Discover Community Create You

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

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

PLoS computational biology - 1 Jun 2015

Palermo Giulia, Bauer Inga, Campomanes Pablo, Cavalli Andrea, Armirotti Andrea, Girotto Stefania, Rothlisberger Ursula, De Vivo Marco

Abstract excerpt

The fatty acid amide hydrolase (FAAH) regulates the endocannabinoid system cleaving primarily the lipid messenger anandamide. FAAH has been well characterized over the years and, importantly, it represents a promising drug target to treat several diseases, including inflammatory-related diseases and cancer. But its enzymatic mechanism for lipid selection to specifically hydrolyze anandamide, rather than similar...

Read the complete abstract on PubMed

Topics

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

Share to Amidohydrolases
Share to Arachidonic Acids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalysis

Share to Computational Biology

Share to Endocannabinoids

Share to Molecular Dynamics Simulation

Share to Polyunsaturated Alkamides

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 26111155
DOI: 10.1371/journal.pcbi.1004231
PMCID: PMC4481349

Genes

FAAH

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Keys to Lipid Selection in Fatty Acid Amide Hydrolase Catalysis: Structural Flexibility, Gating Residues and Multiple Binding Pockets.PMID 26111155Read ↗

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

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

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

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

Conformational gating, dynamics and allostery in human monoacylglycerol lipase.Semantic proximity Read ↗

Identification of two serine residues involved in catalysis by fatty acid amide hydrolase.Semantic proximity Read ↗

Structural and functional insights into ABHD5, a ligand-regulated lipase co-activator.Semantic proximity Read ↗

A gatekeeper helix determines the substrate specificity of Sjögren-Larsson Syndrome enzyme fatty aldehyde dehydrogenase.Semantic proximity Read ↗

Unsaturated bond recognition leads to biased signal in a fatty acid receptor.Semantic proximity Read ↗

Amphipathic Helices Enable Fatty Acid Uptake and Activation by Human FATP2 at ER Contact SitesSemantic proximity Read ↗

A catalytic mechanism for cysteine N-terminal nucleophile hydrolases, as revealed by free energy simulations.Semantic proximity Read ↗

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