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Literature summary for 2.7.1.32 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)

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
CK-alpha
-
Mus musculus
CK-alpha1/beta
-
Mus musculus
CK-beta
-
Mus musculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Mus musculus