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Plant fatty acid (ethanol) amide hydrolases
Rhidaya Shrestha1, Sang-chul Kim, John M Dyer
1University of North Texas, Center for Plant Lipid Research, Department of Biological Sciences, Denton, P.O. Box 305220, TX 76203, USA.
Biochimica Et Biophysica Acta
|April 21, 2006
Summary
Fatty acid amide hydrolase (FAAH) enzymes in plants metabolize N-acylethanolamines (NAEs), similar to animal FAAH. These plant enzymes share conserved structures and catalytic residues, indicating a conserved function in regulating lipid mediators.
Area of Science:
- Biochemistry
- Plant Molecular Biology
- Enzymology
Background:
- Fatty acid amide hydrolase (FAAH) regulates N-acylethanolamines (NAEs) in vertebrates, impacting physiological and behavioral processes.
- A plant FAAH homologue suggests a similar pathway for NAE metabolism in plants.
Purpose of the Study:
- To identify and characterize FAAH genes in monocots (Oryza sativa) and legumes (Medicago truncatula).
- To investigate the enzymatic activity and structural properties of plant FAAH proteins.
Main Methods:
- Identification of candidate FAAH genes in rice and M. truncatula.
- Cloning and expression of cDNAs in E. coli to produce recombinant proteins.
- In vitro NAE amidohydrolase assays, kinetic analysis, inhibition studies, sequence alignment, motif analysis, and homology modeling.
Main Results:
- Candidate FAAH genes were identified in rice and M. truncatula with conserved exon-intron organizations.
- Recombinant plant FAAH proteins catalyzed NAE hydrolysis in vitro.
- Plant FAAH enzymes exhibited conserved domain organization and conserved catalytic residues, with similar structure-activity relationships to mammalian FAAH despite low sequence identity.
Conclusions:
- Plant and mammalian FAAH proteins share conserved structure-activity relationships, suggesting a conserved role in NAE metabolism.
- Understanding plant FAAH molecular properties is crucial for elucidating the metabolic regulation of NAE lipid mediators in plants.