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| Content Provider | Springer Nature Link |
|---|---|
| Author | Hsu, Li Jen Chu, Fang Hua |
| Copyright Year | 2014 |
| Abstract | Terpenoids have many biological functions and a comprehensive range of applications. Here, we cloned two monoterpene synthase genes, Tc-αpin/teo and Tc-teo, from Taiwania cryptomerioides. The enzymes encoded by these genes shared 97 % amino acid sequences similarity but had different terpene product profiles. Using structural modeling and site-directed mutagenesis, we successfully identified three plasticity residues around the active site of Tc-αPIN/TEO, namely Y327, Y429 and Y575 that are involved in secondary cyclization. The mutants in which the phenolic residues were replaced with phenylalanines seemed to lose their preference for α-pinene synthesis, indicating that the tyrosine hydroxyl groups at these sites were necessary for the formation of bicyclic terpene products. |
| Starting Page | 1 |
| Ending Page | 8 |
| Page Count | 8 |
| File Format | |
| ISSN | 16142942 |
| Journal | Tree Genetics & Genomes |
| Volume Number | 11 |
| Issue Number | 1 |
| e-ISSN | 16142950 |
| Language | English |
| Publisher | Springer Berlin Heidelberg |
| Publisher Date | 2014-11-19 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Monoterpene synthase Plasticity residues Protein engineering cyclization Site-directed mutagenesis Structure-function Forestry Plant Genetics & Genomics Plant Breeding/Biotechnology Tree Biology Biotechnology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics Molecular Biology Horticulture Forestry |
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