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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Multifunctional acyltransferases from Tetrahymena thermophila
Eva-Maria Biester1, Janine Hellenbrand, Margrit Frentzen
1Institute for Biology I, RWTH Aachen University, Worringer Weg 1, 52074 Aachen, Germany. em.biester@bio1.rwth-aachen.de
Lipids
|December 14, 2011
Summary
Researchers identified novel multifunctional acyltransferases in Tetrahymena thermophila. These enzymes produce triacylglycerols and wax esters, expanding our understanding of lipid metabolism and DGAT2-related enzymes.
Area of Science:
- Biochemistry
- Molecular Biology
- Protozoology
Background:
- Multifunctional acyltransferases esterify various acyl-acceptors with activated fatty acids.
- Mammalian acyltransferases share structural and functional properties relevant to lipid synthesis.
Purpose of the Study:
- Identify and characterize novel acyltransferases from Tetrahymena thermophila.
- Investigate the catalytic activities and substrate specificities of these protozoan enzymes.
- Determine their relationship to known diacylglycerol acyltransferase 2 (DGAT2) family members.
Main Methods:
- Sequence analysis to identify candidate proteins with acyltransferase motifs and predicted transmembrane structures.
- Heterologous expression of Tetrahymena sequences in recombinant yeast.
- In vitro enzymatic assays using various acyl-acceptors and acyl-CoA thioesters.
Main Results:
- Four Tetrahymena proteins were identified with characteristics similar to mammalian acyltransferases.
- Recombinant yeast expressing these proteins produced triacylglycerols and wax esters.
- Enzymatic assays confirmed the esterification of fatty alcohols, diols, diacylglycerols, and isoprenols with acyl-CoA thioesters.
Conclusions:
- A new group of DGAT2-related multifunctional acyltransferases has been identified in protozoa.
- These enzymes play a role in lipid biosynthesis, including the production of triacylglycerols and wax esters.
- The findings expand the known diversity of acyltransferases and their evolutionary relationships.
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