Cloning and characterization of the Arabidopsis thaliana lupeol synthase gene

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 multifunc...

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Bibliographic Details
Published in:Phytochemistry (Oxford) 1998-12, Vol.49 (7), p.1905-1911
Main Authors: R. Herrera, Jennifer B, Bartel, Bonnie, Wilson, William K, Matsuda, Seiichi P.T
Format: Article
Language:English
Subjects:
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
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Summary: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.
ISSN:0031-9422
1873-3700
DOI:10.1016/S0031-9422(98)00366-5