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Article

Carboxyl-terminal disulfide bond of acid sphingomyelinase is critical for its secretion and enzymatic function.

Biochemistry - 25 Dec 2007

Lee Ching Yin, Tamura Taku, Rabah Nadia, Lee Dong-Young Donna, Ruel Isabelle, Hafiane Anouar, Iatan Iulia, Nyholt Dana, Laporte Frédéric, Lazure Claude, Wada Ikuo, Krimbou Larbi, Genest Jacques

Abstract excerpt

The human acid sphingomyelinase (ASM, EC 3.1.4.12), a lysosomal and secretory protein coded by the sphingomyelin phosphodiesterase 1 (SMPD-1) gene, catalyzes the degradation of sphingomyelin (SM) to ceramide and phosphorylcholine. We examined the structural-functional properties of its carboxyl-terminus (amino acids 462-629), which harbors approximately 1/3 of all mutations discovered in the SMPD-1 gene. We...

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PMID: 18052040
DOI: 10.1021/bi700817g

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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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