Delineation of xenobiotic substrate sites in rat glutathione S‐transferase M1‐1

Glutathione S‐transferases catalyze the conjugation of glutathione with endogenous and exogenous xenobiotics. Hu and Colman (1995) proposed that there are two distinct substrate sites in rat GST M1‐1, a 1‐chloro‐2,4‐dintrobenzene (CDNB) substrate site located in the vicinity of tyrosine‐115, and a m...

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Veröffentlicht in:	Protein science 2005-10, Vol.14 (10), p.2526-2536
Hauptverfasser:	Hearne, Jennifer L., Colman, Roberta F.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution - genetics Animals Binding Sites - genetics BTP, 1,3‐Bis [tris (hydroxymethyl) methylamino] propane CD, circular dichroism CDNB, 1‐chloro‐2,4‐dinitrobenzene DMF, N,N′‐dimethylformamide EDTA, disodium ethylenediamine tetraacetate ESI‐MS, electrospray ionization mass spectrometry glutathione S‐transferase M1‐1 Glutathione Transferase - chemistry Glutathione Transferase - genetics Glutathione Transferase - metabolism GSH, glutathione GST, glutathione S‐transferase IPTG, isopropyl‐β‐D‐thiogalactoside Kinetics LB, Luria‐Bertani mBBr, monobromobimane, 4‐bromo‐methyl‐3,6,7‐trimethyl‐1,5‐diazabicyclo‐[3.3.0]octa‐3,6‐diene‐2,8‐dione Tris, Tris(hydroxymethyl)aminomethane monobromobimane Mutagenesis, Site-Directed Protein Binding - genetics Protein Structure, Secondary Rats rpm, revolutions per minute site‐directed mutagenesis substrate site Substrate Specificity TFA, trifluoro‐acetic acid Xenobiotics - chemistry Xenobiotics - metabolism
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