase dbr:Cysteine dbr:Eukaryotes dbr:Glycoprotein dbr:Atherosclerosis dbr:Hypoxia_(medical) dbr:Sulfur dbr:Disulfide_bonds dbr:Hypoxia-inducible_factors dbr:Macrophage dbr:Unfolded_protein_response dbr:Oxidation dbr:Oxidoreductase dbr:Thiol dbr:Nucleophilic_attack dbr:Thiol-disulfide_exchange |
| dbp:caption | Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell. (en) |
| dbp:interpro | IPR007266 (en) |
| dbp:name | Endoplasmic reticulum oxidoreductin 1 (en) |
| dbp:pdb | , (en) |
| dbp:pfam | PF04137 (en) |
| dbp:symbol | ERO1 (en) |
| dbp:wikiPageUsesTemplate | dbt:Enzyme-stub dbt:PDB2 dbt:Pfam_box |
| dcterms:subject | dbc:Biomolecules dbc:Enzymes |
| gold:hypernym | dbr:Enzyme |
| rdf:type | owl:Thing dbo:Biomolecule wikidata:Q206229 wikidata:Q8054 yago:Abstraction100002137 yago:Activator114723079 yago:Catalyst114723628 yago:Chemical114806838 yago:Compound114818238 yago:Enzyme114732946 yago:Macromolecule114944888 yago:Material114580897 yago:Matter100020827 yago:Molecule114682133 yago:OrganicCompound114727670 yago:Part113809207 yago:PhysicalEntity100001930 yago:Protein114728724 yago:Relation100031921 dbo:Protein yago:Substance100019613 yago:Thing100002452 yago:Unit109465459 yago:WikicatEnzymes |
| rdfs:comment | ER oxidoreductin 1 (Ero1) is an oxidoreductase enzyme that catalyses the formation and isomerization of protein disulfide bonds in the endoplasmic reticulum (ER) of eukaryotes. ER Oxidoreductin 1 (Ero1) is a conserved, luminal, glycoprotein that is tightly associated with the ER membrane, and is essential for the oxidation of protein dithiols. Since disulfide bond formation is an oxidative process, the major pathway of its catalysis has evolved to utilise oxidoreductases, which become reduced during the thiol-disulfide exchange reactions that oxidise the cysteine thiol groups of nascent polypeptides. Ero1 is required for the introduction of oxidising equivalents into the ER and their direct transfer to protein disulfide isomerase (PDI), thereby ensuring the correct folding and assembly of (en) |
| rdfs:label | ER oxidoreductin (en) |
| owl:sameAs | freebase:ER oxidoreductin yago-res:ER oxidoreductin wikidata:ER oxidoreductin https://global.dbpedia.org/id/2KZJT |
| prov:wasDerivedFrom | wikipedia-en:ER_oxidoreductin?oldid=1032198712&ns=0 |
| foaf:depiction | wiki-commons:Special:FilePath/PDB_1rp4_EBI.jpg |
| foaf:isPrimaryTopicOf | wikipedia-en:ER_oxidoreductin |
| is dbo:wikiPageRedirects of | dbr:ER_Oxidoreductin |
| is dbo:wikiPageWikiLink of | dbr:Cholera_toxin dbr:ER_Oxidoreductin |
| is foaf:primaryTopic of | wikipedia-en:ER_oxidoreductin |
