* Your assessment is very important for improving the workof artificial intelligence, which forms the content of this project
Download Structure-function study of the C-terminal tail of Thioredoxin Reductase
Citric acid cycle wikipedia , lookup
Butyric acid wikipedia , lookup
Bottromycin wikipedia , lookup
Ribosomally synthesized and post-translationally modified peptides wikipedia , lookup
Western blot wikipedia , lookup
Gaseous signaling molecules wikipedia , lookup
Peptide synthesis wikipedia , lookup
Protein adsorption wikipedia , lookup
Protein moonlighting wikipedia , lookup
Genetic code wikipedia , lookup
Protein structure prediction wikipedia , lookup
Enzyme inhibitor wikipedia , lookup
Proteolysis wikipedia , lookup
Expanded genetic code wikipedia , lookup
Evolution of metal ions in biological systems wikipedia , lookup
Point mutation wikipedia , lookup
Catalytic triad wikipedia , lookup
List of types of proteins wikipedia , lookup
Structure-function study of the C-terminal tail of Thioredoxin Reductase Thioredoxin reductase (TR) is an enzyme that functions in maintaining cellular redox homeostasis and protecting the cell from oxidative damage. TR is the only enzyme that reduces the protein thioredoxin, which functions in further reducing proteins and other cellular substrates. This system works as an antioxidant that protects the cell from damaging molecules like hydrogen peroxide and oxygen metabolism byproducts. This project seeks to identify crucial amino acid residues present in TR that help orient the enzyme’s unique C-terminal tail, which contains the adjacent cysteine residues responsible for thioredoxin reduction. Mutation of positively charged lysine (K) residues to the neutral amino acid alanine (A) at positions 26 and 121 of TR resulted in significantly decreased enzymatic activity towards lipoic acid, a substrate that mimics the C-terminus of TR. TR is a popular target for anti-tumor therapy, and understanding the full mechanism may further the development of anti-tumor drugs.