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Characterization of the Omega class glutathione transferases

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Date

2001

Authors

Board, Philip
Coggan, Marjorie
Chelvanayagam, Gareth
Easteal, Simon
Jermiin, Lars Sommer
Schulte, Jurgen
Danley, D
Hoth, L
Griffor, M
Kamath, A

Journal Title

Journal ISSN

Volume Title

Publisher

Elsevier

Abstract

The Omega class of glutathione transferases (GST) has been discovered by analysis of the expressed sequence tag database and sequence alignment. 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 crystal structure indicates that GSTO 1-1 has a characteristic GST fold. Unlike other mammalian glutathione transferases, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.

Description

Keywords

Keywords: Glutathione transferase superfamily; Omega class; X-ray crystallography

Citation

URI

http://hdl.handle.net/1885/90731

Collections

ANU Research Publications

Source

Chemico-Biological Interactions

Type

Journal article

Book Title

Entity type

Access Statement

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