Plant fatty acid (ethanol) amide hydrolases

Shrestha, Rhidaya; Kim, Sang‐Chul; Dyer, John M.; Dixon, Richard A.; Chapman, Kent D.

doi:10.1016/j.bbalip.2006.03.004

Cited by 27 publications

(37 citation statements)

References 37 publications

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“…The proteins were visualized in gels by Coomassie Blue staining, or proteins were electrophoretically transferred to polyvinylidene fluoride (PVDF) membranes (0.2 m; Bio-Rad) according to the protocol described elsewhere (10). The recombinant proteins expressing the His tag at the C terminus were detected by chemiluminescence using a 1:2000 dilution of mouse monoclonal anti-His antibodies (ABGENT, San Diego, CA) and a solution of 1:4000 dilution of goat anti-mouse IgG conjugated to a peroxidase (Bio-Rad).…”

Section: Sds-page and Western Blotting Of Purified Faah Proteinseach mentioning

confidence: 99%

“…FAAH Assays on Purified Proteins from Different E. coli Cell Lines-The NAE amidohydrolase assays were conducted as described previously (7,10,33) with few modifications. The reactions were conducted for 30 min at 30°C, 120 rpm, in 150 l of BTP buffer (50 mM BisTris propane-HCl, pH 9.0) containing different concentrations of radiolabeled NAEs, the new NAElike compounds, and different concentrations of purified protein (see figure legends for more details of the composition of each reaction mixture).…”

Section: Sds-page and Western Blotting Of Purified Faah Proteinseach mentioning

confidence: 99%

“…Enzyme reactions were terminated by the addition of hot isopropyl alcohol (70°C). The lipids were extracted, and the distribution of the radioactivity was evaluated by radiometric scanning of TLC plates as described elsewhere (10).…”

Section: Sds-page and Western Blotting Of Purified Faah Proteinseach mentioning

confidence: 99%

“…The x-ray crystallography data of the rat protein provided new insights about the mode of action of this enzyme in NAE hydrolysis identifying a Ser-Ser-Lys catalytic triad (9,10). Although no tertiary structure has been determined yet for plant FAAH, a structural homology model was developed for the amidase domain of the Arabidopsis FAAH protein, and conserved catalytic residues were identified experimentally (10,11).…”

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Synthesis of Phenoxyacyl-Ethanolamides and Their Effects on Fatty Acid Amide Hydrolase Activity

Faure

Nagarajan

Hwang

et al. 2014

Journal of Biological Chemistry

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Background: Fatty acid amide hydrolase (FAAH) belongs to the family of amidase signature proteins and is involved in N-acylethanolamine (NAE) metabolism. Results: New synthetic phenoxyacyl-ethanolamide compounds increased the amidohydrolase activity of FAAH. Conclusion: Phenoxyacyl-ethanolamide compounds increased the activity of the FAAH enzyme in plants and animals. Significance: New properties of FAAH proteins were revealed with these phenoxyacyl-ethanolamide compounds, and the potential for their applications in vivo was demonstrated.

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Section: Sds-page and Western Blotting Of Purified Faah Proteinseach mentioning

confidence: 99%

Section: Sds-page and Western Blotting Of Purified Faah Proteinseach mentioning

confidence: 99%

Section: Sds-page and Western Blotting Of Purified Faah Proteinseach mentioning

confidence: 99%

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confidence: 99%

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Synthesis of Phenoxyacyl-Ethanolamides and Their Effects on Fatty Acid Amide Hydrolase Activity

Faure

Nagarajan

Hwang

et al. 2014

Journal of Biological Chemistry

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“…Functional homologues of the Arabidopsis FAAH (AtFAAH) also were identified in Oryza sativa and Medicago truncatula, supporting a common mechanism for the regulation of NAE hydrolysis in diverse plant species (15). To begin to understand the in vivo role of NAEs in plants, we generated Arabidopsis plants with altered AtFAAH expression and analyzed their response to an NAE type that we have previously shown to induce strong morphological effects on seedlings (9,10).…”

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confidence: 99%

Manipulation of Arabidopsis fatty acid amide hydrolase expression modifies plant growth and sensitivity to N -acylethanolamines

Wang

Shrestha

Kilaru

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

158

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In vertebrates, the endocannabinoid signaling pathway is an important lipid regulatory pathway that modulates a variety of physiological and behavioral processes. N-Acylethanolamines (NAEs) comprise a group of fatty acid derivatives that function within this pathway, and their signaling activity is terminated by an enzyme called fatty acid amide hydrolase (FAAH), which hydrolyzes NAEs to ethanolamine and their corresponding free fatty acids. Bioinformatic approaches led to the identification of plant homologues of FAAH that are capable of hydrolyzing NAEs in vitro. To better understand the role of NAEs in plants, we identified T-DNA knockouts to Arabidopsis FAAH (AtFAAH; At5g64440) and generated plants overexpressing AtFAAH. Here we show that seeds of AtFAAH knockouts had elevated levels of endogenous NAEs, and seedling growth was hypersensitive to exogenously applied NAE. On the other hand, seeds and seedlings of AtFAAH overexpressors had lower endogenous NAE content, and seedlings were less sensitive to exogenous NAE. Moreover, AtFAAH overexpressors displayed enhanced seedling growth and increased cell size. AtFAAH expression and FAAH catalytic activity increased during seed germination and seedling growth, consistent with the timing of NAE depletion during seedling establishment. Collectively, our results show that AtFAAH is one, but not the only, modulator of endogenous NAE levels in plants, and that NAE depletion likely participates in the regulation of plant growth.endocannabinoids ͉ lipids ͉ seedling growth ͉ signaling

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Ex vivo lipidomics reveal monoacylglycerols as substrates for a fatty acid amide hydrolase in the legume Medicago truncatula

Arias‐Gaguancela,

Herrell,

Chapman

2024

FEBS Letters

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Fatty acid amide hydrolase (FAAH) is a conserved hydrolase in eukaryotes with promiscuous activity toward a range of acylamide substrates. The native substrate repertoire for FAAH has just begun to be explored in plant systems outside the model Arabidopsis thaliana. Here, we used ex vivo lipidomics to identify potential endogenous substrates for Medicago truncatula FAAH1 (MtFAAH1). We incubated recombinant MtFAAH1 with lipid mixtures extracted from M. truncatula and resolved their profiles via gas chromatography–mass spectrometry (GC–MS). Data revealed that besides N‐acylethanolamines (NAEs), sn‐1 or sn‐2 isomers of monoacylglycerols (MAGs) were substrates for MtFAAH1. Combined with in vitro and computational approaches, our data support both amidase and esterase activities for MtFAAH1. MAG‐mediated hydrolysis via MtFAAH1 may be linked to biological roles that are yet to be discovered.

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Plant fatty acid (ethanol) amide hydrolases

Cited by 27 publications

References 37 publications

Synthesis of Phenoxyacyl-Ethanolamides and Their Effects on Fatty Acid Amide Hydrolase Activity

Synthesis of Phenoxyacyl-Ethanolamides and Their Effects on Fatty Acid Amide Hydrolase Activity

Manipulation of Arabidopsis fatty acid amide hydrolase expression modifies plant growth and sensitivity to N -acylethanolamines

Ex vivo lipidomics reveal monoacylglycerols as substrates for a fatty acid amide hydrolase in the legume Medicago truncatula

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