22 イソプレノイド生合成における鎖延長機構 : Bacillus stearothermophilusのプレニルトランスフェラーゼ遺伝子のクローニングとその解析(口頭発表の部)

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Prenyltransferases catalyze the sequential condensation of isopentenyl diphosphate (IPP) with allylic diphosphates to produce prenyl diphosphates with various chain lengths and stereochemistries. They are extremely interesting from both mechanistic and synthetic view points in that they catalyze the repetition of stereospecific condensation of IPP with prenyl diphosphates to give products with certain chain lengths and stereochemistries fixed by the specificities of the individual enzymes (Scheme 1). In order to extend the comparative study of prenyltransferase structures, and also to elucidate the molecular mechanisms of the catalytic function, we isolated and sequenced the gene for farnesyl diphosphate (FPP) synthase from a thermophilic bacterium, Bacillus stearothermophilus. We also succeeded in the overproduction in Escherichia coli of this thermostable enzyme, its purification to homogeneity, and crystallization. Molecular cloning of heptaprenyl diphosphate (Hep-PP) synthase of the same bacterium was also achieved by application of PCR reactions using some nucleotide probes whose sequences were found to be characteristic of prenyltransferase genes. As a result, this enzyme was proved to consist of two different proteins with molecular masses of 25kDa (Component A) and 36kDa (Component B). The amino acid sequence of Component B showed 31.9% and 31.8% similarities with those of FPP synthase of the same bacterium and hexaprenyl diphosphate (Hex-PP) synthase of Saccharomyces cerevisiae, respectively. In contrast, Compond A had no such similarities.
天然有機化合物討論会の論文
1994-09-20

22 イソプレノイド生合成における鎖延長機構 : Bacillus stearothermophilusのプレニルトランスフェラーゼ遺伝子のクローニングとその解析(口頭発表の部)

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