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Engineered selenium-containing glutaredoxin displays strong glutathione peroxidase activity rivaling natural enzyme

Ge, Y.; Qi, Z.; Wang, Y.; Liu, X.; Li, J.; Xu, J.; Liu, J.; Shen, J.

International Journal of Biochemistry and Cell Biology 41(4): 900-906

2008


ISSN/ISBN: 1357-2725
PMID: 18805505
DOI: 10.1016/j.biocel.2008.08.032
Accession: 022555827

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Insertion of selenocysteine (Sec) into protein scaffolds provides an opportunity for designing enzymes with improved and unusual catalytic properties. The use of a common thioredoxin fold with a high affinity for glutathione in glutaredoxin (Grx) and glutathione peroxidase (GPx) suggests a possibility of engineering Grx into GPx and vice versa.

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