Escherichia coli cyclopropane fatty acid synthase.

Escherichia coli fatty acid cyclopropane synthase (CFAS) was overproduced and purified as a His6-tagged protein. This recombinant enzyme is as active as the native enzyme with a Km of 90 microm for S-AdoMet and a specific activity of 5 x 10(-2) micromol.min(-1).

Synthesis and evaluation of analogues of S-adenosyl-L-methionine, as inhibitors of the E. coli cyclopropane fatty acid synthase.

Analogues of S-adenosyl-L-methionine were synthesized and evaluated as inhibitors of the purified E. coli cyclopropane fatty acid synthase, a model for M. tuberculosis cyclopropane synthases that are potential targets for antituberculous drugs.