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ABSTRACT:
SUBMITTER: Shtraizent N
PROVIDER: S-EPMC2431059 | biostudies-literature | 2008 Apr
REPOSITORIES: biostudies-literature
Shtraizent Nataly N Eliyahu Efrat E Park Jae-Ho JH He Xingxuan X Shalgi Ruth R Schuchman Edward H EH
The Journal of biological chemistry 20080214 17
Herein we report the mechanism of human acid ceramidase (AC; N-acylsphingosine deacylase) cleavage and activation. A highly purified, recombinant human AC precursor underwent self-cleavage into alpha and beta subunits, similar to other members of the N-terminal nucleophile hydrolase superfamily. This reaction proceeded with first order kinetics, characteristic of self-cleavage. AC self-cleavage occurred most rapidly at acidic pH, but also at neutral pH. Site-directed mutagenesis and expression s ...[more]