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Cover Feature: Identification of Chimeric αβγ Diterpene Synthases Possessing both Type II Terpene Cyclase and Prenyltransferase Activities (ChemBioChem 21/2017)
Author(s) -
Mitsuhashi Takaaki,
Okada Masahiro,
Abe Ikuro
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700550
Subject(s) - diterpene , prenyltransferase , terpene , linker , enzyme , chemistry , stereochemistry , cyclase , atp synthase , biochemistry , biology , biosynthesis , computer science , operating system
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. on page 2104 in Issue 21, 2017 (DOI: 10.1002/cbic.201700445).