Cloning and characterization of α-pinene synthase from Chamaecyparis formosensis Matsum
Journal
Holzforschung
Journal Volume
63
Journal Issue
1
Pages
69-74
Date Issued
2009
Author(s)
Abstract
Analyzing the gene sequences of terpene synthase (TPS) may contribute to a better understanding of terpenes biosynthesis and evolution of phylogenetic taxonomy. Chamaecyparis formosensis is an endemic and precious conifer of Taiwan. To understand the biosynthesis mechanism of terpenes in this tree, a full length of putative mono-TPS, named as Cf-Pin (GeneBank accession no. EU099434), was obtained by PCR method and RACE extension. The Cf-Pin has an 1887-bp open reading frame and encodes 628 amino acids. To identify the function of Cf-Pin, the recombinant protein from Escherichia coli was incubated with geranyl diphosphate, produced one major product, the structure of which was elucidated. GC/MS analysis and matching of retention time and mass spectrum with authentic standards revealed that this product is α-pinene. This is the first report of cloning of a mono-TPS and functionally expressed in E. coli and which could be identified as α-pinene synthase from a Cupressaceae conifer. © 2009 by Walter de Gruyter.
SDGs
Type
journal article