{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Love AC"],"funding":["NCCIH NIH HHS","NIGMS NIH HHS"],"pubmed_abstract":["The marine bacterial flavoenzymes Clz9 and Tcz9 can process cannabigerolic acid (CBGA) to the minor cannabinoid, cannabichromenic acid (CBCA), however, the mechanistic details of this extrinsic transformation are still obscure. Here, we report a thorough analysis of CBCA-formation by Clz9 and Tcz9 through high-resolution crystallographic characterization, biochemical analysis, and spectroscopic interrogation. Our work reveals that Clz9 and Tcz9 use different biochemical mechanisms from <i>Cannabis</i> cyclases and each other in their production of CBCA. Collection of a high-resolution substrate-bound structure, the first for any cannabinoid cyclase, provides key insights into how active site architecture affects substrate binding and stereoselectivity. Engineering approaches improve the st"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.10.07.680811"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12632287"],"repository":["biostudies-literature"],"pubmed_title":["Structural and biochemical basis for cannabinoid cyclase activity in marine bacterial flavoenzymes."],"pmcid":["PMC12632287"],"funding_grant_id":["F32 GM150232","R01 AT012641"],"pubmed_authors":["Love AC","Palfey BA","Quinnell DE","Gappy R","Sheehy M","Lee A","Zangwill L","Kao YC","Hubert FM","Hsu J","Sirohi H","Moore BS","Chang G"],"additional_accession":[]},"is_claimable":false,"name":"Structural and biochemical basis for cannabinoid cyclase activity in marine bacterial flavoenzymes.","description":"The marine bacterial flavoenzymes Clz9 and Tcz9 can process cannabigerolic acid (CBGA) to the minor cannabinoid, cannabichromenic acid (CBCA), however, the mechanistic details of this extrinsic transformation are still obscure. Here, we report a thorough analysis of CBCA-formation by Clz9 and Tcz9 through high-resolution crystallographic characterization, biochemical analysis, and spectroscopic interrogation. Our work reveals that Clz9 and Tcz9 use different biochemical mechanisms from <i>Cannabis</i> cyclases and each other in their production of CBCA. Collection of a high-resolution substrate-bound structure, the first for any cannabinoid cyclase, provides key insights into how active site architecture affects substrate binding and stereoselectivity. Engineering approaches improve the st","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Oct","modification":"2026-06-14T03:18:51.079Z","creation":"2026-06-14T03:08:45.945Z"},"accession":"S-EPMC12632287","cross_references":{"pubmed":["41278791"],"doi":["10.1101/2025.10.07.680811"]}}