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Article

Functional characterization of the postulated intramolecular sphingolipid activator protein domain of human acid sphingomyelinase.

Biological chemistry - 1 Dec 2004

Kölzer Melanie, Ferlinz Klaus, Bartelsen Oliver, Hoops Silvia Locatelli, Lang Florian, Sandhoff Konrad

Abstract excerpt

Degradation of membrane-bound sphingomyelin to phosphorylcholine and ceramide is catalyzed by the water-soluble lysosomal acid sphingomyelinase (A-SMase). The presence of sphingolipid activator proteins (Saps: saposins A-D; GM2 activator) is not essential to mediate this reaction at the water-lipid interface in vivo . A hypothesis based on amino acid sequence alignments suggests that the enzyme possesses an...

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Identifiers

PMID: 15653433
DOI: 10.1515/BC.2004.154

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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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