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Catalytic Site Cysteines of Thiol Enzyme : Sulfurtransferases
Author
Source
Issue
Vol. 2011, Issue 2011 (31 Dec. 2011), pp.1-7, 7 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2010-12-28
Country of Publication
Egypt
No. of Pages
7
Main Subjects
Abstract EN
Thiol enzymes have single- or double-catalytic site cysteine residues and are redox active.
Oxidoreductases and isomerases contain double-catalytic site cysteine residues, which are oxidized to a disulfide via a sulfenyl intermediate and reduced to a thiol or a thiolate.
The redox changes of these enzymes are involved in their catalytic processes.
On the other hand, transferases, and also some phosphatases and hydrolases, have a single-catalytic site cysteine residue.
The cysteines are redox active, but their sulfenyl forms, which are inactive, are not well explained biologically.
In particular, oxidized forms of sulfurtransferases, such as mercaptopyruvate sulfurtransferase and thiosulfate sulfurtransferase, are not reduced by reduced glutathione but by reduced thioredoxin.
This paper focuses on why the catalytic site cysteine of sulfurtransferase is redox active.
American Psychological Association (APA)
Nagahara, Noriyuki. 2010. Catalytic Site Cysteines of Thiol Enzyme : Sulfurtransferases. Journal of Amino Acids،Vol. 2011, no. 2011, pp.1-7.
https://search.emarefa.net/detail/BIM-492343
Modern Language Association (MLA)
Nagahara, Noriyuki. Catalytic Site Cysteines of Thiol Enzyme : Sulfurtransferases. Journal of Amino Acids No. 2011 (2011), pp.1-7.
https://search.emarefa.net/detail/BIM-492343
American Medical Association (AMA)
Nagahara, Noriyuki. Catalytic Site Cysteines of Thiol Enzyme : Sulfurtransferases. Journal of Amino Acids. 2010. Vol. 2011, no. 2011, pp.1-7.
https://search.emarefa.net/detail/BIM-492343
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-492343