# Recently discovered heteromeric enzymes in natural product biosynthesis

**Authors:** Zhongtian Yu, Ikuro Abe

PMC · DOI: 10.1016/j.jbc.2025.108516 · The Journal of Biological Chemistry · 2025-04-17

## TL;DR

This review summarizes newly discovered enzyme complexes involved in the biosynthesis of natural products and their potential for redesigning biosynthetic systems.

## Contribution

The paper consolidates recent discoveries of heteromeric enzymes in natural product biosynthesis and their genetic and structural foundations.

## Key findings

- Heteromeric enzymes play a role in the biosynthesis of natural products and metabolic pathways.
- Recent studies reveal the genetic and structural bases for forming these enzyme complexes.
- These findings offer insights for redesigning biosynthetic machinery.

## Abstract

The abundant diversity and elegant complexity in the chemical structures of natural products have attracted vigorous investigations of the chemistry and enzymology underlying their biosynthetic processes over the past few decades. Among the biochemical events, the formation of complexes of heteromeric enzymes has been observed in the biosynthesis of several natural products and metabolic pathways. In this review, we aim to consolidate the recently discovered cases of heteromeric enzymes in natural product biosynthesis and metabolism, in order to clarify the genetic and structural bases leading to the formation of these heteromeric complexes and provide insights for the rational redesign of proteins in biosynthetic machineries.

## Full-text entities

- **Diseases:** Wilson's disease (MESH:D006527)
- **Chemicals:** C (MESH:D002244), homoorientin (MESH:C057912), pyrophosphate (MESH:C107241), 4-coumaryl 4-coumarate (MESH:C507369), Metal (MESH:D008670), TPP (MESH:D013835), puerarin (MESH:C033607), MgCl2 (MESH:D015636), oxazolone (MESH:D010081), water (MESH:D014867), Methanobactins (MESH:C491147), AibH2 (-), Hinokiresinols (MESH:C119821), lipstatin (MESH:C054164), Aib (MESH:C100049), glucoside (MESH:D005960), N-oxalylglycine (MESH:C040947), coenzyme M (MESH:D015080), sugar (MESH:D000073893), ATP (MESH:D000255), Fe (MESH:D007501), luteolin (MESH:D047311), PnAA (MESH:C003126), Mn (MESH:D008345), hexahistidine (MESH:C471213), daidzein (MESH:C004742), serine (MESH:D012694), platensimycin (MESH:C510909), cysteine (MESH:D003545), thioamide (MESH:D013854)
- **Species:** Methanocaldococcus jannaschii (species) [taxon 2190], Staphylococcus aureus (species) [taxon 1280], Cryptomeria japonica (Japanese cedar, species) [taxon 3369], Microbacterium trichothecenolyticum (species) [taxon 69370], Talaromyces purpureogenus (species) [taxon 1266744], Asparagus officinalis (garden asparagus, species) [taxon 4686], Saccharomyces cerevisiae (baker's yeast, species) [taxon 4932], Streptomyces toxytricini (species) [taxon 67369], Escherichia coli (E. coli, species) [taxon 562]
- **Mutations:** A49 G, cysteine by alanine

## Full text

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## Figures

8 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12141560/full.md

## References

58 references — full list in the complete paper: https://tomesphere.com/paper/PMC12141560/full.md

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Source: https://tomesphere.com/paper/PMC12141560