Structural insights into a bacterial terpene cyclase fused with haloacid Dehalogenase-like phosphatase.

ABSTRACT: Terpene cyclases (TCs), consisting of various combinations of α, β, and γ domains, have been extensively studied. Recently, non-canonical enzymes comprising a TCβ domain and a haloacid dehalogenase (HAD)-like domain (referred to as HAD-TCβ) have been discovered. However, their overall structure remains unclear. In this study, we determined the co-crystal structures of drimenol synthase from Aquimarina spongiae (AsDMS), which catalyzes the conversion of farnesyl pyrophosphate (1) into drimenol (2). Crystallographic analyses of the enzyme bound to substrates 1 and drimenyl monophosphate (3) demonstrated that the TCβ domain catalyzes a class II cyclization reaction initiated by protonation, whereas the HAD domain catalyzes a phosphatase-like dephosphorylation reaction dependent on a divalent

SUBMITTER: Fujiyama K 

PROVIDER: S-EPMC12365925 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature