{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Osika KR"],"funding":["NIGMS NIH HHS"],"pubmed_abstract":["Drimenol synthase from <i>Aquimarina spongiae</i> (AsDMS) is a highly unusual bifunctional sesquiterpene synthase that integrates two distinct, sequential isoprenoid processing activities within a single polypeptide chain. AsDMS catalyzes the class II cyclization of farnesyl diphosphate (FPP) to form drimenyl diphosphate, which then undergoes enzyme-catalyzed hydrolysis to yield drimenol, a bioactive sesquiterpene alcohol with antifungal and anticancer properties. Here, we report the X-ray crystal structures of AsDMS and its complex with a sesquiterpene thiol, which are the first of a terpene cyclase-phosphatase. The AsDMS structure exhibits a two-domain architecture consisting of a terpene cyclase β domain and a haloacid dehalogenase (HAD)-like phosphatase domain, with two distinct active"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.02.11.637696"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11844523"],"repository":["biostudies-literature"],"pubmed_title":["Crystal Structure and Catalytic Mechanism of Drimenol Synthase, a Bifunctional Terpene Cyclase-Phosphatase."],"pmcid":["PMC11844523"],"funding_grant_id":["T32 GM133398","P30 GM133893","R01 GM056838"],"pubmed_authors":["Gaynes MN","Christianson DW","Osika KR"],"additional_accession":[]},"is_claimable":false,"name":"Crystal Structure and Catalytic Mechanism of Drimenol Synthase, a Bifunctional Terpene Cyclase-Phosphatase.","description":"Drimenol synthase from <i>Aquimarina spongiae</i> (AsDMS) is a highly unusual bifunctional sesquiterpene synthase that integrates two distinct, sequential isoprenoid processing activities within a single polypeptide chain. AsDMS catalyzes the class II cyclization of farnesyl diphosphate (FPP) to form drimenyl diphosphate, which then undergoes enzyme-catalyzed hydrolysis to yield drimenol, a bioactive sesquiterpene alcohol with antifungal and anticancer properties. Here, we report the X-ray crystal structures of AsDMS and its complex with a sesquiterpene thiol, which are the first of a terpene cyclase-phosphatase. The AsDMS structure exhibits a two-domain architecture consisting of a terpene cyclase β domain and a haloacid dehalogenase (HAD)-like phosphatase domain, with two distinct active","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2026-05-21T03:09:45.305Z","creation":"2025-04-04T00:17:05.959Z"},"accession":"S-EPMC11844523","cross_references":{"pubmed":["39990494"],"doi":["10.1101/2025.02.11.637696"]}}