Characterization of the omega class glutathione transferases

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

Characterization of the omega class glutathione transferases

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

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

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.

Original language	English
Pages (from-to)	204-206
Number of pages	3
Journal	Chemico-Biological Interactions
Volume	133
Issue number	1-3
Publication status	Published - 28 Feb 2001

Cite this

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title = "Characterization of the omega class glutathione transferases",

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.",

keywords = "Glutathione transferase superfamily, Omega class, X-ray crystallography",

author = "Board, {P. G.} and M. Coggan and G. Chelvanayagam and S. Easteal and Jermiin, {L. S.} and Schulte, {G. K.} and Danley, {D. E.} and Hoth, {L. R.} and Griffor, {M. C.} and Kamath, {A. V.} and Rosner, {M. H.} and Chrunyk, {B. A.} and Perregaux, {D. E.} and Gabel, {C. A.} and Geoghegan, {K. F.} and J. Pandit",

year = "2001",

month = feb,

day = "28",

language = "English",

volume = "133",

pages = "204--206",

journal = "Chemico-Biological Interactions",

issn = "0009-2797",

publisher = "Elsevier Ireland Ltd",

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TY - JOUR

T1 - Characterization of the omega class glutathione transferases

AU - Board, P. G.

AU - Coggan, M.

AU - Chelvanayagam, G.

AU - Easteal, S.

AU - Jermiin, L. S.

AU - Schulte, G. K.

AU - Danley, D. E.

AU - Hoth, L. R.

AU - Griffor, M. C.

AU - Kamath, A. V.

AU - Rosner, M. H.

AU - Chrunyk, B. A.

AU - Perregaux, D. E.

AU - Gabel, C. A.

AU - Geoghegan, K. F.

AU - Pandit, J.

PY - 2001/2/28

Y1 - 2001/2/28

N2 - 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.

AB - 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.

KW - Glutathione transferase superfamily

KW - Omega class

KW - X-ray crystallography

UR - http://www.scopus.com/inward/record.url?scp=0003207694&partnerID=8YFLogxK

M3 - Article

SN - 0009-2797

VL - 133

SP - 204

EP - 206

JO - Chemico-Biological Interactions

JF - Chemico-Biological Interactions

IS - 1-3

ER -

Characterization of the omega class glutathione transferases

Abstract

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