Abstract

Changes in 24-alkene sterol product distribution resulting from deuterium substitution on the coenzyme methyl group of AdoMet and on the sterol acceptor molecule at C-23 and C-24 were used to determine kinetic isotope effects for the terminating deprotonations involved in sterol biomethylation catalyzed by (S)-adenosyl-L-methionine-Δ 24-sterol methyl transferase (SMT) enzyme. By this method 24(28)-methylene cycloartanol and cyclosadol were shown to be synthesized by two different SMT enzymes.

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