Cloning, sequencing and functional expression of a novel human thioredoxin reductase

• Published in: FEBS letters Vol. 442; no. 1; pp. 105 - 111
• Main Authors: Gasdaska, Pamela Y., Berggren, Margareta M., Berry, Marla J., Powis, Garth
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 08.01.1999
• Subjects: Amino Acid Sequence; Base Sequence; Catalytic Domain - genetics; Cell Line; Cloning, Molecular; Conserved Sequence; DNA, Complementary - genetics; Female; Gene Expression; Glutathione Reductase - genetics; Human; Humans; Male; Molecular Sequence Data; Molecular Weight; Nucleic Acid Conformation; Pregnancy; RNA, Messenger - chemistry; RNA, Messenger - genetics; RNA, Messenger - metabolism; Sequence Homology, Amino Acid; Thioredoxin reductase; Thioredoxin-Disulfide Reductase - chemistry; Thioredoxin-Disulfide Reductase - genetics; Thioredoxin-Disulfide Reductase - metabolism; Tissue Distribution; Transfection; Human; Thioredoxin reductase
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(98)01638-X

The DNA sequence encoding a novel human thioredoxin reductase has been determined. The protein is predicted to have 524 amino acids including a conserved -Cys-Val-Asn-Val-Gly-Cys catalytic site and a selenocysteine containing C-terminal -Gly-Cys-SeCys-Gly. The predicted molecular mass is 56.5. The newly identified TR sequence exhibits 54% identity to a previously reported human thioredoxin reductase and 37% identity to human glutathione reductase. Transient transfection of human embryonal kidney cells results in a 5-fold increase in thioredoxin reductase activity but no increase in glutathione reductase activity.