Human geranylgeranyl diphosphate synthase. cDNA cloning and expression

• Published in: The Journal of biological chemistry Vol. 274; no. 9; pp. 5888 - 5894
• Main Authors: Kuzuguchi, T, Morita, Y, Sagami, I, Sagami, H, Ogura, K
• Format: Journal Article
• Language: English
• Published: United States 26.02.1999
• Subjects: Alkyl and Aryl Transferases - genetics; Alkyl and Aryl Transferases - immunology; Amino Acid Sequence; Animals; Base Sequence; Brain - enzymology; Cattle; Cloning, Molecular; Cross Reactions; DNA; DNA, Complementary; Escherichia coli - genetics; Farnesyltranstransferase; Humans; Molecular Sequence Data; Nucleic Acid Hybridization; RNA, Messenger - genetics; Sequence Homology, Amino Acid
• ISSN: 0021-9258
• DOI: 10.1074/jbc.274.9.5888

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.