A non-synonymous nucleotide substitution can account for one evolutionary route to sesquiterpene synthase activity in the TPS-b subgroup

详细信息    查看全文

• 作者：Sol Green^a ; ^{sol.green@plantandfood.co.nz"" rel=""nofollow} ; Edward N. Baker^b ; William Laing^a
• 关键词：Terpene synthase ; Evolution ; α ; -Farnesene ; Mutagenesis ; Protein modelling ; Malus × ; domestica
• 刊名：FEBS Letters
• 出版年：2011
• 出版时间：23 June 2011
• 年：2011
• 卷：585
• 期：12
• 页码：1841-1846
• 全文大小：1165 K

文摘

Plant sesquiterpene and hemiterpene synthases in the monoterpene synthase dominated TPS-b subgroup are thought to have evolved independently from a monoterpene synthase ancestor. A TPS-b sesquiterpene synthase from apple (MdAFS1), which predominantly produces α-farnesene, can also synthesize the monoterpene (E)-β-ocimene. The dual activity offered a functional link to an ancestral MdAFS1 enzyme and a rational basis for investigation of the evolution of TPS-b sesquiterpene enzymes. Protein modelling and mutagenesis analysis of the MdAFS1 active site identified a non-synonymous nucleotide substitution that could account for the requisite shift in substrate specificity necessary for the emergence of its sesquiterpene activity during the evolution of the TPS-b enzymes.