Evolution of the active site of human glutathione transferase A2-2 for enhanced activity with dietary isothiocyanates

• Published in: Biochimica et biophysica acta Vol. 1850; no. 4; pp. 742 - 749
• Main Authors: Zhang, Wei, Dourado, Daniel F.A.R., Mannervik, Bengt
• Format: Journal Article
• Language: English
• Published: Netherlands 01.04.2015
• Subjects: active sites; biotransformation; Catalysis; Catalytic Domain; chemical defenses; Detoxication; Diet; Directed evolution; Enzyme engineering; evolutionary adaptation; excretion; food plants; glucosinolates; glutathione; Glutathione transferase; Glutathione Transferase - chemistry; Glutathione Transferase - metabolism; Humans; Isoenzymes - chemistry; Isoenzymes - metabolism; Isothiocyanate; isothiocyanates; Isothiocyanates - pharmacology; microorganisms; mutagenesis; mutants; neoplasms; phytophagous insects; protective effect; Substrate Specificity; thioglucosidase; tissues; toxicity; Detoxication; Isothiocyanate; Directed evolution; Enzyme engineering; Glutathione transferase

Organic isothiocyanates (ITCs) are produced by plants, in which they are released from glucosinolates by myrosinase. ITCs are generally toxic and serve as a chemical defense against herbivorous insects and against infections by microorganisms. In mammalian tissues subtoxic concentrations of ITCs can...