PubMed:10026212 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/10026212","sourcedb":"PubMed","sourceid":"10026212","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/10026212","text":"Human geranylgeranyl diphosphate synthase. cDNA cloning and expression.\nGeranylgeranyl 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 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