Diversity of Acyl-ACP Thioesterases and Their Role in Fatty Acid Biosynthesis
Author Information
Author(s): Jing Fuyuan, Cantu David C, Tvaruzkova Jarmila, Chipman Jay P, Nikolau Basil J, Yandeau-Nelson Marna D, Reilly Peter J
Primary Institution: Iowa State University
Hypothesis
What is the diversity in enzymatic specificity and activity of acyl-ACP thioesterases across different organisms?
Conclusion
The study reveals that acyl-ACP thioesterases can be used to diversify the fatty acid biosynthesis pathway to produce novel fatty acids.
Supporting Evidence
- 31 acyl-ACP thioesterases were characterized from diverse phylogenetic sources.
- Enzymes were clustered into three classes based on substrate specificity.
- Several novel acyl-ACP thioesterases were identified that act on short-chain and unsaturated acyl-ACPs.
Takeaway
Scientists studied different enzymes that help plants make fatty acids and found many types that can create different kinds of fats.
Methodology
The study involved phylogenetic analysis and functional characterization of 31 acyl-ACP thioesterases from various organisms, expressed in E. coli.
Limitations
The study may not cover all acyl-ACP thioesterases, as some sequences could not be grouped into subfamilies.
Statistical Information
P-Value
p<0.001
Statistical Significance
p<0.001
Digital Object Identifier (DOI)
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