Abstract
Thiaisoleucine (2-amino-3-methylthiobutyrate) completely inhibited the growth of strain K-12 of Escherichia coli at a concentration of 5 × 10−3m. The inhibition was antagonized by growth-factor amounts of l-isoleucine. Thiaisoleucine inhibited the deamination of threonine and the transfer of 14C-isoleucine to soluble ribonucleic acid and underwent transamination with α-ketoglutarate as the amino acceptor. In each case, the analogue appeared to be less effective than isoleucine as either an inhibitor or substrate.
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