Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

An endocannabinoid catabolic enzyme FAAH and its paralogs in an early land plant reveal evolutionary and functional relationship with eukaryotic orthologs.

Scientific reports - 20 Feb 2020

Haq Imdadul, Kilaru Aruna

Abstract excerpt

Endocannabinoids were known to exist only among Animalia but recent report of their occurrence in early land plants prompted us to study its function and metabolism. In mammals, anandamide, as an endocannabinoid ligand, mediates several neurological and physiological processes, which are terminated by fatty acid amide hydrolase (FAAH). We identified nine orthologs of FAAH in the moss Physcomitrella patens...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amidohydrolases
Share to Crystallography, X-Ray
Share to Endocannabinoids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen-Ion Concentration

Share to Ligands

Share to Plant Proteins

Share to Protein Structure, Secondary

Share to Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 32080293
DOI: 10.1038/s41598-020-59948-7
PMCID: PMC7033180

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An endocannabinoid catabolic enzyme FAAH and its paralogs in an early land plant reveal evolutionary and functional relationship with eukaryotic orthologs.PMID 32080293Read ↗

Tempo and mode in the endocannaboinoid system.Semantic proximity Read ↗

The endocannabinoid hydrolase FAAH is an allosteric enzyme.Semantic proximity Read ↗

Evidence for distinct roles in catalysis for residues of the serine-serine-lysine catalytic triad of fatty acid amide hydrolase.Semantic proximity Read ↗

Fatty acid amide hydrolase C385A polymorphism affects susceptibility to various diseases.Semantic proximity Read ↗

Mutations in Arabidopsis fatty acid amide hydrolase reveal that catalytic activity influences growth but not sensitivity to abscisic acid or pathogens.Semantic proximity Read ↗

Keys to Lipid Selection in Fatty Acid Amide Hydrolase Catalysis: Structural Flexibility, Gating Residues and Multiple Binding Pockets.Semantic proximity Read ↗

The Interplay between 2-Arachidonoylglycerol and Anandamide Amidohydrolase in NeuropathySemantic proximity Read ↗

Structure-based design of a FAAH variant that discriminates between the N-acyl ethanolamine and taurine families of signaling lipids.Semantic proximity Read ↗

Microdeletion in a FAAH pseudogene identified in a patient with high anandamide concentrations and pain insensitivitySemantic proximity Read ↗

Molecular basis of FAAH-OUT-associated human pain insensitivitySemantic proximity Read ↗

The Role of (E)-β-Farnesene in Tritrophic Interactions: Biosynthesis, Chemoreception, and EvolutionSemantic proximity Read ↗

Molecular basis of <i>FAAH-OUT</i> -associated human pain insensitivitySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.