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Redox regulation of cysteine-dependent enzymes.
J Anim Sci. 2010 Apr; 88(4):1297-306.JA

Abstract

It is well-established that maintenance of the intracellular redox (i.e., reduction-oxidation) state is critical for cell survival and that prolonged or abnormal perturbations toward oxidation result in cell dysfunction. This is exemplified by the widespread observation of oxidative stress in many pathological conditions, as well as the positive effects of antioxidants in treating certain conditions or extending the life span itself. In addition to the effects of oxidation on the lipid bilayer and modification of DNA in the nucleus, proteins are also modulated by the redox state. One of the primary targets of oxidation within a protein is the AA cysteine, whose thiol side chain is highly sensitive to all types of oxidizing agents. Although this sensitivity is used to prevent oxidation within the cell by potent defense mechanisms, such as glutathione, the use of cysteine in the active site of enzymes leaves them open to oxidant-mediated damage. Whether the damage is due to a pathological condition or to postmortem mediated loss of redox homeostasis, cysteine-dependent enzymes are targets of all forms of reactive oxygen, nitrogen, and sulfur species. A greater understanding of the redox-mediated control of cysteine-dependent enzymes opens the door to the selective use of antioxidants to prevent or reverse the cellular damage their inhibition causes.

Authors+Show Affiliations

Department of Gerontology, and the Sanders-Brown Center on Aging, University of Kentucky, Lexington, USA. rodneyg@uky.edu

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Review

Language

eng

PubMed ID

19820057

Citation

Guttmann, R P.. "Redox Regulation of Cysteine-dependent Enzymes." Journal of Animal Science, vol. 88, no. 4, 2010, pp. 1297-306.
Guttmann RP. Redox regulation of cysteine-dependent enzymes. J Anim Sci. 2010;88(4):1297-306.
Guttmann, R. P. (2010). Redox regulation of cysteine-dependent enzymes. Journal of Animal Science, 88(4), 1297-306. https://doi.org/10.2527/jas.2009-2381
Guttmann RP. Redox Regulation of Cysteine-dependent Enzymes. J Anim Sci. 2010;88(4):1297-306. PubMed PMID: 19820057.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Redox regulation of cysteine-dependent enzymes. A1 - Guttmann,R P, Y1 - 2009/10/09/ PY - 2009/10/13/entrez PY - 2009/10/13/pubmed PY - 2010/6/15/medline SP - 1297 EP - 306 JF - Journal of animal science JO - J Anim Sci VL - 88 IS - 4 N2 - It is well-established that maintenance of the intracellular redox (i.e., reduction-oxidation) state is critical for cell survival and that prolonged or abnormal perturbations toward oxidation result in cell dysfunction. This is exemplified by the widespread observation of oxidative stress in many pathological conditions, as well as the positive effects of antioxidants in treating certain conditions or extending the life span itself. In addition to the effects of oxidation on the lipid bilayer and modification of DNA in the nucleus, proteins are also modulated by the redox state. One of the primary targets of oxidation within a protein is the AA cysteine, whose thiol side chain is highly sensitive to all types of oxidizing agents. Although this sensitivity is used to prevent oxidation within the cell by potent defense mechanisms, such as glutathione, the use of cysteine in the active site of enzymes leaves them open to oxidant-mediated damage. Whether the damage is due to a pathological condition or to postmortem mediated loss of redox homeostasis, cysteine-dependent enzymes are targets of all forms of reactive oxygen, nitrogen, and sulfur species. A greater understanding of the redox-mediated control of cysteine-dependent enzymes opens the door to the selective use of antioxidants to prevent or reverse the cellular damage their inhibition causes. SN - 1525-3163 UR - https://www.unboundmedicine.com/medline/citation/19820057/Redox_regulation_of_cysteine_dependent_enzymes_ L2 - https://academic.oup.com/jas/article-lookup/doi/10.2527/jas.2009-2381 DB - PRIME DP - Unbound Medicine ER -