Protein oxidation: An overview of metabolism of sulphur containing amino acid, Cysteine

Ahmad, S and Khan, H. and Shahab, U. and Rehman, S and Rafi, Z. and Khan, M.Y and Ansari, A. and Siddiqui, Z. and Ashraf, J.M. and Abdullah, S.M.S., and Habib, S. and Uddin ., M (2017) Protein oxidation: An overview of metabolism of sulphur containing amino acid, Cysteine. Frontiers in Bioscience - Scholar, 9 (1). pp. 71-87. ISSN 19450516

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Official URL: https://www.bioscience.org/2017/v9s/af/474/list.ht...

Abstract

The available data suggest that among cellular constituents, proteins are the major target for oxidation primarily because of their quantity and high rate of interactions with ROS. Proteins are susceptible to ROS modifications of amino acid side chains which alter protein structure. Among the amino acids, Cysteine (Cys) is more prone to oxidation by ROS because of its high nucleophilic property. The reactivity of Cys with ROS is due to the presence of thiol group. In the oxidised form, Cys forms disulfide bond, which are primary covalent cross-link found in proteins, and which stabilize the native conformation of a protein. Indirect evidence suggests that thiol modifications by ROS may be involved in neurodegenerative disorders, but the significance and precise extent of the contributions are poorly understood. Here, we review the role of oxidized Cys in different pathological consequences and its biochemistry may increase the research in the discovery of new therapies. The purpose of this review is to re-examine the role and biochemistry of oxidised Cys residues.

Item Type: Article
Uncontrolled Keywords: Cys; Cysteine; Disulfide bond; Protein oxidation; Reactive oxygen species; Review; ROS; Sulphur containing amino acids; Thiol group
Subjects: R Medicine > R Medicine (General)
Divisions: Faculties > Faculty of Medicine > J.N. Medical College
Depositing User: AMU Library
Date Deposited: 29 Jan 2018 07:20
Last Modified: 01 Feb 2018 05:33
URI: http://ir.amu.ac.in/id/eprint/11011

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