Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1948264 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2009 | 12 Pages |
Abstract
Chemical approaches have also been used to study the enzymatic mechanism of thioredoxin reductase. The approach divides the enzyme into two modules, a large protein module lacking selenocysteine and a small, synthetic selenocysteine-containing peptide. Study of this semisynthetic enzyme has revealed three distinct enzymatic pathways that depend on the properties of the substrate. The enzyme utilizes a macromolecular mechanism for protein substrates, a second mechanism for small molecule substrates and a third pathway for selenium-containing substrates such as selenocystine.
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Authors
Robert J. Hondal,