Enhancing structural diversity of terpenoids by multisubstrate terpene synthases

• Min Li and
• Hui Tao

Beilstein J. Org. Chem. 2024, 20, 959–972, doi:10.3762/bjoc.20.86

• ), hammershoyl diphosphate (111), and ancheryl diphosphate (112) (Figure 8c). Subsequently, terpentetriene synthase from Kitasatospora griseola (Cyc2) and kolavelool synthase from Herpetosiphon aurantiacus (HaKS) were identified as capable of converting these building blocks into C16 scaffolds, whereas other

• building blocks synthesized by SpSodMT variants, and 113–122 are selected typical products yielded by terpentetriene synthase and kolavelool synthase with further modifications by a cytochrome P450 CYP720B1. Structures of C16 terpenes identified via genome mining of C16 biosynthetic gene clusters from

Efficient production of clerodane and ent-kaurane diterpenes through truncated artificial pathways in Escherichia coli

• Fang-Ru Li,
• Xiaoxu Lin,
• Qian Yang,
• Ning-Hua Tan and
• Liao-Bin Dong

Beilstein J. Org. Chem. 2022, 18, 881–888, doi:10.3762/bjoc.18.89

• alternative to bypass synthetic challenges. In this study, we constructed two truncated artificial pathways to efficiently produce terpentetriene and ent-kaurene, two representative clerodane and ent-kaurane diterpenes, in Escherichia coli. Both pathways depend on the exogenous addition of isoprenoid alcohol

• to reinforce the supply of IPP and DMAPP via two sequential phosphorylation reactions. Optimization of these constructs provided terpentetriene and ent-kaurene titers of 66 ± 4 mg/L and 113 ± 7 mg/L, respectively, in shake-flask fermentation. The truncated pathways to overproduce clerodane and ent

• -kaurane skeletons outlined here may provide an attractive route to prepare other privileged diterpene scaffolds. Keywords: artificial pathway; ent-kaurene; Escherichia coli; overproduction; terpentetriene; Introduction Diterpenoids, of which there are over 34,000 members (http://terokit.qmclab.com