Cloning and characterization of α-pinene synthase from Chamaecyparis formosensis Matsum

Fang-Hua Chu, Pei-Min Kuo, Yu-Rong Chen, Sheng-Yang Wang
<span title="2009-01-01">2009</span> <i title="Walter de Gruyter GmbH"> <a target="_blank" rel="noopener" href="" style="color: black;">Holzforschung</a> </i> &nbsp;
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
more &raquo; ... 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 a-pinene. This is the first report of cloning of a mono-TPS and functionally expressed in E. coli and which could be identified as a-pinene synthase from a Cupressaceae conifer.
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="">doi:10.1515/hf.2009.019</a> <a target="_blank" rel="external noopener" href="">fatcat:eoqzohz5bngmxggkvhmttccqu4</a> </span>
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