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

Authors :
Ching Yin Lee
Tamura, Taku
Rabah, Nadia
Dong-Young Donna Lee
Ruel, Isabelle
Hafiane, Anouar
Iatan, Iulia
Nyholt, Dana
Laporte, Frederic
Lazure, Claude
Wada, Ikuo
Krimbou, Larbi
Genest, Jacques
Source :
Biochemistry. Dec 25, 2007, Vol. 46 Issue 51, p14969, 10 p.
Publication Year :
2007

Abstract

A study was conducted to explore the structural and functional properties of carboxyl-terminus (amino acids 462-629) from the human acid sphingomyelinase (ASM), protein coded by the sphingomyelin phosphodiesterase 1 (SMPD-1). The results suggest that the carboxyl-terminus of the ASM is crucial for its protein structure which dictates the enzymatic function and secretion.

Details

Language :
English
ISSN :
00062960
Volume :
46
Issue :
51
Database :
Gale General OneFile
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
edsgcl.174099787