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Chimeric Terpene Synthases Possessing both Terpene Cyclization and Prenyltransfer Activities

期刊

CHEMBIOCHEM
卷 19, 期 11, 页码 1106-1114

出版社

WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201800120

关键词

biosynthesis; cyclization; enzymes; structure-activity relationships; terpenoids

资金

  1. MEXT, Japan (JSPS KAKENHI) [JP15H01836, JP16H06443]
  2. JST/NSFC Strategic International Collaborative Research Program Japan-China
  3. JSPS Research Fellowships for Young Scientists
  4. Grants-in-Aid for Scientific Research [16H06443] Funding Source: KAKEN

向作者/读者索取更多资源

Prenyltransferase (PT) and terpene synthase (TPS) are key enzymes in the formation of the basic carbon skeletons of terpenoids. The PTs determine the prenyl carbon chain length, whereas TPSs generate the structural complexity of the molecular scaffolds, forming various ring structures. Normally, PTs and TPSs are separate, independent enzymes. However, in 2007, a chimeric enzyme, in which the PT was fused with the TPS, was found in a fungus. Recent studies have revealed that such chimeric TPSs are widely distributed in fungi and function in the biosyntheses of various terpene natural products, including sesterterpenes, which are a relatively rare group of terpenoids. This review summarizes the accumulated knowledge of these recently discovered, unique, chimeric TPSs.

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