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

[Effect of E54 mutation of human secreted phospholipase A2 GIIE on substrate selectivity].

Sheng wu gong cheng xue bao = Chinese journal of biotechnology - 25 Jul 2021

Hou Shulin, Bai Junping, Lu Xin, Zhang Yulong, Xu Tingting, Xie Jun

Abstract excerpt

Human secreted phospholipase A2 GIIE (hGIIE) is involved in inflammation and lipid metabolism due to its ability of hydrolyzing phospholipids. To reveal the mechanism of substrate head-group selectivity, we analyzed the effect of mutation of hGIIE on its activity and selectivity. hGIIE structural analysis showed that E54 might be related to its substrate head-group selectivity. According to the sequence...

Read the complete abstract on PubMed

Topics

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

Share to Kinetics
Share to Mutation
Share to Phospholipids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Saccharomycetales

Share to Substrate Specificity

Source

Identifiers

PMID: 34327916
DOI: 10.13345/j.cjb.200572

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

[Effect of E54 mutation of human secreted phospholipase A2 GIIE on substrate selectivity].PMID 34327916Read ↗

The atypical binding mechanism of second calcium on phospholipase A2 group IIE.Semantic proximity Read ↗

Increasing the flexibility of the substrate binding pocket of Streptomyces phospholipase D can enhance its catalytic efficiency in soybean phosphatidylcholine.Semantic proximity Read ↗

[Semi-rational design improves the catalytic activity of butyrylcholinesterase against ghrelin].Semantic proximity Read ↗

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

Discovery of novel allosteric effectors based on the predicted allosteric sites for Escherichia coli D-3-phosphoglycerate dehydrogenase.Semantic proximity Read ↗

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

Analysis of a novel prophage-encoded group A Streptococcus extracellular phospholipase A(2).Semantic proximity Read ↗

Phosphatase activity of soluble epoxide hydrolase.Semantic proximity Read ↗

A new functional assay reveals that membrane binding is critical for overactivation of the phosphoinositide 3-kinase H1047R mutant.Semantic proximity Read ↗

Enhancing the thermostability of a mono- and diacylglycerol lipase from Malassizia globose by stabilizing a flexible loop in the catalytic pocket.Semantic proximity Read ↗

Effect of Cysteine Residue Substitution in the GCSAG Motif of the PMGL2 Esterase Active Site on the Enzyme Properties.Semantic proximity Read ↗

Allosteric Ensembles Elucidate Mechanisms of Inhibition in Human Soluble Epoxide HydrolaseSemantic proximity Read ↗

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