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Article

The evolution of catalytic efficiency and substrate promiscuity in human theta class 1-1 glutathione transferase.

Journal of molecular biology - 1 Dec 2006

Griswold Karl E, Aiyappan Nandini S, Iverson Brent L, Georgiou George

Abstract excerpt

Theta class glutathione transferases (GST) from various species exhibit markedly different catalytic activities in conjugating the tripeptide glutathione (GSH) to a variety of electrophilic substrates. For example, the human theta 1-1 enzyme (hGSTT1-1) is 440-fold less efficient than the rat theta 2-2 enzyme (rGSTT2-2) with the fluorogenic substrate 7-amino-4-chloromethyl coumarin (CMAC). Large libraries of...

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Identifiers

PMID: 17011574
DOI: 10.1016/j.jmb.2006.09.012
PMCID: PMC1995603

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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