Cloning and sequencing of a human thioredoxin reductase

• Published in: FEBS letters Vol. 373; no. 1; pp. 5 - 9
• Main Authors: Gasdaska, Pamela Y., Gasdaska, John R., Cochran, Shawn, Powis, Garth
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 02.10.1995
• Subjects: Amino Acid Sequence; Animals; Bacteria - enzymology; Base Composition; Base Sequence; Cloning, Molecular; Escherichia coli - enzymology; Escherichia coli - genetics; Female; Glutathione Reductase - genetics; Human placenta; Humans; Mice; Molecular Sequence Data; Molecular Weight; Oligodeoxyribonucleotides; Open Reading Frames; Placenta - enzymology; Plants - enzymology; Pregnancy; Sequence Homology, Amino Acid; Thioredoxin reductase; Thioredoxin-Disulfide Reductase - biosynthesis; Thioredoxin-Disulfide Reductase - genetics; Thioredoxin-Disulfide Reductase - isolation & purification; Human placenta; Thioredoxin reductase
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(95)01003-W

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 redoxactive cysteines in the putative FAD binding domain and has a dimer interface domain not previously seen with prokaryote and lower eukaryote thioredoxin reductases.