Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase.

No abstract is available for this paper.

• Publication year

  1995

• Venue

  Biochemistry

• Publication date

  1995-03-21

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1021/BI00011A012PMID 7893654
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation.

  1994cited by this paper
• Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.

  1994cited by this paper
• Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo.

  1994cited by this paper
• Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin.

  1994cited by this paper
• Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo.

  1994cited by this paper
• Protein disulphide isomerase: building bridges in protein folding.

  1994cited by this paper
• Dissecting the mechanism of protein disulfide isomerase: catalysis of disulfide bond formation in a model peptide.

  1994cited by this paper
• Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo.

  1993cited by this paper
• Local conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor and their roles in folding.

  1993cited by this paper
• Crystal structure of the DsbA protein required for disulphide bond formation in vivo

  1993cited by this paper
• The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.

  1993cited by this paper
• Redox properties of protein disulfide isomerase (dsba) from escherichia coli

  1993cited by this paper
• Bacterial protein disulfide isomerase: efficient catalysis of oxidative protein folding at acidic pH.

  1993cited by this paper
• A pathway for disulfide bond formation in vivo.

  1993cited by this paper
• The bonds that tie: catalyzed disulfide bond formation.

  1993cited by this paper
• Oxidized redox state of glutathione in the endoplasmic reticulum.

  1992cited by this paper
• Identification of a protein required for disulfide bond formation in vivo.

  1991cited by this paper
• Protein folding.

  1990cited by this paper
• Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin

  1985cited by this paper
• Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor.

  1984cited by this paper
• Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione

  1980cited by this paper
• Experimental studies of protein folding and unfolding.

  1978cited by this paper
• Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect.

  1971cited by this paper

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  2014cites this paper
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• Engineered Pathways for Correct Disulfide Bond Oxidation

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• Residual factor VIII-like cofactor activity of thioredoxin and related oxidoreductases.

  2010cites this paper
• Mechanisms of Oxidative Protein Folding in the Bacterial Cell Envelope

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• The Structure of the Bacterial Oxidoreductase Enzyme DsbA in Complex with a Peptide Reveals a Basis for Substrate Specificity in the Catalytic Cycle of DsbA Enzymes*

  2009cites this paper
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  2009cites this paper
• Detecting folding intermediates of a protein as it passes through the bacterial translocation channel.

  2009cites this paper
• Structure and function of the oxidoreductase DsbA1 from Neisseria meningitidis.

  2009cites this paper
• Evidence for proton shuffling in a thioredoxin-like protein during catalysis.

  2008cites this paper
• DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli.

  2008cites this paper
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  2007cites this paper
• Similarities and differences in the thioredoxin superfamily.

  2006cites this paper
• Determination of the ΔpKa between the active site cysteines of thioredoxin and DsbA

  2006cites this paper
• Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles

  2006cites this paper
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• Mutational Alterations of the Key cis Proline Residue That Cause Accumulation of Enzymatic Reaction Intermediates of DsbA, a Member of the Thioredoxin Superfamily

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  2005cites this paper
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  2004cites this paper
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  2004cites this paper
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  2003cites this paper
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  2003cites this paper
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  2003cites this paper
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  2003cites this paper
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  2003cites this paper
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  2003cites this paper
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  2003cites this paper
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  2003cites this paper
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  2002cites this paper
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  2002cites this paper
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  2002cites this paper
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  2002cites this paper
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  2002cites this paper
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  2002cites this paper
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  2001cites this paper
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  2001cites this paper
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  2000cites this paper
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  2000cites this paper
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  1999cites this paper
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  1999cites this paper
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  1999cites this paper
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  1999cites this paper
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  1999cites this paper
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  1999cites this paper
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  1999cites this paper
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  1999cites this paper
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  1999cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1998cites this paper
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  1997cites this paper
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  1997cites this paper
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  1996cites this paper
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  1996cites this paper
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  1996cites this paper
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  1996cites this paper