Cloning and sequencing of a human thioredoxin reductase.
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Gasdaska PY, Gasdaska JR, Cochran S, Powis G
Cloning and sequencing of a human thioredoxin reductase.
FEBS Lett. 1995 Oct 2;373(1):5-9.
- PubMed ID
- 7589432 [ View in PubMed]
- 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.