Steps in reductive activation of the disulfide‐generating enzyme Ero1p
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Summary
It is found that the C150C295 disulfide sets a physiologically appropriate threshold for enzyme activation by guarding a key neighboring disulfides from reduction by guarding one of the electron transfer pathways from substrate thiol groups to oxygen.
- Type
- article
- Published
- 2010-10-01
- Cited by
- 27
- References
- 23
- Access
- Open access
- OpenAlex
- https://openalex.org/W1566996957
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:44892858
Keywords
Chemistry, Enzyme, Redox, Endoplasmic reticulum, Protein disulfide-isomerase
References
- Processing of X-ray diffraction data collected in oscillation mode.
- A colorimetric method for determining low concentrations of mercaptans.
- A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
- Crystallography & NMR system: A new software suite for macromolecular structure determination.
- Functional properties of the two redox-active sites in yeast protein disulphide isomerase in vitro and in vivo.
- Oxidative Activity of Yeast Ero1p on Protein Disulfide Isomerase and Related Oxidoreductases of the Endoplasmic Reticulum*
- Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell.
- The interpretation of protein structures: estimation of static accessibility.
- Improved methods for building protein models in electron density maps and the location of errors in these models.
- Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p.
- The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum.
- Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum.
- Oxidative protein folding in the mammalian endoplasmic reticulum.
- A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cells
- Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidation
- Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels.
- Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engine.
- Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum.
- MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
- Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1.
Cited by
- The mechanism of endoplasmic reticulum oxidoreductase 1 α (Ero1α) inactivation
- Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals
- Functional in Vitro Analysis of the ERO1 Protein and Protein-disulfide Isomerase Pathway*
- Sulfhydryl oxidases: sources, properties, production and applications
- Hyperactivity of the Ero1α Oxidase Elicits Endoplasmic Reticulum Stress but No Broad Antioxidant Response
- Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262
- Structure, Mechanism, and Evolution of Ero1 Family Enzymes
- Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerases
- The Physiological Functions of Mammalian Endoplasmic Oxidoreductin 1: On Disulfides and More
- The endoplasmic reticulum sulfhydryl oxidase Ero1β drives efficient oxidative protein folding with loose regulation.
- Multiple ways to make disulfides.
- The antioxidant machinery of the endoplasmic reticulum: Protection and signaling.
- Balanced Ero1 activation and inactivation establishes ER redox homeostasis
- The oxidative protein folding machinery in plant cells
- Significant reduction in errors associated with nonbonded contacts in protein crystal structures: automated all-atom refinement with PrimeX
- Ero1–PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum
- Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1*
- Disulfide Bond Formation: Identifying Roles of PDI Family Thiol Oxidoreductases and ER Oxidant Pathways
- Chemistry and Enzymology of Disulfide Cross-linking in Proteins
- Reexamining the Function of Glutathione in Oxidative Protein Folding and Secretion
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- The nonactive site cysteine residues of yeast protein disulfide isomerase are not required for cell viability.
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