Identification and Characterization of Bifunctional Drimenol Synthases of Marine Bacterial Origin
Nhu Ngoc Quynh Vo, Yuhta Nomura, Kiyomi Kinugasa, Hiroshi Takagi, Shunji Takahashi
Abstract
TT motif is also critical for cyclization. Thus, AsDMS utilizes both motifs in the reactions. Remarkably, the unique protein architecture of AsDMS, which is characterized by the fusion of a HAD-like domain (N-domain) and a terpene synthase β domain (C-domain), significantly differentiates this new enzyme. Our findings of the first examples of bacterial DMSs suggest the biosynthesis of drimane sesquiterpenes in bacteria and shed light on the divergence of the structures and functions of terpene synthases.
Topics & Concepts
BiochemistryStructural motifBiosynthesisTerpeneDephosphorylationStereochemistryActive siteBiologyDehalogenaseChemistryEnzymePhosphatasePlant biochemistry and biosynthesisMicrobial Natural Products and BiosynthesisNatural product bioactivities and synthesis