A selective inactivation of dimethylallyl-transfering activity of prenyltransferase.

  title={A selective inactivation of dimethylallyl-transfering activity of prenyltransferase.},
  author={Kyozo Ogura and Takako Koyama and Shuichi Seto},
  journal={Biochemical and biophysical research communications},
  volume={35 6},
4 Citations
Crystallization and partial characterization of prenyltransferase from avian liver.
This is the first preparation of a stable crystalline enzyme of sterol and terpene biosynthesis and it has been shown to be homogeneous by polyacrylamide gel electrophoresis at pH 8.4, and by electrophoreis in sodium dodecyl sulfate containing gels.
Substrate Binding of avian liver prenyltransferase.
Data are interpreted to indicate that each subunit of avian liver prenyltransferase has a single allylic binding site accommodating dimethylallyl, geranyl, and farnesyl pyrophosphates, and one binding site for isopentenyl pyphosphate.
Biosynthesis of carotenoids
The carotenoids that are found in the photosynthetic pigment-protein complexes of higher plants, algae and phototrophic bacteria, including cyanobacteria, are C40 tetraterpenes. They are


Properties of farnesyl pyrophosphate synthetase of pig liver.
The purification of 3,3-dimethylallyl- and geranyl-transferase and of isopentenyl pyrophosphate isomerase from pig liver.
From product-inhibition studies of the geranyltransferase reaction, the order of addition of substrates to and release of products from the enzyme has been deduced: geranyl pyroph phosphate combines with the enzyme first, followed by isopentenyl pyrophosphate.
γ,γ-Dimethyl-allyl-pyrophosphat und Geranyl-pyrophosphat, biologische Vorstufen des Squalens Zur Biosynthese der Terpene, VI1)
3-Methyl-Δ3-butenyl-1-pyrophosphat (Isopentenyl-pyrophosphat) spielt im Stoffwechsel die Rolle eines „aktiven Isoprens”, d. h. es ist der gemeinsame Baustein aller unter die „Isoprenregel” fallenden