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C252S
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slightly increased turnover
D313A
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low expression level
E134A
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slightly increased turnover
E151A
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slightly increased turnover
E303N
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small reduction of kcat
H181A
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low expression level
N254A
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similar initial activity like wild type enzyme, but time instability
N308 A
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small reduction of kcat
N354A
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strongly reduced activity, only minor effect on Km for both substrates
R149K
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slightly increased turnover
S86T
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moderate reduction of the catalytic efficiency
D255A
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complete loss of activity
E255A
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almost complete loss of activity
E303A
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10fold decrease in activity
E320A
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26fold higher Km for ATP
F352A
the mutant exhibits a higher turnover number compared to the wild type enzyme
F352L
the mutant exhibits a higher turnover number compared to the wild type enzyme
L401A
the mutant of isoform ChoKalpha1 exhibts a lower turnover number compared to the wild type enzyme
L401F
the mutant of isoform ChoKalpha1 exhibts a lower turnover number compared to the wild type enzyme
N255A
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complete loss of activity
P59A/P60A
site-directed mutagenesis
P61A/P62A
site-directed mutagenesis
P72A/P73A
site-directed mutagenesis
R111A
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2-25% catalytic efficiency compared to the wild type enzyme
S39D/S40D
the choline kinase beta phosphorylation mimic behaves kinetically like the wild type enzyme
S86A
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2-25% catalytic efficiency compared to the wild type enzyme
W387A
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2-25% catalytic efficiency compared to the wild type enzyme
Y197/333F
the mutant shows reduced activity in the presence of epidermal growth factor receptor compared to the wild type enzyme
Y197F
the mutant shows reduced activity in the presence of epidermal growth factor receptor compared to the wild type enzyme
Y333F
the mutant shows reduced activity in the presence of epidermal growth factor receptor compared to the wild type enzyme
S25A
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mutation results in 32% decrease of phosphatidylcholine synthesis compared to the wild type enzyme
S25D
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mutation results in 14% increase of phosphatidylcholine synthesis compared to the wild type enzyme
S30A
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specific activity reduced by 44%, phosphorylation reduced by 70%
S30A/S85A
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specific activity reduced by 60%, phosphorylation reduced by 83%
S85A
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specific activity reduced by 8%, phosphorylation reduced by 17%
S25A
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mutation results in 32% decrease of phosphatidylcholine synthesis compared to the wild type enzyme
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S25D
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mutation results in 14% increase of phosphatidylcholine synthesis compared to the wild type enzyme
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D167A
the mutant shows about 14% activity compared to the wild type enzyme
T29A
the mutant shows about 10% activity compared to the wild type enzyme
T29S
the mutant shows slightly increased activity compared to the wild type enzyme
moe
construction of isozyme mutants cek1-1, cek2-1, and cek3-1, and seedling phenotype of the Arabidopsis thaliana cek1-1, cek2-1, and cek3-1 mutants in response to tunicamycin (Tm)-induced endoplasmic reticulum (ER) stress, overview
moe
construction of isozyme mutants cek1-1, cek2-1, and cek3-1, and seedling phenotype of the Arabidopsis thaliana cek1-1, cek2-1, and cek3-1 mutants in response to tunicamycin (Tm)-induced endoplasmic reticulum (ER) stress,overview
moe
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construction of isozyme mutants cek1-1, cek2-1, and cek3-1, and seedling phenotype of the Arabidopsis thaliana cek1-1, cek2-1, and cek3-1 mutants in response to tunicamycin (Tm)-induced endoplasmic reticulum (ER) stress, overview
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moe
-
construction of isozyme mutants cek1-1, cek2-1, and cek3-1, and seedling phenotype of the Arabidopsis thaliana cek1-1, cek2-1, and cek3-1 mutants in response to tunicamycin (Tm)-induced endoplasmic reticulum (ER) stress,overview
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D255A
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no activity detectable
D255A
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omplete loss of activity
D255E
-
activity almost completely abolished
D255E
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small residual activity
D255N
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no activity detectable
D255N
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small residual activity
D301A
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complete loss of activity
D301A
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no activity detectable
D301E
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complete loss of activity
D301E
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no activity detectable
D301N
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complete loss of activity
D301N
-
no activity detectable
E125A
-
reduced activity
E125A
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modest reduction of kcat and Km for ATP
E125D
-
increased turnover
E125Q
-
reduced activity
E125Q
-
modest reduction of kcat and Km for ATP
E303A
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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
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slightly increased turnover
E320A
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reduction of ATP affinity and time instability
H253A
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reduced activity
H253A
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similar initial activity like wild type enzyme, but time instability
N260A
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activity almost completely abolished, strongly increased Km for Mg2+
N260A
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small residual activity
N308D
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slightly increased turnover
N308D
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modest reduction of kcat
N308Q
-
reduced activity
N308Q
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modest reduction of kcat
N87A
-
reduced activity
N87A
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small reduction of the catalytic efficiency
R111A
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reduced activity
R111A
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4-fold increase in Km for ATP
R149A
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reduced activity
S86A
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strongly reduced activity, increased Km for ATP
S86A
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pronounced reduction of the catalytic efficiency
W387A
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strongly reduced activity, only minor effect on Km for both substrates
W387A
-
strong reduction of kcat (30-fold)
D306A
inactive
D306A
site-directed mutagenesis, inactive mutant of ChoKalpha1
E125A
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2-25% catalytic efficiency compared to the wild type enzyme
E125A
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modest change in kcat/Km with a marked decrease in the affinity for Ca2+ and a significant increase in Km for Mg2+
additional information
comparison of the c-Src binding potential of ChoK as the full-length (FL) enzyme or with the first 49 (DELTA49) or 79 (DELTA79) residues truncated. The FL and DELTA49 variants include the poly-proline region, whereas the DELTA79 variant does not. All constructs extend up to the C-terminal residue, Val457, overview. The c-Src-ChoKalpha1 interaction occurs with the enzymatically dead D306A variant of ChoKalphaDELTA49, indicating that the association is independent of ChoKalpha1 activity. Both the P61A/P62A and the DELTA62 are difficult to purify and less soluble than their FL, DELTA49, or DELTA79 counterparts, as well as the P59A/P60A or P72A/P73A constructs
additional information
-
comparison of the c-Src binding potential of ChoK as the full-length (FL) enzyme or with the first 49 (DELTA49) or 79 (DELTA79) residues truncated. The FL and DELTA49 variants include the poly-proline region, whereas the DELTA79 variant does not. All constructs extend up to the C-terminal residue, Val457, overview. The c-Src-ChoKalpha1 interaction occurs with the enzymatically dead D306A variant of ChoKalphaDELTA49, indicating that the association is independent of ChoKalpha1 activity. Both the P61A/P62A and the DELTA62 are difficult to purify and less soluble than their FL, DELTA49, or DELTA79 counterparts, as well as the P59A/P60A or P72A/P73A constructs
additional information
construction of enzyme N-terminally truncated mutant ChoKalpha1-DELTA79, inhibitor TCD-717 binding structure, overview