Abstract

1. 1. An enzyme that catalyses the synthesis of lanthionine from cysteine was purified 20-fold from the larval fat body of the silkworm, Bombyx mori. 2. 2. The pH optimum is 9.0 and pyridoxal phosphate is a necessary cofactor. 3. 3. From the present results, it seemed plausible that the enzyme catalyses the reaction of substitution at the β-carbon atom of cysteine or serine, resulting in formation of cystathionine or lanthionine in the presence of homocysteine or cysteine as a cosubstrate in the second reaction stage in B. mori.

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