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Literature summary for 2.7.1.138 extracted from
- The leucine 10 residue in the pleckstrin homology domain of ceramide kinase is crucial for its catalytic activity (2005), FEBS Lett., 579, 4383-4388.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| transient overexpression of FLAG-tagged wild-type and mutant enzymes in HEK293 cells | Mus musculus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E8A | site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme | Mus musculus |
| G2A | site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme | Mus musculus |
| L10A | site-directed mutagenesis, 99% reduced activity compared to the wild-type enzyme, substrate affinity and activation by Ca2+ are unaffected, mutation within the pleckstrin homology domain | Mus musculus |
| L10I | site-directed mutagenesis, 71% reduced activity compared to the wild-type enzyme, substrate affinity and activation by Ca2+ are unaffected, mutation within the pleckstrin homology domain | Mus musculus |
| additional information | construction of N-terminally truncated mutants lacking the first 7, 12, or 76 amino acid residues, respectively, mutant DELTAN7 is still active while mutants DELTAN12 and DELTAN76 are catalytically inactive | Mus musculus |
| P9A | site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme | Mus musculus |
| S12A | site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme | Mus musculus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 19.2 | - |
ceramide | recombinant mutant L10I | Mus musculus |  |
| 20.9 | - |
ceramide | recombinant wild-type enzyme | Mus musculus | |
| 82.7 | - |
ATP | recombinant mutant L10I | Mus musculus | |
| 85.6 | - |
ATP | recombinant wild-type enzyme | Mus musculus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Mus musculus | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates the enzyme | Mus musculus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + ceramide | Mus musculus | - |
ADP + ceramide 1-phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + ceramide = ADP + ceramide 1-phosphate | Leu10 in the pleckstrin homology domain of the enzyme is crucial for catalytic activity | Mus musculus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Mus musculus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + ceramide | - |
Mus musculus | ADP + ceramide 1-phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the N-terminus of the enzyme harbors a myristoylation site and the pleckstrin homology domain, the first is required for lipid anchor modification of the enzyme, the latter is required for membrane association or activity through high afinity binding of phosphatidyl inositol phosphate | Mus musculus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CERK | - |
Mus musculus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Mus musculus | |
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Release 2023.1 (January 2023)
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