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J Biol Chem, Vol. 274, Issue 9, 5888-5894, February 26, 1999

Human Geranylgeranyl Diphosphate Synthase
cDNA CLONING AND EXPRESSION

Tsuyoshi Kuzuguchi, Yuiko Morita, Ikuko Sagami, Hiroshi Sagami, and Kyozo Ogura

From the Institute for Chemical Reaction Science, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai, 980-8577, Japan

Geranylgeranyl diphosphate (GGPP) synthase (GGPPSase) catalyzes the synthesis of GGPP, which is an important molecule responsible for the C20-prenylated protein biosynthesis and for the regulation of a nuclear hormone receptor (LXR·RXR). The human GGPPSase cDNA encodes a protein of 300 amino acids which shows 16% sequence identity with the known human farnesyl diphosphate (FPP) synthase (FPPSase). The GGPPSase expressed in Escherichia coli catalyzes the GGPP formation (240 nmol/min/mg) from FPP and isopentenyl diphosphate. The human GGPPSase behaves as an oligomeric molecule with 280 kDa on a gel filtration column and cross-reacts with an antibody directed against bovine brain GGPPSase, which differs immunochemically from bovine brain FPPSase. Northern blot analysis indicates the presence of two forms of the mRNA.


Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.



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