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Literature summary extracted from

  • Kim, T.J.; Mitsutake, S.; Kato, M.; Igarashi, Y.
    The leucine 10 residue in the pleckstrin homology domain of ceramide kinase is crucial for its catalytic activity (2005), FEBS Lett., 579, 4383-4388.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.138 transient overexpression of FLAG-tagged wild-type and mutant enzymes in HEK293 cells Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.138 E8A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Mus musculus
2.7.1.138 G2A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Mus musculus
2.7.1.138 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
2.7.1.138 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
2.7.1.138 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
2.7.1.138 P9A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Mus musculus
2.7.1.138 S12A site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.138 19.2
-
 ceramide recombinant mutant L10I Mus musculus
2.7.1.138 20.9
-
 ceramide recombinant wild-type enzyme Mus musculus
2.7.1.138 82.7
-
 ATP recombinant mutant L10I Mus musculus
2.7.1.138 85.6
-
 ATP recombinant wild-type enzyme Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.1.138 membrane
-
 Mus musculus 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.138 Ca2+ activates the enzyme Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.138 ATP + ceramide Mus musculus
-
 ADP + ceramide 1-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.138 Mus musculus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.138 ATP + ceramide = ADP + ceramide 1-phosphate Leu10 in the pleckstrin homology domain of the enzyme is crucial for catalytic activity Mus musculus
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.138 additional information
-
-
 Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.138 ATP + ceramide
-
 Mus musculus ADP + ceramide 1-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.138 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

EC Number Synonyms Comment Organism
2.7.1.138 CERK
-
 Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.138 ATP
-
 Mus musculus