Cloning and sequencing of a human thioredoxin reductase
- 2 October 1995
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 373 (1), 5-9
- https://doi.org/10.1016/0014-5793(95)01003-w
Abstract
The DNA sequence encoding human placental thioredoxin reductase has been determined. Of the 3826 base pairs sequenced, 1650 base pairs were in an open reading frame encoding a mature protein with 495 amino acids and a calculated molecular mass of 54,171. Sequence analysis showed strong similarity to glutathione reductases and other NADPH-dependent reductases. Human thioredoxin reductase contains the redox-active cysteines in the putative FAD binding domain and has a dimer interface domain not previously seen with prokaryote and lower eukaryote thioredoxin reductases.Keywords
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