Cover Feature: Identification of Chimeric αβγ Diterpene Synthases Possessing both Type II Terpene Cyclase and Prenyltransferase Activities (ChemBioChem 21/2017). (19th October 2017)

• Record Type: Journal Article
• Authors: Mitsuhashi, Takaaki; Okada, Masahiro; Abe, Ikuro
• Is Part Of: Chembiochem. Volume 18:Number 21(2017)
• Page Start: 2080
• Page End: 2080
• Publication Date: 2017-10-19
• Subjects: biosynthesis -- enzymes -- mutagenesis -- prenyltransferases -- structure elucidation -- terpenoids; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201700550
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract : The cover feature shows a new type of chimeric diterpene synthase composed of three domains (α, β, and γ).These are the first enzymes to possessing both type II TC and PT activities. The α domain is responsible for the PT activity, whereas the βγ domains make up the type II TC. Additionally, between the α and βγ domains, there is a characteristic linker in which minimal secondary structure is predicted. This linker does not exist in other previously characterized three‐domain (αβγ) terpene synthases. Therefore, both the catalytic activity and protein architecture substantially differentiate these new enzymes from previously characterized terpene synthases. More information can be found in the communication by I. Abe et al. onpage 2104 in Issue 21, 2017 (DOI:10.1002/cbic.201700445 ).