Artificial Substrates for Farnesylpyrophosphate Synthetase

Abstract

Some analogues of 3-methyl-2-butenylpyrophosphate (DMAPP) having a hetero atom or a cyclopropane ring were found to be a substrate for hog liver farnesylpyrophosphate synthetase. The enzymatic reaction products were analyzed by GLC, TLC and GC-MS. The structures of the products were elucidated to be a farnesyl-PP type. Among the artificial substrates the allylic-PP [3c] having a cyclopropane ring was the best suited. Although its K_m value was larger than that of DMAPP, the V_max values were almost the same between them. These results suggest that the "ionization-condensation-elimination" mechanism proposed by Poulter would be applicable to this enzymatic reaction and that this enzyme can have such a wide specificity that it may be widely applied to bioorganic synthesis.