| Description | Characterized enzymes in the terpene cyclase like 2 family include sesquiterpene cyclases, such as epi-isozizaene synthase and pentalenene synthase, as well as 2-methylisoborneol synthase, which processes a naturally occuring noncanonical isoprenoid substrate [ , ]. As with other enzymes with the 'terpenoid synthase fold', they have two conserved metal binding motifs, proposed to coordinate Mg2 ion-bridged binding of the diphosphate moiety of FPP to the enzymes. Metal-triggered substrate ionization initiates catalysis, and the α-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. These enzymes function in the monomeric form and are found mostly in fungi and bacteria [ , ]. | Name | Terpene cyclase-like 2 |
| Short Name | Terpene_cyclase-like_2 | Type | Family |
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