Shin-ichi Ohnuma

TL;DR: Comparisons of kinetic parameters of the mutated and wild type enzymes revealed several phenomena that may relate with the change of the ultimate chain length, which might suggest that the aromatic ring of tyrosine 81 blocks the chain elongation longer than FPP.

TL;DR: 20 FPP synthases, each of which has a different amino acid at position 81, are constructed and analyzed, and observations strongly indicate that the amino acid does not come into contact with the substrates but directly contacts the ω-terminal of an elongating allylic product.

TL;DR: Sequence analysis revealed that each mutant contained a few amino acid substitutions and that the mutation of Phe-77, which is located on the fifth amino acid upstream from the first aspartate-rich consensus motif, is the most effective for elongating the ultimate product.

TL;DR: An expression screening method for cloning the GGPP synthase gene is developed, which utilizes the carotenoid biosynthesis genes of Erwinia uredovora to visualize a clone expressing GG PP synthase, and a genomic DNA library from S. acidocaldarius is screened by using this method.

TL;DR: Six mutated archaeal GGPP synthases were constructed and it was revealed that the region around the first aspartate-rich motif is essential for the product specificity of all FPP synthase and that the mechanism of the chain termination in eukaryotic F PP synthases (type I) is different from those of prokaryoticFPP synthased (type II).