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Substrate profiling of glutathione S-transferase with engineered enzymes and matched glutathione analogues.
Feng, Shan; Zhang, Lei; Adilijiang, Gulishana; Liu, Jieyuan; Luo, Minkui; Deng, Haiteng.
Afiliação
  • Feng S; MOE Key Laboratory of Bioinformatics, School of Life Sciences, Renhuan Building 301, Tsinghua University, 100084 Beijing (China).
Angew Chem Int Ed Engl ; 53(28): 7149-53, 2014 Jul 07.
Article em En | MEDLINE | ID: mdl-24889263
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 (GSH-R1) as the cosubstrate. The GSH-R1 conjugation products can react with an azido-based biotin probe for ready enrichment and MS identification. Proof-of-principle studies were carried to detect the products of GSH-R1 conjugation to 1-chloro-2,4-dinitrobenzene (CDNB) and dopamine quinone. The BIGS technology was then used to identify GSTM1 substrates in the Chinese herbal medicine Ganmaocongji.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Ano de publicação: 2014 Tipo de documento: Article