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

Mutation of F417 but not of L418 or L420 in the lipid binding domain decreases the activity of triacylglycerol hydrolase.

Journal of lipid research - 1 Feb 2006

Alam Mustafa, Gilham Dean, Vance Dennis E, Lehner Richard

Abstract excerpt

Human triacylglycerol hydrolase (hTGH) has been shown to play a role in hepatic lipid metabolism. Triacylglycerol hydrolase (TGH) hydrolyzes insoluble carboxylic esters at lipid/water interfaces, although the mechanism by which the enzyme adsorbs to lipid droplets is unclear. Three-dimensional modeling of hTGH predicts that catalytic residues are adjacent to an alpha-helix that may mediate TGH/lipid interaction....

Read the complete abstract on PubMed

Topics

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

Share to Acylation
Share to Butyrates
Share to Catalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cysteine

Share to Lipase

Share to Nitrophenols

Share to Phenylalanine

Share to Spodoptera

Source

Identifiers

PMID: 16282638
DOI: 10.1194/jlr.M500344-JLR200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Mutation of F417 but not of L418 or L420 in the lipid binding domain decreases the activity of triacylglycerol hydrolase.PMID 16282638Read ↗

Val-407 and Ile-408 in the beta5'-loop of pancreatic lipase mediate lipase-colipase interactions in the presence of bile salt micelles.Semantic proximity Read ↗

DDHD2 possesses both lipase and transacylase capacities that remodel triglyceride acyl chainsSemantic proximity Read ↗

Phosphatase activity of soluble epoxide hydrolase.Semantic proximity Read ↗

Effects of natural mutations in lecithin:cholesterol acyltransferase on the enzyme structure and activity.Semantic proximity Read ↗

Structural basis for catalysis and substrate specificity of human ACAT1Semantic proximity Read ↗

Distant homology modeling of LCAT and its validation through in silico targeting and in vitro and in vivo assays.Semantic proximity Read ↗

Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase.Semantic proximity Read ↗

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

Novel N-terminal mutation of human apolipoprotein A-I reduces self-association and impairs LCAT activation.Semantic proximity Read ↗

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

Crystal structure of PMGL2 esterase from the hormone-sensitive lipase family with GCSAG motif around the catalytic serine.Semantic proximity Read ↗

Discovery of a novel homocysteine thiolactone hydrolase and the catalytic activity of its natural variants.Semantic proximity Read ↗

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