| First Author | Board PG | Year | 2000 |
| Journal | J Biol Chem | Volume | 275 |
| Issue | 32 | Pages | 24798-806 |
| PubMed ID | 10783391 | Mgi Jnum | J:70880 |
| Mgi Id | MGI:2148419 | Doi | 10.1074/jbc.M001706200 |
| Citation | Board PG, et al. (2000) Identification, characterization, and crystal structure of the Omega class glutathione transferases. J Biol Chem 275(32):24798-806 |
| abstractText | 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. |
