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

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

The Journal of biological chemistry - 26 Sept 2003

McKinney Michele K, Cravatt Benjamin F

Abstract excerpt

Fatty acid amide hydrolase (FAAH) is a mammalian amidase signature enzyme that inactivates neuromodulatory fatty acid amides, including the endogenous cannabinoid anandamide and the sleep-inducing substance oleamide. The recent determination of the three-dimensional structures of FAAH and two distantly related bacterial amidase signature enzymes indicates that these enzymes employ an unusual serine-serine-lysine...

Read the complete abstract on PubMed

Topics

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

Share to Amidohydrolases
Share to Catalysis
Share to Hydrolysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinetics

Share to Lysine

Share to Serine

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 12734197
DOI: 10.1074/jbc.M303922200

Genes

FAAH

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evidence for distinct roles in catalysis for residues of the serine-serine-lysine catalytic triad of fatty acid amide hydrolase.PMID 12734197Read ↗

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

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

The endocannabinoid hydrolase FAAH is an allosteric enzyme.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 ↗

Superfamily-wide portrait of serine hydrolase inhibition achieved by library-versus-library screeningSemantic proximity Read ↗

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

Structural basis for the activation of acid ceramidase.Semantic proximity Read ↗

A rationally designed mutant of plasma platelet-activating factor acetylhydrolase hydrolyzes the organophosphorus nerve agent soman.Semantic proximity Read ↗

Endocannabinoid enzyme engineering: soluble human thio-monoacylglycerol lipase (sol-S-hMGL).Semantic proximity Read ↗

ASM variants in the spotlight: A structure-based atlas for unraveling pathogenic mechanisms in lysosomal acid sphingomyelinaseSemantic proximity Read ↗

Covalent inhibitors of human monoacylglycerol lipase: ligand-assisted characterization of the catalytic site by mass spectrometry and mutational analysis.Semantic proximity Read ↗

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