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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
biochemistry, genetics and molecular biology
X‐ray crystal structures of cytosolic glutathione S‐transferases: Implications for protein architecture, substrate recognition and catalytic function
European Journal of Biochemistry, Volume 220, No. 3, Year 1994
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Description
Crystal structures of cytosolic glutathione S‐transferases (EC 2.5.1.18), complexed with glutathione or its analogues, are reviewed. The atomic models define protein architectural relationships between the different gene classes in the superfamily, and reveal the molecular basis for substrate binding at the two adjacent subsites of the active site. Considerable progress has been made in understanding the mechanism whereby the thiol group of glutathione is destabilized (lowering its pKa) at the active site, a rate‐enhancement strategy shared by the soluble glutathione S‐transferases. Copyright © 1994, Wiley Blackwell. All rights reserved
Authors & Co-Authors
Dirr, Heini W.
South Africa, Johannesburg
University of the Witwatersrand
Germany, Planegg
Max-planck-institut Für Biochemie
Reinemer, Peter
Germany, Planegg
Max-planck-institut Für Biochemie
Huber, Robert
Germany, Planegg
Max-planck-institut Für Biochemie
Statistics
Citations: 381
Authors: 3
Affiliations: 2
Identifiers
Doi:
10.1111/j.1432-1033.1994.tb18666.x
ISSN:
00142956
e-ISSN:
14321033
Research Areas
Genetics And Genomics