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 multifunctional enzyme that forms other triterpene alcohols, including beta-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.
Herrera
J B
JB
Department of Chemistry, Rice University, Houston, TX 77005, USA.
Bartel
B
B
Wilson
W K
WK
Matsuda
S P
SP
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics*; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics / Q000302:isolation & purification; D017343:Genes, Plant; D019751:Intramolecular Transferases / Q000235:genetics*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010940:Plant Proteins / Q000235:genetics*; D010957:Plasmids; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D010940:Plant Proteins; D019751:Intramolecular Transferases; C117114:lupeol synthase