2014
DOI: 10.1002/ange.201402000
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Substrate Profiling of Glutathione S‐transferase with Engineered Enzymes and Matched Glutathione Analogues

Abstract: The identification of specific substrates of glutathione S‐transferases (GSTs) is important for understanding drug metabolism. A method termed bioorthogonal identification of GST substrates (BIGS) was developed, in which a reduced glutathione (GSH) analogue was developed for recognition by a rationally engineered GST to label the substrates of the corresponding native GST. A K44G‐W40A‐R41A mutant (GST‐KWR) of the mu‐class glutathione S‐transferases GSTM1 was shown to be active with a clickable GSH analogue (GS… Show more

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Cited by 3 publications
(4 citation statements)
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“…Contributing to the recent effort toward substrate profiling for a wide range of transferases, Deng and colleagues formulated a technique called 'bioorthogonal identification of GST substrates' (BIGS) by developing allele-specific pair of GST mutant and modified reduced glutathione. 117 Upon analysis of the crystal structure of GSTM1 from S. japonicum, they generated a K44G/W40A/ R41A triple mutant (GST-KWR) that was able to modify a homopropargylic ester of GSH (GSH-R1) as its substrate with efficiency comparable to the wild-type GSTM1-GSH pair (Figure 9C). Although the mutant was still active toward GSH, it showed preference toward modified GSH in a competitive assay, demonstrating its functional orthogonality.…”
Section: Acs Chemical Biologymentioning
confidence: 99%
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“…Contributing to the recent effort toward substrate profiling for a wide range of transferases, Deng and colleagues formulated a technique called 'bioorthogonal identification of GST substrates' (BIGS) by developing allele-specific pair of GST mutant and modified reduced glutathione. 117 Upon analysis of the crystal structure of GSTM1 from S. japonicum, they generated a K44G/W40A/ R41A triple mutant (GST-KWR) that was able to modify a homopropargylic ester of GSH (GSH-R1) as its substrate with efficiency comparable to the wild-type GSTM1-GSH pair (Figure 9C). Although the mutant was still active toward GSH, it showed preference toward modified GSH in a competitive assay, demonstrating its functional orthogonality.…”
Section: Acs Chemical Biologymentioning
confidence: 99%
“…As an interesting application, the GST-KWR and GSH-R1 pair was used to identify multiple substrates, such as cyclodopaglucoside and callystatin A, from the Chinese herbal medicine Ganmaochongli using LC-MS/MS of the enriched sample (Figure 9C). 117 Recently, Ahn and colleagues have demon- versatile handle for profiling and characterizing cellular glutathionylation. 118 β-Galactosyltransferase.…”
Section: Acs Chemical Biologymentioning
confidence: 99%
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