Abstract
A carbon-sulfur lyase has been found in Tulbaghia violacea Harv. which is capable of acting on l-cysteine sulfoxides in a manner similar to the alliinase reaction described in the genus Allium. The enzyme has a substrate specificity similar to that of alliinase, and its activity is enhanced by pyridoxal phosphate. Cupric ion also stimulates its activity, but the enzyme does not appear to require copper as a co-factor. Amino acid sulfoxides found in the tissue give rise to pyruvate when treated with an enzymic preparation from T. violacea, indicating that the mechanism responsible for odor production in Tulbaghia is the same as that in Allium. Data are presented to support the classification of alliinase-like enzymes into two groups on the basis of optimal pH.
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