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Literature summary for 3.5.1.23 extracted from
- Autoproteolytic cleavage and activation of human acid ceramidase (2008), J. Biol. Chem., 283, 11253-11259.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | a highly purified, recombinant human acid ceramidase precursor undergoes self-cleavage into alpha and beta subunits. The following mechanism for acid ceramidase self-cleavage and activation is proposed: Asp162 likely forms a hydrogen bond with Cys143, initiating a conformational change that allows Arg159 to act as a proton acceptor. This, in turn, facilitates an intermediate thioether bond between Cys143 and Ile142, the site of acid ceramidase cleavage. Hydrolysis of this bond is catalyzed by water | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| acid ceramidase | - |
Homo sapiens |
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Release 2023.1 (January 2023)
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