Abstract
Purification of Geranylgeranyl Pyrophosphate Synthetase from Micrococcus lysodeikticus
Highlights
Since the enzyme purification achieved in this study did not result in the isolation of an unequivocally homogeneous protein, it remains uncertain whether one or several enzymes are involved in the biosynthesis of geranylgeranyl pyrophosphate from isopentenyl pyrophosphate and the three ally1 pyrophosphates
The purified preparation appeared to be homogeneous by electrophoretic criteria and in column chromatographic studies with Sephadex G-200
Sedimentation velocity analysis revealed the presence of a minor contaminant estimated to be 4.7% of the total protein
Summary
Farnesol (Givaudan-Delawanna, Inc., New York), geraniol (Puriss, Aldrich Chemical Company, Inc., Milwaukee), and dimethylallyl alcohol were redistilled under reduced pressure and pyrophosphorylated by the method described by Cramer and. The finding that heating and enzyme concentration differentially affect the reaction rates with dimethylallyl-PP and farnesyl-PP indicates that the structure or conformation of the enzyme protein can be so modified as to alter the relative specificity of the enzyme for the three substrates. For this reason, the effect of urea on the activity of the enzyme for the three substrates was investigated. The effect of urea on enzyme activity with geranyl-PP appears, at least in some respects, to be intermediate between that for reactions with dimethylallyl-PP and farnesyl-PP
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