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Synonyms
choline kinase, choline kinase alpha, chokalpha, choline kinase beta, choline/ethanolamine kinase, chk-alpha, chokalpha1, schok, ck-alpha, choline kinase-alpha,
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0.7
ATP
-
isozyme CKB-2, pH 10.0, 37°C
1
ATP
-
C252S mutant enzyme, pH 10, 37°C
1
ATP
-
N308Q mutant enzyme, pH 10, 37°C
1.2
ATP
-
N354A mutant enzyme, pH 10, 37°C
1.3
ATP
-
D255D mutant enzyme, pH 10, 37°C
1.5
ATP
-
N308D mutant enzyme, pH 10, 37°C
1.7
ATP
-
E134A mutant enzyme, pH 10, 37°C
1.7
ATP
-
N87A mutant enzyme, pH 10, 37°C
1.7
ATP
-
wild type enzyme including His-tag, pH 10, 37°C
1.9
ATP
-
H253A mutant enzyme, pH 10, 37°C
1.9
ATP
-
S85T mutant enzyme, pH 10, 37°C
2
ATP
-
N308A mutant enzyme, pH 10, 37°C
2.2
ATP
-
E125D mutant enzyme, pH 10, 37°C
2.2
ATP
-
R149A mutant enzyme, pH 10, 37°C
2.2
ATP
-
W387A mutant enzyme, pH 10, 37°C
2.3
ATP
-
R149K mutant enzyme, pH 10, 37°C
2.4
ATP
-
isozyme CKA-2, pH 10.0, 37°C
2.4
ATP
-
wild type enzyme, pH 10, 37°C
2.5
ATP
-
S86A mutant enzyme, pH 10, 37°C
3.1
ATP
-
N260A mutant enzyme, pH 10, 37°C
3.2
ATP
-
E125A mutant enzyme, pH 10, 37°C
4.2
ATP
-
E125Q mutant enzyme, pH 10, 37°C
4.5
ATP
-
E151A mutant enzyme, pH 10, 37°C
5.4
ATP
-
E303A mutant enzyme, pH 10, 37°C
6.9
ATP
-
E303D mutant enzyme, pH 10, 37°C
7
ATP
-
R111A mutant enzyme, pH 10, 37°C
8.8
ATP
-
E303Q mutant enzyme, pH 10, 37°C
45
ATP
-
E320A mutant enzyme, pH 10, 37°C
0.002
choline
-
dimer
0.4
choline
-
N260A mutant enzyme, pH 10, 37°C
0.7
choline
-
R149A mutant enzyme, pH 10, 37°C
0.7
choline
-
S85T mutant enzyme, pH 10, 37°C
0.8
choline
-
E125D mutant enzyme, pH 10, 37°C
0.8
choline
-
N308Q mutant enzyme, pH 10, 37°C
1
choline
-
C252S mutant enzyme, pH 10, 37°C
1
choline
-
N308D mutant enzyme, pH 10, 37°C
1
choline
-
N354A mutant enzyme, pH 10, 37°C
1
choline
-
wild type enzyme including His-tag, pH 10, 37°C
1.1
choline
-
E125A mutant enzyme, pH 10, 37°C
1.2
choline
-
R149K mutant enzyme, pH 10, 37°C
1.2
choline
-
W387A mutant enzyme, pH 10, 37°C
1.5
choline
-
N308A mutant enzyme, pH 10, 37°C
1.6
choline
-
isozyme CKA-2, pH 10.0, 37°C
1.6
choline
-
E125Q mutant enzyme, pH 10, 37°C
1.6
choline
-
H253A mutant enzyme, pH 10, 37°C
1.6
choline
-
wild type enzyme, pH 10, 37°C
1.7
choline
-
R111A mutant enzyme, pH 10, 37°C
1.8
choline
-
E134A mutant enzyme, pH 10, 37°C
1.8
choline
-
N87A mutant enzyme, pH 10, 37°C
2.2
choline
-
E151A mutant enzyme, pH 10, 37°C
3
choline
-
E320A mutant enzyme, pH 10, 37°C
3.4
choline
-
E303Q mutant enzyme, pH 10, 37°C
3.6
choline
-
E303D mutant enzyme, pH 10, 37°C
5
choline
-
S86A mutant enzyme, pH 10, 37°C
5.4
choline
-
D255D mutant enzyme, pH 10, 37°C
10
choline
-
E303A mutant enzyme, pH 10, 37°C
13
choline
-
isozyme CKB-2, pH 10.0, 37°C
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0.24
choline
-
N260A mutant enzyme, pH 10, 37°C
0.25
choline
-
D255D mutant enzyme, pH 10, 37°C
2.4
choline
-
W387A mutant enzyme, pH 10, 37°C
2.6
choline
-
N354A mutant enzyme, pH 10, 37°C
7
choline
-
E303A mutant enzyme, pH 10, 37°C
9.8
choline
-
S86A mutant enzyme, pH 10, 37°C
20.8
choline
-
N308A mutant enzyme, pH 10, 37°C
21
choline
-
E125A mutant enzyme, pH 10, 37°C
27.1
choline
-
R111A mutant enzyme, pH 10, 37°C
29.7
choline
-
N87A mutant enzyme, pH 10, 37°C
31.4
choline
-
E125Q mutant enzyme, pH 10, 37°C
35.7
choline
-
S85T mutant enzyme, pH 10, 37°C
37.5
choline
-
N308Q mutant enzyme, pH 10, 37°C
38.7
choline
-
E303D mutant enzyme, pH 10, 37°C
38.9
choline
-
R149A mutant enzyme, pH 10, 37°C
42.9
choline
-
H253A mutant enzyme, pH 10, 37°C
58.7
choline
-
E303Q mutant enzyme, pH 10, 37°C
72.3
choline
-
wild type enzyme including His-tag, pH 10, 37°C
74
choline
-
wild type enzyme, pH 10, 37°C
79.9
choline
-
E320A mutant enzyme, pH 10, 37°C
84.3
choline
-
C252S mutant enzyme, pH 10, 37°C
84.6
choline
-
N308D mutant enzyme, pH 10, 37°C
87.9
choline
-
R149K mutant enzyme, pH 10, 37°C
89.2
choline
-
E151A mutant enzyme, pH 10, 37°C
97.3
choline
-
E134A mutant enzyme, pH 10, 37°C
130
choline
-
E125D mutant enzyme, pH 10, 37°C
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C252S
-
slightly increased turnover
D313A
-
low expression level
E134A
-
slightly increased turnover
E151A
-
slightly increased turnover
E303N
-
small reduction of kcat
H181A
-
low expression level
N254A
-
similar initial activity like wild type enzyme, but time instability
N308 A
-
small reduction of kcat
N354A
-
strongly reduced activity, only minor effect on Km for both substrates
R149K
-
slightly increased turnover
S86T
-
moderate reduction of the catalytic efficiency
D255A
-
no activity detectable
D255A
-
omplete loss of activity
D255E
-
activity almost completely abolished
D255E
-
small residual activity
D255N
-
no activity detectable
D255N
-
small residual activity
D301A
-
complete loss of activity
D301A
-
no activity detectable
D301E
-
complete loss of activity
D301E
-
no activity detectable
D301N
-
complete loss of activity
D301N
-
no activity detectable
E125A
-
reduced activity
E125A
-
modest reduction of kcat and Km for ATP
E125D
-
increased turnover
E125Q
-
reduced activity
E125Q
-
modest reduction of kcat and Km for ATP
E303A
-
strongly reduced activity, increased Km for both substrates, strongly increased Km for Mg2+
E303A
-
strong reduction of the catalytic efficiency
E303D
-
reduced activity
E303D
-
small reduction of kcat
E320A
-
slightly increased turnover
E320A
-
reduction of ATP affinity and time instability
H253A
-
reduced activity
H253A
-
similar initial activity like wild type enzyme, but time instability
N260A
-
activity almost completely abolished, strongly increased Km for Mg2+
N260A
-
small residual activity
N308D
-
slightly increased turnover
N308D
-
modest reduction of kcat
N308Q
-
reduced activity
N308Q
-
modest reduction of kcat
N87A
-
reduced activity
N87A
-
small reduction of the catalytic efficiency
R111A
-
reduced activity
R111A
-
4-fold increase in Km for ATP
R149A
-
reduced activity
S86A
-
strongly reduced activity, increased Km for ATP
S86A
-
pronounced reduction of the catalytic efficiency
W387A
-
strongly reduced activity, only minor effect on Km for both substrates
W387A
-
strong reduction of kcat (30-fold)
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Gee, P.; Kent, C.
Multiple isoforms of choline kinase from Caenorhabditis elegans: cloning, expression, purification, and characterization
Biochim. Biophys. Acta
1648
33-42
2003
Caenorhabditis elegans
brenda
Peisach, D.; Gee, P.; Kent, C.; Xu, Z.
The crystal structure of choline kinase reveals a eukaryotic protein kinase fold
Structure
11
703-713
2003
Caenorhabditis elegans
brenda
Yuan, C.; Kent, C.
Identification of critical residues of ATP kinase A2 from Caenorhabditis elegans
J. Biol. Chem.
279
17801-17809
2004
Caenorhabditis elegans
brenda
Aoyama, C.; Liao, H.; Ishidate, K.
Structure and function of choline kinase isoforms in mammalian cells
Prog. Lipid Res.
43
266-281
2004
Saccharomyces cerevisiae, Caenorhabditis elegans, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Milanese, L.; Espinosa, A.; Campos, J.M.; Gallo, M.A.; Entrena, A.
Insight into the inhibition of human choline kinase: homology modeling and molecular dynamics simulations
ChemMedChem
1
1216-1228
2006
Caenorhabditis elegans, Homo sapiens
brenda
Janardhan, S.; Srivani, P.; Sastry, G.N.
Choline kinase: an important target for cancer
Curr. Med. Chem.
13
1169-1186
2006
Saccharomyces cerevisiae, Caenorhabditis elegans, Homo sapiens, Mus musculus, Rattus norvegicus, Schizosaccharomyces pombe
brenda