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Paralogous members of the oxidosqualene cyclase (OSC) family encode a diversity of enzymes that are important in triterpenoid biosynthesis. This report describes the isolation of the  Gentiana straminea  gene  GsAS2  that encodes a  β  - amyrin synthase ( β AS) enzyme. Unlike its previously isolated paralog  GsAS1, GsAS2  lacks introns. Its predicted protein product was is a 759 residue polypeptide that shares high homology with other known  β -amyrin synthases ( β ASs). Heterologously expressed  GsAS2  generates more  β -amyrin in yeast than does  GsAS1 . Constitutive over-expression of  GsAS2  resulted in a 5.7 fold increase in oleanolic acid accumulation, while over-expression of  GsAS1  led to a 3 fold increase. Additionally, RNAi-directed suppression of  GsAS2  and  GsAS1  in  G. straminea  decreased oleonolic acid levels by 65.9% and 21% respectively, indicating that  GsAS2  plays a more important role than  GsAS1  in oleanolic acid biosynthesis in  G. straminea . We uses a docking model to explore the catalytic mechanism of GsAS1/2 and predicted that GsAS2, with its Y560, have higher efficiency than GsAS1 and mutated versions of GsAS2 in  β -amyrin produce. When the key residue in GsAS2 was mutagenized, it produced about 41.29% and 71.15% less  β -amyrin than native, while the key residue in GsAS1 was mutagenized to that in GsAS2, the mutant produced 38.02% more  β -amyrin than native GsAS1.

An Intronless β-amyrin Synthase Gene is More Efficient in Oleanolic Acid Accumulation than its Paralog in Gentiana straminea