The C-S Lyases of Higher Plants

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Abstract
Cystine lyase degrades L-cystine by a .beta.-elimination to form cysteine persulfide, pyruvate, and ammonia. This enzyme is common in Brassica sp. and has been purified to homogeneity from extracts of broccoli (Brassica oleracea var. botrytis) buds. Two isozymes were separated on DEAE-Fractogel columns and the first peak, cystine lyase I further purified to homogeneity. The purified enzyme had a narrow range of substrate specificity with L-cystine and S-alkyl-L-cysteine sulfoxides being the primary substrates. The Km for L-cystine was 1.9 millimolar and for S-ethyl-L-cysteine sulfoxide was 15.6 millimolar, suggesting that L-cystine would be preferred in vivo. Using gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis the molecular weight of the holoenzyme was estimated as 152,000 composed of subunits of approximately 49,000. This strongly suggests the native enzyme is a trimer. The presence of carbohydrate in the native enzyme was detected at the level of 5.8% on a weight basis. Except for the ability to utilize L-cystine as a substrate there are many similarities between cystine lyase I and the alliin lyase of onion (Allium cepa).