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- W1697331194 abstract "Publisher Summary This chapter discusses about the S-substituted L-cysteine sulfoxide lyase from shiitake mushroom. Fruiting bodies of shiitake mushrooms (Lentinus edodes) give a characteristic flavor on maceration of the fresh mushroom and on rehydration of the dried mushroom. Studies have demonstrated that the principal flavor component lenthionine (1,2,3,5,6-pentathiepane) arises enzymatically from the nonvolatile precursor which was identified as 2-(γ-glutamylamino)-4,6,8,9, 10-pentaoxo-4,6,8,10-tetrathio-undecanoic acid. At least two distinct enzymes are involved in the sequence of action; one is γ-glutamyltransferase which acts on lentinic acid to liberate the γ-glutamyl moiety and the other is the S-substituted L-cysteine sulfoxide lyase which acts on the primary product, degluta-myllentinic acid, to produce ammonia, pyruvate, and a thiosulfinate by catalyzing a β-elimination reaction similar to that catalyzed by Allium alliinases. The thiosulfinate produces lenthionine, probably spontaneously. The enzyme can be assayed by measuring the rate of pyrurate formation. Pyruvate is conveniently estimated by the color intensity of its 2,4-dinitrophenylhyrazone in alkali, or more precisely, by NADH oxidation in a coupled reaction with lactate dehydrogenase." @default.
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- W1697331194 date "1987-01-01" @default.
- W1697331194 modified "2023-09-26" @default.
- W1697331194 title "S-Substituted l-cysteine sulfoxide lyase from shiitake mushroom" @default.
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- W1697331194 doi "https://doi.org/10.1016/0076-6879(87)43076-0" @default.
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