Engineering the Prenyltransferase Domain of a Bifunctional Assembly-Line Terpene Synthase.

ABSTRACT: Copalyl diphosphate (CPP) synthase from Penicillium verruculosum (PvCPS) is a bifunctional diterpene synthase with both prenyltransferase and class II cyclase activities. The prenyltransferase α domain catalyzes the condensation of C₅ dimethylallyl diphosphate with three successively added C₅ isopentenyl diphosphates (IPPs) to form C₂₀ geranylgeranyl diphosphate (GGPP), which then undergoes a class II cyclization reaction at the βγ domain interface to generate CPP. The prenyltransferase α domain mediates oligomerization to form a 648-kD (αβγ)₆ hexamer. In the current study, we explore prenyltransferase structure-function relationships in this oligomeric assembly-line platform with the goal of generating alternative linear isoprenoid produc

SUBMITTER: Ronnebaum TA 

PROVIDER: S-EPMC8551067 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature