Authors
Shoma Araki, Takahisa Nakane, Yasuo Watanabe, Yukihiro Tsuchiya
Published in
The Journal of toxicological sciences. Volume 51. Issue 10. Pages 557-563.
Abstract
S-allyl-L-cysteine (SAC) is a major bioactive compound in aged black garlic with multiple pharmacological benefits, including antioxidant and neuroprotective effects; however, the underlying molecular mechanisms of these benefits remain unclear. In our previous study, we demonstrated that cystathionine γ-lyase (CSE), a sulfur-containing amino acid-metabolizing enzyme involved in the transsulfuration pathway, metabolizes S-nitroso-L-cysteine via a C-S lyase reaction. In this study, we investigated whether CSE-mediated metabolism is involved in the physiological effects of various cysteine derivatives, including SAC. We evaluated the potential of a series of S-alkylcysteine derivatives with varying alkyl chain lengths and degrees of unsaturation as CSE substrates. Recombinant CSE experiments revealed that thiol compounds were produced from propyl derivatives, whereas supersulfides were generated from ethyl, propyl, and allyl derivatives. Kinetic analysis demonstrated that the allyl derivative exhibited a stronger substrate affinity than the propyl derivative, similar to that of the endogenous substrate cystathionine. This study suggests a novel molecular basis for CSE-mediated metabolism and subsequent supersulfide production, which contributes to the diverse health-promoting effects of SAC in mammalian tissues.
PMID:
42816375
Bibliographic data and abstract were imported from PubMed on 01 Oct 2026.
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