Multi-domain terpenoid cyclase architecture and prospects for proximity in bifunctional catalysis.

ABSTRACT: Crystal structures of terpenoid cyclases reveal assemblies of three basic domains designated α, β, and γ. While the biosynthesis of cyclic monoterpenes (C₁₀) and sesquiterpenes (C₁₅) most often involves enzymes with α or αβ domain architecture, the biosynthesis of cyclic diterpenes (C₂₀), sesterterpenes (C₂₅), and triterpenes (C₃₀) can involve enzymes with α, αα, βγ, or αβγ domain architecture. Indeed, some enzymes of terpenoid biosynthesis are bifunctional, with distinct active sites that catalyze sequential reactions. Interestingly, some of these enzymes oligomerize to form dimers, tetramers, and hexamers. Not only can such assemblies enable enzyme regulation by allostery, but they can also provide a modest enhancement of terpenoid p

SUBMITTER: Chen M 

PROVIDER: S-EPMC5143216 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature