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

Autor:	Fang-Hua Chu, Pei-Min Kuo, Yu-Rong Chen, Sheng-Yang Wang
Rok vydání:	2008
Předmět:	Cloning Chamaecyparis formosensis ATP synthase biology medicine.disease_cause biology.organism_classification Terpenoid Biomaterials Terpene Open reading frame Biochemistry Phylogenetics biology.protein medicine Escherichia coli
Zdroj:	hfsg. 63:69-74
ISSN:	1437-434X 0018-3830
DOI:	10.1515/hf.2009.019
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::1cc03b7c97abf177fc3757a86b73ad81 https://doi.org/10.1515/hf.2009.019 Zobrazit plný text záznamu