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Biology subjects

Dho, Y.

Publications and source records attributed to Dho, Y..

2 recordsLinked to original sources

Discovery of homoharringtonine pathway enzymes reveals a whole plant model for coordinated biosynthesis

Plants produce diverse molecules that inhibit protein translation. A lead example is homoharringtonine (HHT), a key tool for ribosomal profiling and an FDA-approved treatment for chronic myeloid leukemia. HHT is commercially produced through semi-synthesis from the alkaloid core cephalotaxine (CET) extracted from endangered Cephalotaxus species. Despite its significance, the CET/HHT biosynthetic pathway remains unresolved. Here, we use paired untargeted metabolomics (stable-isotope precursor feeding) and transcriptomics to elucidate a near-complete biosynthesis to CET without prior knowledge of intermediates and biosynthetic genes. We show that while the CET core is biosynthesized only in growing root tips, CET and HHT accumulate throughout the plant. We discovered seven pathway intermediates and six novel enzymes that produce cephalotaxinone, the likely direct precursor of CET. Included are non-canonical cytochrome P450s, an atypical short-chain dehydrogenase, and a 2-oxoglutarate-dependent dioxygenase that together result in carbon excision and CET/HHT pentacyclic backbone formation. This study establishes a metabolic route to the HHT core scaffold and suggests a whole-plant coordination model in Cephalotaxus, where cephalotaxinone is produced in root tips and distributed throughout the plant for subsequent elaboration to HHT.

biochemistry↗

Neofunctionalized carbonic anhydrases in the biosynthesis of neuroactive plant alkaloids

Plants synthesize numerous alkaloids that mimic animal neurotransmitters. The diversity of alkaloid structures is achieved through the generation and tailoring of unique carbon scaffolds. However, many neuroactive alkaloids belong to a scaffold class for which no biosynthetic route or enzyme catalyst is known. By studying highly coordinated, tissue-specific gene expression in plants that produce neuroactive Lycopodium alkaloids, we identified a new enzyme class for alkaloid biosynthesis: neofunctionalized -carbonic anhydrases (CAHs). We show that three CAH-like (CAL) enzymes are involved in a cryptic biosynthetic route to a key bicyclic precursor of the Lycopodium alkaloids, and additionally, we describe a series of oxidative tailoring steps that generate the optimized acetylcholinesterase inhibition activity of huperzine A. Our findings suggest a broader involvement of CAL enzymes in specialized metabolism and provide an example for how successive scaffold tailoring steps can drive potency against a natural protein target of interest.

biochemistry↗