The present invention relates to an expression cassette encoding a fusion protein comprising a nucleotide sequence encoding an amino acid sequence shown in SEQ ID NO: 1 or a fragment thereof, which directs protein decay, or encoding an amino acid sequence which is at least 60% identical to the amino acid sequence which directs protein decay; and also comprising a nucleotide sequence encoding a protein of interest, wherein the nucleotide sequences are fused together in frame. Further, the present invention relates to a vector comprising the expression cassette, a host cell comprising the expression cassette or a host cell comprising the vector which comprises the expression cassette. Additionally, the present invention relates to a method for the production of a triterpenoid using the host cell comprising the expression cassette of the present invention.

This document relates to using bidirectional, multi-enzymatic scaffolds to biosynthesize cannabinoids in recombinant hosts.

A strain of Yarrowia lipolytica was engineered to overexpress -hydroxy -methylglutaryl-CoA reductase and farnesyl pyrophosphate synthase, as rate-limiting enzymes in the mevalonate and sesquiterpenoid synthesis pathways respectively. Metabolite extracts from this strain were run on LC-MS and showed a number of novel compounds being produced, including terpenoids varying in lengths and oxidation states. Upon NMR and MS/MS structure validation as well as biochemical assays, these compounds were determined as a new class of non-natural compounds, bifunctional terpenoids. Studies on the overexpression of P450 enzymes, alcohol oxidase, aldehyde dehydrogenase, and alcohol dehydrogenase showed that expression of these enzymes in addition to -hydroxy -methylglutaryl-CoA reductase and farnesyl pyrophosphate synthase increase the production of bifunctional terpenoids. Bioactivity assays demonstrate the application of bifunctional terpenoids.

Disclosed are, inter alia, double stranded RNAi (dsRNAi) agents inhibiting expression of 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR), for example, human HMGCR, compositions including the same, and methods of treatment using the same.

The present disclosure relates to synthetic biology and, in particular the bioproduction of isoprenoids using heterologous expression of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase (HMGR) enzyme(s).