The Mechanism of High M r Thioredoxin Reductase from Drosophila melanogaster
Open Access
- 1 August 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (35) , 33020-33028
- https://doi.org/10.1074/jbc.m303762200
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Three-dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine-dependent enzymeProceedings of the National Academy of Sciences, 2001
- Substitution of the Thioredoxin System for Glutathione Reductase in Drosophila melanogasterScience, 2001
- Thioredoxin reductaseEuropean Journal of Biochemistry, 2000
- Twists in Catalysis: Alternating Conformations of Escherichia coli Thioredoxin ReductaseScience, 2000
- Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequenceProceedings of the National Academy of Sciences, 2000
- Thioredoxin Reductase from Plasmodium falciparum: Evidence for Interaction between the C-Terminal Cysteine Residues and the Active Site Disulfide−DithiolBiochemistry, 1999
- Human Placenta Thioredoxin ReductaseJournal of Biological Chemistry, 1998
- Recombinant putative glutathione reductase of Plasmodium falciparum exhibits thioredoxin reductase activityMolecular and Biochemical Parasitology, 1996
- Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene.Proceedings of the National Academy of Sciences, 1996
- A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity.Proceedings of the National Academy of Sciences, 1996