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FEBS Lett. 1999 Jan 8;442(1):105-11.

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

Author information

1
Arizona Cancer Center, University of Arizona, Tucson 85724-5024, USA.

Abstract

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.

PMID:
9923614
DOI:
10.1016/s0014-5793(98)01638-x
[Indexed for MEDLINE]
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