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Article

Determinants of pH profile and acyl chain selectivity in lysosomal phospholipase A2.

Journal of lipid research - 1 Jul 2018

Hinkovska-Galcheva Vania, Kelly Robert, Manthei Kelly A, Bouley Renee, Yuan Wenmin, Schwendeman Anna, Tesmer John J G, Shayman James A

Abstract excerpt

Lysosomal phospholipase A2 (LPLA2) is characterized by broad substrate recognition, peak activity at acidic pH, and the transacylation of lipophilic alcohols, especially N-acetyl-sphingosine. Prior structural analysis of LPLA2 revealed the presence of an atypical acidic residue, Asp13, in the otherwise hydrophobic active site cleft. We hypothesized that Asp13 contributed to the pH profile and/or substrate...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 29724779
DOI: 10.1194/jlr.M084012
PMCID: PMC6027918

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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.

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