Phytochemistry (Oxford), 1998-12, Vol.49 (7), p.1905-1911
1998
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- Autor(en) / Beteiligte
- Titel
- Cloning and characterization of the Arabidopsis thaliana lupeol synthase gene
- Ist Teil von
- Phytochemistry (Oxford), 1998-12, Vol.49 (7), p.1905-1911
- Ort / Verlag
- Amsterdam: Elsevier Ltd
- Erscheinungsjahr
- 1998
- Quelle
- Elsevier ScienceDirect Journals
- Beschreibungen/Notizen
- A 2274 bp Arabidopsis thaliana cDNA was isolated that encodes a protein 57% identical to cycloartenol synthase from the same organism. The expressed recombinant protein encodes lupeol synthase, which converts oxidosqualene to the triterpene lupeol as the major product. Lupeol synthase is a multifunctional enzyme that forms other triterpene alcohols, including β-amyrin, as minor products. Sequence analysis suggests that lupeol synthase diverged from cycloartenol synthase after plants diverged from fungi and animals. This evolutionary order is the reason that fungi and animals do not make lupeol.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0031-9422eISSN: 1873-3700DOI: 10.1016/S0031-9422(98)00366-5Titel-ID: cdi_proquest_miscellaneous_69131338
- Format
- –
- Schlagworte
- Amino Acid Sequence, Arabidopsis - enzymology, Arabidopsis - genetics, Arabidopsis thaliana, Biological and medical sciences, Brassicaceae, cloning, Cloning, Molecular, DNA, Complementary - genetics, DNA, Complementary - isolation & purification, Enzymes, Fundamental and applied biological sciences. Psychology, Genes, Plant, Genes. Genome, Intramolecular Transferases - genetics, lupeol, Metabolism, Molecular and cellular biology, molecular evolution, Molecular genetics, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Plant physiology and development, Plant Proteins - genetics, Plasmids, Saccharomyces cerevisiae - enzymology, Saccharomyces cerevisiae - genetics, Sequence Homology, Amino Acid, triterpenes