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Redox regulation and trapping sulphenic acid in the peroxide sensitive human mitochondrial branched chain aminotransferase

Coles, Steven; Hutson, Susan M.; Poole, Leslie B.; Conway, Myra E.

Authors

Steven Coles

Susan M. Hutson

Leslie B. Poole

Myra Conway Myra.Conway@uwe.ac.uk
Occasional Associate Lecturer - CHSS - DAS



Contributors

Abstract

The human branched chain aminotransferase enzymes are key regulators of glutamate metabolism in the brain and are among a growing number of redox-sensitive proteins. Studies that use thiol-specific reagents and electrospray ionization mass spectrometry demonstrate that the mitochondrial BCAT enzyme has a redox-active CXXC center, which on oxidation forms a disulfide bond (RSSR), via a cysteine sulfenic acid intermediate. Mechanistic details of this redox regulation were revealed by the use of mass spectrometry and dimedone modification. We discovered that the thiol group at position C315 of the CXXC motif acts a redox sensor, whereas the thiol group at position C318 permits reversible regulation by forming an intrasubunit disulphide bond. Because of their roles in redox regulation and catalysis, there is a growing interest in cysteine sulphenic acids. Therefore, development of chemical tags/methods to trap these transient intermediates is of immense importance. © 2008 Humana Press, a part of Springer Science+Business Media, LLC.

Journal Article Type Article
Publication Date Dec 1, 2008
Journal Methods in Molecular Biology
Print ISSN 1064-3745
Publisher Humana Press
Peer Reviewed Not Peer Reviewed
Volume 476
Pages 139-152
Series Title Methods in Molecular Biology
DOI https://doi.org/10.1007/978-1-59745-129-1_10
Keywords molecular biology, redox-mediated signal transduction, sulphenic acid, human mitochondrial branched chaim aminotransferase
Public URL https://uwe-repository.worktribe.com/output/1008215
Publisher URL http://www.springerprotocols.com/BookToc/doi/10.1007/978-1-59745-129-1