Mutational analysis of human glutathione transferase A2-2 identifies structural elements supporting high activity with the prodrug azathioprine.

doi:10.1093/protein/gzs006

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Article

Mutational analysis of human glutathione transferase A2-2 identifies structural elements supporting high activity with the prodrug azathioprine.

Protein engineering, design & selection : PEDS - 1 Apr 2012

Modén Olof, Zhang Wei, Mannervik Bengt

Abstract excerpt

Glutathione transferase (GST) A2-2 is the human enzyme displaying the highest catalytic activity with the prodrug azathioprine (Aza). The reaction releases pharmacologically active 6-mercaptopurine by displacing the imidazole moiety from the Aza molecule. The GST-catalyzed reaction is of medical significance, since high rates of Aza activation may lead to adverse side effects in treated patients. The present...

Topics

Amino Acid Substitution
Animals
Azathioprine
Binding Sites
Catalysis
Glutathione Transferase
Humans
Immunosuppressive Agents
Kinetics
Mutation
Prodrugs
Rats
Structure-Activity Relationship
Substrate Specificity

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Open in PubMed

Identifiers

PMID: 22334756
DOI: 10.1093/protein/gzs006

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