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  • Title: Formation of a stable and catalytically active complex of the two essential components of hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26.
    Author: Yoshida I, Koyama T, Ogura K.
    Journal: Biochem Biophys Res Commun; 1989 Apr 28; 160(2):448-52. PubMed ID: 2541701.
    Abstract:
    Formation of a stable complex of the two essential components of hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26, which represents the catalytically active state of this enzyme, is observed in the presence of a relatively high concentrations of inorganic pyrophosphate or one of the substrates, isopentenyl diphosphate or farnesyl diphosphate. The apparent molecular mass of the complex is estimated to be about 50 kDa by gel filtration with Superose 12.
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