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Antioxidants & redox signaling
Mar 15, 2011;14 (6): 1065-77.

Cysteine-based redox switches in enzymes.

Chananat Klomsiri, P Andrew Karplus, Leslie B Poole
Author Information
  1. Chananat Klomsiri: Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem, North Carolina 27157, USA.
PMID: 20799881 DOI: 10.1089/ars.2010.3376

Abstract

The enzymes involved in metabolism and signaling are regulated by posttranslational modifications that influence their catalytic activity, rates of turnover, and targeting to subcellular locations. Most prominent among these has been phosphorylation/dephosphorylation, but now a distinct class of modification coming to the fore is a set of versatile redox modifications of key cysteine residues. Here we review the chemical, structural, and regulatory aspects of such redox regulation of enzymes and discuss examples of how these regulatory modifications often work in concert with phosphorylation/dephosphorylation events, making redox dependence an integral part of many cell signaling processes. Included are the emerging roles played by peroxiredoxins, a family of cysteine-based peroxidases that now appear to be major players in both antioxidant defense and cell signaling.

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Grants

  1. R01 GM050389/NIGMS NIH HHS
  2. R01 GM075304/NIGMS NIH HHS
  3. R33 CA126659/NCI NIH HHS

MeSH Term

Animals
Cysteine
Enzymes
Humans
Models, Biological
Oxidation-Reduction
Peroxiredoxins
Phosphorylation
Protein Processing, Post-Translational
Signal Transduction

Chemicals

Enzymes
Peroxiredoxins
Cysteine
Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Review
Article has an altmetric score of 11

Word Cloud

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