EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.1.23 | expression in Escherichia coli BL21(DE3) | Pseudomonas aeruginosa |
3.5.1.23 | wild-type and C-terminal truncated CDase, expression in HEK-293 cells | Rattus norvegicus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.5.1.23 | E757R | mutation has no effect on activity, subcellular localization of mutant CDase expressed in HEK-293 cells | Rattus norvegicus |
3.5.1.23 | F756D | inactive mutant, subcellular localization of mutant CDase expressed in HEK-293 cells | Rattus norvegicus |
3.5.1.23 | F756I | mutation has little effect on activity, subcellular localization of mutant CDase expressed in HEK-293 cells | Rattus norvegicus |
3.5.1.23 | F756R | inactive mutant, subcellular localization of mutant CDase expressed in HEK-293 cells | Rattus norvegicus |
3.5.1.23 | I758D | inactive mutant, subcellular localization of mutant CDase expressed in HEK-293 cells | Rattus norvegicus |
3.5.1.23 | I758F | mutation decreases activity to 20% of wild-type CDase activity, subcellular localization of mutant CDase expressed in HEK-293 cells | Rattus norvegicus |
3.5.1.23 | I758R | inactive mutant, subcellular localization of mutant CDase expressed in HEK-293 cells | Rattus norvegicus |
3.5.1.23 | I758V | same activity as wild-type CDase, subcellular localization of mutant CDase expressed in HEK-293 cells | Rattus norvegicus |
3.5.1.23 | additional information | truncation of four, but not three, amino acid residues at the C-terminus results in a complete loss of activity as well as surface expression in HEK-293 cells, the truncated enzymes are retained in the endoplasmic reticulum and rapidly degraded without transportation to the Golgi apparatus also leading to an immature/incorrect glycosylation of the protein | Rattus norvegicus |
3.5.1.23 | additional information | truncation of six C-terminal amino acids, but not of five, results in complete loss of CDase activity | Pseudomonas aeruginosa |
3.5.1.23 | V665D | inactive mutant | Pseudomonas aeruginosa |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.5.1.23 | endoplasmic reticulum | 113 kDa developing form, enzyme which is truncated at the C-terminus by four amino acids is retained in the endoplasmic reticulum and rapidly degraded without transportation to the Golgi apparatus | Rattus norvegicus | 5783 | - |
3.5.1.23 | Golgi apparatus | 133 kDa mature form | Rattus norvegicus | 5794 | - |
3.5.1.23 | additional information | subcellular localization of wild-type and several C-terminal truncated CDases | Rattus norvegicus | - |
- |
3.5.1.23 | plasma membrane | wild-type CDase is located at plasma membranes | Rattus norvegicus | 5886 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.23 | additional information | Rattus norvegicus | neutral ceramidase is involved in the regulation of ceramide-mediated signaling | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.23 | Pseudomonas aeruginosa | - |
- |
- |
3.5.1.23 | Rattus norvegicus | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.5.1.23 | glycoprotein | - |
Rattus norvegicus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.23 | 4-nitrobenzo-2-oxa-1,3-diazoyl-N-dodecanoylsphingosine + H2O | - |
Rattus norvegicus | 4-nitrobenzo-2-oxa-1,3-diazoyl-dodecanoic acid + sphingosine | - |
r | |
3.5.1.23 | additional information | neutral ceramidase is involved in the regulation of ceramide-mediated signaling | Rattus norvegicus | ? | - |
? | |
3.5.1.23 | additional information | the C-terminal residues Ile-758 and Phe-756 are essential for enzyme function, the C-terminal tail is indispensable for the correct folding, localization and enzyme activity | Rattus norvegicus | ? | - |
? | |
3.5.1.23 | additional information | the C-terminal tail is essential for enzyme activity and correct folding | Pseudomonas aeruginosa | ? | - |
? | |
3.5.1.23 | N-acylsphingosine + H2O | CDase cleaves the N-acyl linkage of ceramide to produce sphingosine and free fatty acid | Rattus norvegicus | a carboxylate + sphingosine | - |
? | |
3.5.1.23 | N-acylsphingosine + H2O | CDase cleaves the N-acyl linkage of ceramide to produce sphingosine and free fatty acid | Pseudomonas aeruginosa | a carboxylate + sphingosine | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.5.1.23 | More | the C-terminal tail is essential for enzyme activity and correct folding | Pseudomonas aeruginosa |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.23 | CDase | - |
Rattus norvegicus |
3.5.1.23 | CDase | - |
Pseudomonas aeruginosa |
3.5.1.23 | neutral ceramidase | - |
Rattus norvegicus |
3.5.1.23 | neutral ceramidase | - |
Pseudomonas aeruginosa |