β-Amyrin synthase from Euphorbia tirucalli. Steric bulk, not the π-electrons of Phe, at position 474 has a key role in affording the correct folding of the substrate to complete the normal polycyclization cascade

β-Amyrin, a triterpene, is widely distributed in plants and its glycosides confer important biological activities. Mutagenesis studies on β-amyrin synthase are very limited as compared with those of squalene-hopene cyclase and lanosterol synthase. This study was conducted to elucidate the function o...

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Veröffentlicht in:	Organic & biomolecular chemistry 2014-06, Vol.12 (23), p.3836-3846
Hauptverfasser:	Ito, Ryousuke, Masukawa, Yukari, Nakada, Chika, Amari, Kanako, Nakano, Chiaki, Hoshino, Tsutomu
Format:	Artikel
Sprache:	eng
Schlagworte:	Chromatography, Gas Cyclization Electrons Euphorbia - enzymology Intramolecular Transferases - metabolism Mutagenesis, Site-Directed Mutant Proteins - chemistry Oleanolic Acid - analogs & derivatives Oleanolic Acid - chemistry Oleanolic Acid - metabolism Phenylalanine - chemistry Structure-Activity Relationship Substrate Specificity
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