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Article

Characterization of putative hydrophobic substrate binding site residues of a Delta class glutathione transferase from Anopheles dirus.

Archives of biochemistry and biophysics - 1 Nov 2008

Lerksuthirat Tassanee, Ketterman Albert J

Abstract excerpt

To date, investigations of the hydrophobic substrate site of the insect Delta class glutathione transferase are limited in number. In the present study, putative hydrophobic site residues of AdGSTD4-4 have been proposed and characterized. These residues are Gln-112, Thr-174, Phe-212, Arg-214, Tyr-215 and Phe-216. It was found that Gln-112 does not contribute significantly to the catalytic properties of AdGSTD4-4....

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PMID: 18760991
DOI: 10.1016/j.abb.2008.08.006

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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