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A Customizable Approach for the Enzymatic Production and Purification of Diterpenoid Natural Products
Published on: October 4, 2019
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A Mechanism for Evolving Novel Plant Sesquiterpene Synthase Function.
Troy Wymore1, Brian Y Chen2, Hugh B Nicholas2
1National Resource for Biomedical Supercomputing, Pittsburgh Supercomputing Center, 300 South Craig Street, Pittsburgh, PA 15213, USA phone: 412-268-4960; fax: 412-268-8200. wymore@psc.edu.
Molecular Informatics
|July 29, 2016
Summary
Plant sesquiterpene synthases are crucial for plant defense. A conserved Asp-Tyr-Asp triad plays a key role in their catalytic cycle, enabling the evolution of new enzyme functions.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Plant sesquiterpene synthases (SsPS) are diverse enzymes vital for plant defense.
- They synthesize complex compounds with high specificity.
- Understanding their catalytic mechanisms and evolution is crucial.
Purpose of the Study:
- To perform a large-scale phylogenetic analysis of plant SsPS.
- To integrate phylogenetic data with structural and experimental information.
- To elucidate the catalytic mechanisms and evolutionary patterns of SsPS.
Main Methods:
- High-resolution phylogenetic analysis of approximately 200 plant SsPS.
- Integration of structural and experimental data.
- Sequence clustering and analysis of conserved catalytic steps.
Main Results:
- Phylogenetic clustering revealed conserved catalytic mechanisms within SsPS groups.
- A highly conserved Asp-Tyr-Asp triad was identified across SsPS.
- This triad is implicated in proton transfer during the catalytic cycle.
Conclusions:
- The conserved Asp-Tyr-Asp triad is a key functional element in plant SsPS catalysis.
- Variations in triad positioning, influenced by external residues, drive enzyme evolution.
- This provides insights into the functional diversification of SsPS.
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