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Literature summary for 3.5.1.23 extracted from
- Catalytic mechanism of eukaryotic neutral ceramidase (2015), Structure, 23, 1371-1372 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant N-glycosylated extracellular region of nCDase in complex with phosphate, X-ray diffraction structure determination and analysis at 2.6 A resolution | Homo sapiens |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | required, binding site structure analysis | Homo sapiens |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ceramide + H2O | Homo sapiens | - |
fatty acid + sphingosine | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q9NR71 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ceramide + H2O | - |
Homo sapiens | fatty acid + sphingosine | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| neutral ceramidase | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | sphingolipid metabolism and interconnected bioactive metabolites derived from ceramide, overview. Ceramide, the essential synthetic building block for sphingomyelin, glycosphingolipids, and ceramide-1-phosphate is hydrolyzed by ceramidase to fatty acid and sphingosine, which then is phosphorylated to sphingosine-1-phosphate (S1P) by sphingosine kinases | Homo sapiens |
| additional information | analysis of the catalytic mechanism of eukaryotic neutral ceramidase, structurally based explanation for ceramide specificity, comparison to the bacterial neutral ceramidase, overview. A general acid-base catalysis mechanism is proposed for amide bond hydrolysis by nCDase. In this mechanism, the Zn2+ ion functions to activate a water molecule for nucleophilic attack of the amide carbon. His196 serves as a general base for proton extraction from water and subsequently, a general acid to shuttle this proton to the nitrogen of ceramide during amide bond cleavage. The catalytic domain of the human enzyme contains an extra 30-residue subdomain inserted within the loop between beta14 and alpha7. In human nCDase, the 30-residue subdomain insert replacing the 6-residue span of bacterial CDase displays specific mobility. Stabilization of the subdomain conformation is aided by two internal disulfide bridges, formed by four cysteines that are conserved in eukaryotes | Homo sapiens |
| physiological function | neutral ceramidases are key enzymes of sphingolipid metabolism that hydrolyze the fatty acyl/sphingosine amide linkage of ceramide at neutral pH | Homo sapiens |
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Release 2023.1 (January 2023)
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