Farnesyl pyrophosphate synthetase located in microsomes from pig liver.
The microsomes from pig liver contained farnesyl pyrophosphate synthetase and it was solubilized with Triton X-100. The microsomal enzyme had a pH optimum of 6.5-7.0 and required Mg2+ or Mn2+ for maximum activity. Dimethylallyl-transferring activity of the enzyme was much lower compared with the geranyl-transferring activity. In the presence of Triton X-100, the geranyl-transferring activity was about two-fold activated whereas the dimethylallyl-transferring activity was almost the same.
D000818:Animals; D003600:Cytosol / Q000201:enzymology; D004122:Dimethylallyltranstransferase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008670:Metals; D008862:Microsomes, Liver / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology; D012995:Solubility; D013552:Swine; D014166:Transferases / Q000378:metabolism*
D008670:Metals; D014166:Transferases; D004122:Dimethylallyltranstransferase