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Antioxidants 2018, 7(7), 86;

S-allylmercaptoglutathione Is a Substrate for Glutathione Reductase (E.C. from Yeast (Saccharomyces cerevisiae)

Department of Plant Physiology, RWTH Aachen University, 52056 Aachen, Germany
Institute of Organic Chemistry, RWTH Aachen University, 52056 Aachen, Germany
Author to whom correspondence should be addressed.
Received: 19 June 2018 / Revised: 28 June 2018 / Accepted: 4 July 2018 / Published: 6 July 2018
(This article belongs to the Special Issue Feature Papers in Antioxidants in 2018)
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Allicin (diallylthiosulfinate) is a potent thiol reagent and natural defense substance produced by garlic (Allium sativum) tissues when damaged. Allicin acts as a redox toxin and oxidizes the cellular glutathione (GSH) pool producing S-allylmercaptoglutathione (GSSA). The cellular enzyme glutathione reductase (GR) uses NADPH to reduce glutathione disulfide (GSSG) back to GSH and replenishes the GSH pool. It was not known whether GR could accept GSSA as a substrate. Here, we report that GR from yeast (Saccharomyces cerevisiae) shows Michaelis–Menten kinetics with GSSA as substrate in vitro (Km = 0.50 mM), but that GSSA is not as good a substrate as GSSG (Km = 0.07 mM). Furthermore, cells unable to synthesize GSH because the γ-glutamylcysteine synthetase (GSH1) gene is deleted, cannot grow without GSH supplementation and we show that the auxotrophic requirement for GSH in Δgsh1 mutants can be met by GSSA in the growth medium, suggesting that GSSA can be reduced to GSH in vivo. View Full-Text
Keywords: allicin; thiosulfinate; garlic; glutathione reductase allicin; thiosulfinate; garlic; glutathione reductase

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Horn, T.; Bettray, W.; Slusarenko, A.J.; Gruhlke, M.C.H. S-allylmercaptoglutathione Is a Substrate for Glutathione Reductase (E.C. from Yeast (Saccharomyces cerevisiae). Antioxidants 2018, 7, 86.

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