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Identification, characterization, and crystal structure of the Omega class glutathione transferases.

The Journal of biological chemistry (2000-04-28)
P G Board, M Coggan, G Chelvanayagam, S Easteal, L S Jermiin, G K Schulte, D E Danley, L R Hoth, M C Griffor, A V Kamath, M H Rosner, B A Chrunyk, D E Perregaux, C A Gabel, K F Geoghegan, J Pandit
ABSTRACT

A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-A resolution and has a characteristic GST fold (Protein Data Bank entry code ). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit. Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.

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Millipore
Glutathione−Agarose, lyophilized powder