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Updated: Apr 15, 2026

A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products
Published on: October 4, 2019
Substrate-Controlled Stereochemistry in Natural Product Biosynthesis.
Wei Ding1, Yongzhen Li1, Qi Zhang1
1Department of Chemistry, Fudan University, Shanghai 200433, China.
Substrate properties, not just enzymes, dictate product outcomes in many natural product biosynthesis pathways. This finding challenges traditional views of enzyme catalysis and opens new avenues for bioengineering.
Area of Science:
- Biochemistry
- Enzymology
- Natural Product Biosynthesis
Background:
- Enzymes are traditionally viewed as the primary determinants of regio- and stereoselectivity in catalysis.
- Emerging evidence suggests substrates can significantly influence product selectivity in enzymatic reactions.
Purpose of the Study:
- To highlight enzymatic reactions where substrate intrinsic properties govern stereoselectivity.
- To explore the role of substrate-controlled stereospecificity in natural product biosynthesis.
- To provide insights for enzyme evolution and bioengineering.
Main Methods:
- Review of literature on enzymatic reactions in natural product biosynthesis.
- Analysis of case studies involving lanthipeptides, sactipeptides, and polyketides.
- Focus on reactions demonstrating substrate-governed stereoselectivity.
Main Results:
- Several enzymatic reactions were identified where substrate properties are the main drivers of stereoselectivity.
- Examples include pathways for lanthipeptides, sactipeptides, and polyketides.
- The intrinsic characteristics of the substrate, rather than enzyme features, dictate the catalytic outcome.
Conclusions:
- Substrate-controlled stereospecificity is a significant factor in enzyme catalysis.
- Understanding this mechanism deepens knowledge of enzyme evolution and function.
- This insight can guide bioengineering for novel product development.
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