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

Catalytic activity and acyl-chain selectivity of diacylglycerol kinase ɛ are modulated by residues in and near the lipoxygenase-like motif.

Journal of molecular biology - 9 Mar 2012

D'Souza Kenneth, Epand Richard M

Abstract excerpt

Diacylglycerol kinase (DGK) ɛ plays an important role in the resynthesis of phosphatidylinositol by mediating the phosphorylation of diacylglycerol to phosphatidic acid. DGKɛ is unique among mammalian DGK isoforms in that it is the only one that shows acyl-chain selectivity, preferring diacylglycerols with an sn-2 arachidonoyl group. The region responsible for this arachidonoyl specificity is the lipoxygenase...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Catalytic Domain
Share to Cholesterol

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Consensus Sequence

Share to Diacylglycerol Kinase

Share to Diglycerides

Share to Hydrophobic and Hydrophilic Interactions

Share to Lipoxygenase

Source

Identifiers

PMID: 22266092
DOI: 10.1016/j.jmb.2012.01.008

Genes

LOX

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Catalytic activity and acyl-chain selectivity of diacylglycerol kinase ɛ are modulated by residues in and near the lipoxygenase-like motif.PMID 22266092Read ↗

Study of arachidonoyl specificity in two enzymes of the PI cycle.Semantic proximity Read ↗

Mutational scanning pinpoints distinct binding sites of key ATGL regulators in lipolysisSemantic proximity Read ↗

Structure, Mutation, Functional Domain Roles and Medical Implications of Glycerol Kinase.Semantic proximity Read ↗

Site-directed mutagenesis of the active site of diacylglycerol kinase alpha: calcium and phosphatidylserine stimulate enzyme activity via distinct mechanisms.Semantic proximity Read ↗

An intact zinc finger motif of the C1B domain is critical for stability and activity of diacylglycerol kinase-ε.Semantic proximity Read ↗

Mutational scanning pinpoints distinct binding sites of key ATGL regulators in lipolysis.Semantic proximity Read ↗

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

Structure of product-bound SMG1 lipase: active site gating implications.Semantic proximity Read ↗

Structural basis for the activation of PLC-γ isozymes by phosphorylation and cancer-associated mutations.Semantic proximity Read ↗

A cancer-associated mutation in atypical protein kinase Cι occurs in a substrate-specific recruitment motif.Semantic proximity Read ↗

Construction of a catalytically inactive cholesterol oxidase mutant: investigation of the interplay between active site-residues glutamate 361 and histidine 447.Semantic proximity Read ↗

Conformationally constrained analogues of diacylglycerol (DAG). 28. DAG-dioxolanones reveal a new additional interaction site in the C1b domain of PKC delta.Semantic proximity Read ↗

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