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Human Geranylgeranyl Diphosphate Synthase
Geranylgeranyl diphosphate (GGPP) synthase (GGPPSase) catalyzes the synthesis of GGPP, which is an important molecule responsible for the C 20 -prenylated protein biosynthesis and for the regulation of a nuclear hormone receptor (LXR·RXR). The human GGPPSase cDNA encodes a protein of 300 amino acid...
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| Published in: | The Journal of biological chemistry 1999-02, Vol.274 (9), p.5888-5894 |
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| Main Authors: | , , , , |
| Format: | Article |
| Language: | English |
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| container_end_page | 5894 |
| container_issue | 9 |
| container_start_page | 5888 |
| container_title | The Journal of biological chemistry |
| container_volume | 274 |
| creator | Kuzuguchi, Tsuyoshi Morita, Yuiko Sagami, Ikuko Sagami, Hiroshi Ogura, Kyozo |
| description | Geranylgeranyl diphosphate (GGPP) synthase (GGPPSase) catalyzes the synthesis of GGPP, which is an important molecule responsible
for the C 20 -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. |
| doi_str_mv | 10.1074/jbc.274.9.5888 |
| format | article |
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for the C 20 -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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for the C 20 -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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for the C 20 -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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| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1999-02, Vol.274 (9), p.5888-5894 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_crossref_primary_10_1074_jbc_274_9_5888 |
| source | ScienceDirect Journals |
| title | Human Geranylgeranyl Diphosphate Synthase |
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