2grt
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HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, OXIDIZED GLUTATHIONE COMPLEX
OverviewOverview
Trypanosoma and Leishmania, pathogens responsible for diseases such as, African sleeping sickness, Chagas' heart disease, or Oriental sore, are, two of the very few genera that do not use the ubiquitous, glutathione/glutathione reductase system to keep a stable cellular redox, balance. Instead, they rely on trypanothione and trypanothione reductase, to protect them from oxidative stress. Trypanothione reductase (TR) and, the corresponding host enzyme, human red blood cell glutathione reductase, (GR), belong to the same flavoprotein family. Despite their closely, related three-dimensional structures and although their natural substrates, share the common structural glutathione core, the two enzymes are mutually, exclusive with respect to their disulfide substrates. This makes the, parasite ... [(full description)]
About this StructureAbout this Structure
2GRT is a [Single protein] structure of sequence from [Homo sapiens] with FAD and GDS as [ligands]. Active as [[1]], with EC number [1.6.4.2]. Full crystallographic information is available from [OCA].
ReferenceReference
Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity., Stoll VS, Simpson SJ, Krauth-Siegel RL, Walsh CT, Pai EF, Biochemistry. 1997 May 27;36(21):6437-47. PMID:9174360
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