Article
Identification of critical amino acids for 3,5,3'-triiodothyronine deiodination by human type 1 deiodinase based on comparative functional-structural analyses of the human, dog, and rat enzymes.
The Journal of biological chemistry - 12 Aug 1994
Toyoda N, Harney J W, Berry M J, Larsen P R
Abstract excerpt
The selenoenzyme, type 1 iodothyronine deiodinase (type 1 DI), catalyzes the activation of thyroxine (T4) to 3,5,3'-triiodothyronine (T3) but 3,3',5'-triiodothyronine (rT3) is the preferred substrate for the human enzyme. Since the dog type 1 DI has a significantly lower affinity for rT3, we clon...
Topics
- Amino Acid Sequence
- Amino Acids
- Animals
- Cells, Cultured
- DNA Mutational Analysis
- DNA, Complementary
- Dogs
- Humans
- Iodide Peroxidase
- Kinetics
- Molecular Sequence Data
- Mutation
- Rats
- Sequence Homology, Amino Acid
- Structure-Activity Relationship
- Triiodothyronine