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Literature summary extracted from

  • Liao, H.; Aoyama, C.; Ishidate, K.; Teraoka, H.
    Deletion and alanine mutation analyses for the formation of active homo- or hetero-dimer complexes of mouse choline kinase-alpha and -beta (2006), Biochim. Biophys. Acta, 1761, 111-120.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.32 expressed in COS-7 cells Mus musculus
2.7.1.32 expression in COS-7 cells Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.32 0.032
-
 choline isozyme CK-beta Mus musculus
2.7.1.32 0.055
-
 choline isozyme CK-alpha1/beta Mus musculus
2.7.1.32 0.083
-
 choline isozyme CK-alpha Mus musculus
2.7.1.32 0.157
-
 choline N-terminal truncated enzyme version of CK-beta Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.32 Mg2+ required for activity Mus musculus

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.32 ATP + choline
-
 Mus musculus ADP + O-phosphocholine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.32 dimer 60% of the active enzyme exists as homodimer and 20% as heterodimer Mus musculus

Synonyms

EC Number Synonyms Comment Organism
2.7.1.32 CK-alpha
-
 Mus musculus
2.7.1.32 CK-alpha1/beta
-
 Mus musculus
2.7.1.32 CK-beta
-
 Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.32 ATP
-
 Mus musculus