TrxR Yeast

Thioredoxin reductase is a member of the dimeric flavoenzyme family. It contains a flavin adenine dinucleotide (FAD) prosthetic group and operates as a homodimer. Each monomer consists of an FAD-binding domain, a NADPH-binding domain, and a thioredoxin-binding domain . The enzyme’s active site contains a redox-active disulfide/dithiol within a conserved CxxC motif, which is essential for its catalytic activity .

Thioredoxin reductase is pivotal in maintaining the redox state of the cell by reducing oxidized thioredoxin. Reduced thioredoxin, in turn, participates in various cellular processes, including DNA synthesis, repair, and defense against oxidative stress . The enzyme is also involved in the regulation of transcription factors and the activation of ribonucleotide reductase, which is essential for DNA synthesis .

Recombinant thioredoxin reductase from yeast is produced through the expression of the thioredoxin reductase gene in yeast cells. This recombinant enzyme retains the functional properties of its native counterpart and is used extensively in research and industrial applications . The yeast expression system offers several advantages, including ease of genetic manipulation, rapid growth, and the ability to perform post-translational modifications .

Recombinant thioredoxin reductase is widely used in biochemical and biophysical studies to understand the enzyme’s structure-function relationship. It is also employed in the development of therapeutic agents targeting redox-related diseases and in the production of recombinant proteins that require a reducing environment for proper folding .