Why is DsbA such an oxidizing disulfide catalyst?

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Standard

Why is DsbA such an oxidizing disulfide catalyst? / Grauschopf, U; Winther, Jakob R.; Korber, P; Zander, T; Dallinger, P; Bardwell, J C.

I: Cell, Bind 83, Nr. 6, 1995, s. 947-55.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Grauschopf, U, Winther, JR, Korber, P, Zander, T, Dallinger, P & Bardwell, JC 1995, 'Why is DsbA such an oxidizing disulfide catalyst?', Cell, bind 83, nr. 6, s. 947-55.

APA

Grauschopf, U., Winther, J. R., Korber, P., Zander, T., Dallinger, P., & Bardwell, J. C. (1995). Why is DsbA such an oxidizing disulfide catalyst? Cell, 83(6), 947-55.

Vancouver

Grauschopf U, Winther JR, Korber P, Zander T, Dallinger P, Bardwell JC. Why is DsbA such an oxidizing disulfide catalyst? Cell. 1995;83(6):947-55.

Author

Grauschopf, U ; Winther, Jakob R. ; Korber, P ; Zander, T ; Dallinger, P ; Bardwell, J C. / Why is DsbA such an oxidizing disulfide catalyst?. I: Cell. 1995 ; Bind 83, Nr. 6. s. 947-55.

Bibtex

@article{75434229d9be4178b1537122f326df97,
title = "Why is DsbA such an oxidizing disulfide catalyst?",
abstract = "DsbA, a member of the thioredoxin family of disulfide oxidoreductases, acts in catalyzing disulfide bond formation by donating its disulfide to newly translocated proteins. We have found that the two central residues within the active site Cys-30-Pro-31-His-32-Cys-33 motif are critical in determining the exceptional oxidizing power of DsbA. Mutations that change these two residues can alter the equilibrium oxidation potential of DsbA by more than 1000-fold. A quantitative explanation for the very high redox potential of DsbA was found by measuring the pKa of a single residue, Cys-30. The pKa of Cys-30 varied dramatically from mutant to mutant and could accurately predict the oxidizing power of each DsbA mutant protein.",
keywords = "Amino Acid Sequence, Base Sequence, Binding Sites, Catalysis, Cysteine, Disulfides, Enzyme Stability, Isomerases, Kinetics, Molecular Sequence Data, Mutation, Oxidation-Reduction, Oxidoreductases, Protein Disulfide-Isomerases, Protein Folding, Recombinant Fusion Proteins, beta-Galactosidase",
author = "U Grauschopf and Winther, {Jakob R.} and P Korber and T Zander and P Dallinger and Bardwell, {J C}",
year = "1995",
language = "English",
volume = "83",
pages = "947--55",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "6",

}

RIS

TY - JOUR

T1 - Why is DsbA such an oxidizing disulfide catalyst?

AU - Grauschopf, U

AU - Winther, Jakob R.

AU - Korber, P

AU - Zander, T

AU - Dallinger, P

AU - Bardwell, J C

PY - 1995

Y1 - 1995

N2 - DsbA, a member of the thioredoxin family of disulfide oxidoreductases, acts in catalyzing disulfide bond formation by donating its disulfide to newly translocated proteins. We have found that the two central residues within the active site Cys-30-Pro-31-His-32-Cys-33 motif are critical in determining the exceptional oxidizing power of DsbA. Mutations that change these two residues can alter the equilibrium oxidation potential of DsbA by more than 1000-fold. A quantitative explanation for the very high redox potential of DsbA was found by measuring the pKa of a single residue, Cys-30. The pKa of Cys-30 varied dramatically from mutant to mutant and could accurately predict the oxidizing power of each DsbA mutant protein.

AB - DsbA, a member of the thioredoxin family of disulfide oxidoreductases, acts in catalyzing disulfide bond formation by donating its disulfide to newly translocated proteins. We have found that the two central residues within the active site Cys-30-Pro-31-His-32-Cys-33 motif are critical in determining the exceptional oxidizing power of DsbA. Mutations that change these two residues can alter the equilibrium oxidation potential of DsbA by more than 1000-fold. A quantitative explanation for the very high redox potential of DsbA was found by measuring the pKa of a single residue, Cys-30. The pKa of Cys-30 varied dramatically from mutant to mutant and could accurately predict the oxidizing power of each DsbA mutant protein.

KW - Amino Acid Sequence

KW - Base Sequence

KW - Binding Sites

KW - Catalysis

KW - Cysteine

KW - Disulfides

KW - Enzyme Stability

KW - Isomerases

KW - Kinetics

KW - Molecular Sequence Data

KW - Mutation

KW - Oxidation-Reduction

KW - Oxidoreductases

KW - Protein Disulfide-Isomerases

KW - Protein Folding

KW - Recombinant Fusion Proteins

KW - beta-Galactosidase

M3 - Journal article

C2 - 8521518

VL - 83

SP - 947

EP - 955

JO - Cell

JF - Cell

SN - 0092-8674

IS - 6

ER -

ID: 43974342