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Volume 272, Number 8, Issue of February 21, 1997 pp. 5192-5198
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Conversion from Archaeal Geranylgeranyl Diphosphate Synthase to Farnesyl Diphosphate Synthase
TWO AMINO ACIDS BEFORE THE FIRST ASPARTATE-RICH MOTIF SOLELY DETERMINE EUKARYOTIC FARNESYL DIPHOSPHATE SYNTHASE ACTIVITY

(Received for publication, October 16, 1996, and in revised form, November 19, 1996)

Shin-ichi Ohnuma , Kazutake Hirooka , Chikara Ohto and Tokuzo Nishino

From the Department of Biochemistry and Engineering, Tohoku University, Aoba Aramaki, Aoba-ku, Sendai 980-77, Japan, and  Bio Research Laboratory, Toyota Motor Corporation 1, Toyota-cho, Toyota 471-71, Japan

Farnesyl diphosphate (FPP) and geranylgeranyl diphosphate (GGPP) are precursors for a variety of important natural products, such as sterols, carotenoids, and prenyl quinones. Although FPP synthase and GGPP synthase catalyze similar consecutive condensations of isopentenyl diphosphate with allylic diphosphates and have several homologous regions in their amino acid sequences, nothing is known about how these enzymes form the specific products. To locate the region that causes the difference of final products between GGPP synthase and FPP synthase, we constructed six mutated archaeal GGPP synthases whose regions around the first aspartate-rich motif were replaced with the corresponding regions of FPP synthases from human, rat, Arabidopsis thaliana, Saccharomyces cerevisiae, Escherichia coli, Bacillus stearothermophilus, and from some other related mutated enzymes. From the analysis of these mutated enzymes, we revealed that the region around the first aspartate-rich motif is essential for the product specificity of all FPP synthases and that the mechanism of the chain termination in eukaryotic FPP synthases (type I) is different from those of prokaryotic FPP synthases (type II). In FPP synthases of type I, two amino acids situated at the fourth and the fifth positions before the motif solely determine their product chain length, while the product specificity of the type II enzymes is determined by one aromatic amino acid at the fifth position before the motif, two amino acids inserted in the motif, and other modifications. These data indicate that FPP synthases have evolved from the progenitor corresponding to the archaeal GGPP synthase in two ways.


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