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ATP + 1-beta-D-arabinofuranosylcytosine 5'-phosphate
ADP + 1-beta-D-arabinofuranosylcytosine 5'-diphosphate
-
-
-
?
ATP + 2',3'-dideoxy-CMP
ADP + ?
2,3-dideoxy-CMP is a poor substrate
-
-
?
ATP + 2-thiouridine 5'-monophosphate
ADP + 2-thiouridine 5'-diphosphate
2-thiouridine 5'-monophosphate is a poor substrate
-
-
?
ATP + ara-CMP
ADP + ara-CDP
ATP + dGMP
ADP + dGDP
-
-
-
-
?
ATP + dUMP
ADP + dUDP
dUMP is a poor substrate
-
-
?
ATP + GTP
ADP + GDP
-
GTP is a poor substrate with Bacillus subtilis CMP kinase
-
-
?
CTP + CMP
CDP + CDP
the activity with CTP is still measurable but less than 0.05% of that with ATP
-
-
?
dCTP + CMP
dCDP + CDP
the activity with dCTP is still measurable but less than 0.05% of that with ATP
-
-
?
dUTP + CMP
dUDP + CDP
the activity with dUTP is still measurable but less than 0.05% of that with ATP
-
-
?
ITP + CMP
IDP + CDP
ITP is a poor substrate
-
-
?
UTP + CMP
UDP + CDP
the activity with UTP is still measurable but less than 0.05% of that with ATP
-
-
?
additional information
?
-
ATP + ara-CMP
ADP + ara-CDP
-
ara-CMP is phosphorylated at rate which represents 14% of that with CMP
-
-
?
ATP + ara-CMP
ADP + ara-CDP
-
-
-
-
?
ATP + ara-CMP
ADP + ara-CDP
ara-CMP is a poor substrate
-
-
?
ATP + CMP
ADP + CDP
-
-
-
-
?
ATP + CMP
ADP + CDP
-
CMP and dCMP are the best phosphate acceptors
-
-
?
ATP + CMP
ADP + CDP
-
-
-
-
?
ATP + CMP
ADP + CDP
-
-
-
?
ATP + CMP
ADP + CDP
-
-
-
r
ATP + CMP
ADP + CDP
-
-
-
?
ATP + CMP
ADP + CDP
-
-
-
?
ATP + CMP
ADP + CDP
the enzyme is specific for CMP
-
-
?
ATP + CMP
ADP + CDP
-
-
-
?
ATP + CMP
ADP + CDP
-
the enzyme preferentially phosphorylates CMP and dCMP
-
-
?
ATP + CMP
ADP + CDP
-
the enzyme preferentially phosphorylates CMP and dCMP
-
-
?
ATP + CMP
ADP + CDP
-
-
-
?
ATP + CMP
ADP + CDP
-
-
-
-
?
ATP + CMP
ADP + CDP
-
effective conversion
-
-
?
ATP + CMP
ADP + CDP
-
cytidylate kinase, UTP, CTP and GTP also possible phosphate donors, no product with CDP as substrate
-
-
?
ATP + dCMP
ADP + dCDP
-
CMP and dCMP are the best phosphate acceptors
-
-
?
ATP + dCMP
ADP + dCDP
-
-
-
-
?
ATP + dCMP
ADP + dCDP
-
-
-
?
ATP + dCMP
ADP + dCDP
-
-
-
r
ATP + dCMP
ADP + dCDP
-
105% of the activity with CMP
-
-
?
ATP + dCMP
ADP + dCDP
Escherichia coli CMPK phosphorylates dCMP nearly as well as it does CMP
-
-
?
ATP + dCMP
ADP + dCDP
-
-
-
?
ATP + dCMP
ADP + dCDP
the enzyme is specific for dCMP
-
-
?
ATP + dCMP
ADP + dCDP
-
-
-
?
ATP + dCMP
ADP + dCDP
-
the enzyme preferentially phosphorylates CMP and dCMP
-
-
?
ATP + dCMP
ADP + dCDP
-
the enzyme preferentially phosphorylates CMP and dCMP
-
-
?
ATP + dCMP
ADP + dCDP
-
-
-
-
?
ATP + dCMP
ADP + dCDP
-
cytidylate kinase
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
?
ATP + UMP
ADP + UDP
-
UMP is phosphorylated at rate which represents 10% of that with CMP
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
-
0.8% of the activity with CMP
-
-
?
ATP + UMP
ADP + UDP
UMP is a poor substrate
-
-
r
ATP + UMP
ADP + UDP
bacterial CMP kinases phosphorylate UMP with very low rates
-
-
?
ATP + UMP
ADP + UDP
UMP is a poor substrate
-
-
?
ATP + UMP
ADP + UDP
CMP kinase possess a weak UMP kinase activity
-
-
?
ATP + UMP
ADP + UDP
UMP is a weak substrate
-
-
?
ATP + UMP
ADP + UDP
-
UMP is a poor substrate
-
-
?
ATP + UMP
ADP + UDP
-
UMP is a poor substrate
-
-
?
dATP + CMP
dADP + CDP
-
-
-
-
?
dATP + CMP
dADP + CDP
-
-
-
?
GTP + CMP
GDP + CDP
-
ATP is equally effective as ATP
-
-
?
GTP + CMP
GDP + CDP
-
-
-
-
?
GTP + CMP
GDP + CDP
-
poor substrate
-
-
?
GTP + CMP
GDP + CDP
-
-
-
?
additional information
?
-
ATP-mediated induced-fit of LID in CMPKcoli modulated by CMP leading to a closed conformation of the active site, protected from water
-
-
?
additional information
?
-
bacterial CMP kinases are specific for CMP and dCMP, whereas the related eukaryotic NMP kinase phosphorylates CMP and UMP with similar efficiency. Bacterial CMP kinase has a narrower NMP-binding pocket and a hydrogen-bonding network involving the pyrimidine moiety specific for the cytosine nucleobase compared to eukaryotic UMP?CMP kinases
-
-
?
additional information
?
-
four key amino acids interacting with the pyrimidine ring of CMP, Ser36, Asp132, Arg110 and Arg188, contribute to the stability, catalysis and substrate specificity of Escherichia coli CMP kinase. D132 is involved in a complicated network of interactions, the strongest being with R110, and also R110 is involved in many interactions, but mainly with D132. Substrate specificities of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
TMP, Ant-dCMP, 5-methyl-CMP, AMP, dAMP, GMP, and dGMP are no substrates
-
-
?
additional information
?
-
-
modelling of CMPK in apo form and in complex with cytidine 5'-monophosphate, structure analysis, overview
-
-
?
additional information
?
-
modelling of CMPK in apo form and in complex with cytidine 5'-monophosphate, structure analysis, overview
-
-
?
additional information
?
-
modelling of CMPK in apo form and in complex with cytidine 5'-monophosphate, structure analysis, overview
-
-
?
additional information
?
-
-
modelling of CMPK in apo form and in complex with cytidine 5'-monophosphate, structure analysis, overview
-
-
?
additional information
?
-
-
CMP kinase from Salmonella typhimurium does not act on UMP
-
-
?
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0.36
1-beta-D-arabinofuranosylcytosine 5'-phosphate
in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.15 - 0.65
2',3'-dideoxy-CMP
0.094
dGMP
-
reaction with ATP
1.46
dUMP
in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.87
ITP
in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
additional information
additional information
kinetics and substrate specificities of wild-type and mutant enzymes, overview
-
0.15
2',3'-dideoxy-CMP
mutant enzyme D185A, at 30°C and pH 7.4
0.46
2',3'-dideoxy-CMP
wild type enzyme, at 30°C and pH 7.4
0.54
2',3'-dideoxy-CMP
mutant enzyme R181M, at 30°C and pH 7.4
0.65
2',3'-dideoxy-CMP
mutant enzyme S101A, at 30°C and pH 7.4
0.37
ara-CMP
-
at 30°C in 50mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1mM phosphoenolpyruvate, 0.2 mM NADH
0.47
ara-CMP
mutant enzyme S101A, at 30°C and pH 7.4
0.53
ara-CMP
wild type enzyme, at 30°C and pH 7.4
0.79
ara-CMP
mutant enzyme R181M, at 30°C and pH 7.4
1
ara-CMP
mutant enzyme D185A, at 30°C and pH 7.4
0.36
araCMP
-
pH 7.4, 30°C
0.36
araCMP
-
reaction with ATP
0.37
araCMP
-
pH 7.4, 30°C
0.038
ATP
-
pH 7.4, reaction with CMP
0.038
ATP
in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.12
ATP
-
at 30°C in 50mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1mM phosphoenolpyruvate, 0.2 mM NADH
0.035
CMP
wild-type enzyme
0.035
CMP
-
reaction with ATP
0.035
CMP
in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.035
CMP
wild type enzyme, at 30°C and pH 7.4
0.035
CMP
wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.038
CMP
mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.04
CMP
-
at 30°C in 50mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1mM phosphoenolpyruvate, 0.2 mM NADH
0.08
CMP
mutant enzyme S101A, at 30°C and pH 7.4
0.12
CMP
-
pH and temperature not specified in the publication
0.19
CMP
mutant enzyme R181M, at 30°C and pH 7.4
0.47
CMP
mutant enzyme D185A, at 30°C and pH 7.4
1
CMP
mutant enzyme R188M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
1.3
CMP
mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
2.5
CMP
mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
2.6
CMP
mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
2.9
CMP
mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
20.2
CMP
mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.087
dATP
-
pH 7.4, reaction with CMP
0.087
dATP
in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.0394
dCMP
wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.055
dCMP
mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.08
dCMP
mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.09
dCMP
mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.094
dCMP
wild-type enzyme
0.094
dCMP
-
pH 7.4, 30°C
0.094
dCMP
in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.094
dCMP
wild type enzyme, at 30°C and pH 7.4
0.165
dCMP
-
pH and temperature not specified in the publication
0.19
dCMP
mutant enzyme S101A, at 30°C and pH 7.4
0.24
dCMP
mutant enzyme D185A, at 30°C and pH 7.4
0.24
dCMP
mutant enzyme R181M, at 30°C and pH 7.4
0.33
dCMP
-
at 30°C in 50mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1mM phosphoenolpyruvate, 0.2 mM NADH
0.77
dCMP
mutant enzyme R188M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
1.8
dCMP
mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
3.5
dCMP
mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
7.3
dCMP
mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.64
GTP
-
reaction with CMP
0.64
GTP
in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.93
UMP
wild-type enzyme
0.93
UMP
-
reaction with ATP
0.93
UMP
in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.93
UMP
wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
1.9
UMP
mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
3.6
UMP
-
at 30°C in 50mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1mM phosphoenolpyruvate, 0.2 mM NADH
3.9
UMP
mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
5.4
UMP
mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
7.9
UMP
mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
8
UMP
mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
11.3
UMP
mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
13.85
UMP
-
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0083 - 0.65
2',3'-dideoxy-CMP
0.0083
2',3'-dideoxy-CMP
mutant enzyme D185A, at 30°C and pH 7.4
0.047
2',3'-dideoxy-CMP
wild type enzyme, at 30°C and pH 7.4
0.12
2',3'-dideoxy-CMP
mutant enzyme R181M, at 30°C and pH 7.4
0.65
2',3'-dideoxy-CMP
mutant enzyme S101A, at 30°C and pH 7.4
0.085
ara-CMP
mutant enzyme D185A, at 30°C and pH 7.4
0.47
ara-CMP
mutant enzyme S101A, at 30°C and pH 7.4
1.36
ara-CMP
mutant enzyme R181M, at 30°C and pH 7.4
56
ara-CMP
wild type enzyme, at 30°C and pH 7.4
0.069
CMP
mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.08
CMP
mutant enzyme S101A, at 30°C and pH 7.4
0.12
CMP
mutant enzyme R188M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.23
CMP
mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.26
CMP
mutant enzyme D185A, at 30°C and pH 7.4
1.38
CMP
mutant enzyme R181M, at 30°C and pH 7.4
1.4
CMP
mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
4.1
CMP
mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
22.4
CMP
mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
52
CMP
-
pH and temperature not specified in the publication
63
CMP
mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
103
CMP
wild type enzyme, at 30°C and pH 7.4
103
CMP
wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.04
dCMP
mutant enzyme R188M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.05
dCMP
mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.06
dCMP
mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.071
dCMP
mutant enzyme D185A, at 30°C and pH 7.4
0.15
dCMP
mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.19
dCMP
mutant enzyme S101A, at 30°C and pH 7.4
0.45
dCMP
mutant enzyme R181M, at 30°C and pH 7.4
0.73
dCMP
mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
14.5
dCMP
mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
21.1
dCMP
mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
30
dCMP
-
pH and temperature not specified in the publication
108
dCMP
wild-type enzyme
108
dCMP
wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
109
dCMP
wild type enzyme, at 30°C and pH 7.4
0.013
UMP
mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.054
UMP
mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.45
UMP
mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.57
UMP
mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.82
UMP
wild-type enzyme
0.82
UMP
wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
8.3
UMP
mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
9.9
UMP
mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
12.2
UMP
-
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.083
ara-CMP
-
mutant enzyme D185A, at 30°C and pH 7.4
1.7
ara-CMP
-
mutant enzyme R181M, at 30°C and pH 7.4
7.5
ara-CMP
-
mutant enzyme S101A, at 30°C and pH 7.4
105
ara-CMP
-
wild type enzyme, at 30°C and pH 7.4
0.0114
CMP
mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.053
CMP
mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.12
CMP
mutant enzyme R188M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.54
CMP
mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.54
CMP
-
mutant enzyme D185A, at 30°C and pH 7.4
1.41
CMP
mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
7.4
CMP
-
mutant enzyme R181M, at 30°C and pH 7.4
25.2
CMP
mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
589
CMP
mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
697
CMP
-
mutant enzyme S101A, at 30°C and pH 7.4
1100
CMP
-
pH and temperature not specified in the publication
2940
CMP
-
wild type enzyme, at 30°C and pH 7.4
2940
CMP
wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.0068
dCMP
mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.052
dCMP
mutant enzyme R188M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.3
dCMP
-
mutant enzyme D185A, at 30°C and pH 7.4
0.4
dCMP
mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
1.1
dCMP
mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
1.88
dCMP
mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
1.9
dCMP
-
mutant enzyme R181M, at 30°C and pH 7.4
4.1
dCMP
mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
6.1
dCMP
-
mutant enzyme S101A, at 30°C and pH 7.4
200
dCMP
-
pH and temperature not specified in the publication
230
dCMP
mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
1150
dCMP
wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
1160
dCMP
-
wild type enzyme, at 30°C and pH 7.4
0.0033
UMP
mutant enzyme D132H, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.0048
UMP
mutant enzyme R110M, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.083
UMP
mutant enzyme D132N, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.3
UMP
mutant enzyme S36A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
0.88
UMP
-
pH and temperature not specified in the publication
0.88
UMP
wild type enzyme, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
1.04
UMP
mutant enzyme D132S, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
1.25
UMP
mutant enzyme D132A, in 50 mM Tris-HCl (pH 7.4), 50 mM KCl, 2 mM MgCl2, 1 mM phosphoenolpyruvate, 0.2 mM NADH, at 30°C
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D185A
the mutant shows severely decreased CMP and dCMP phosphoryation activity compared to the wild type enzyme
R181M
the mutant shows severely decreased CMP and dCMP phosphoryation activity compared to the wild type enzyme
S101A
the mutation reduces CMP phosphorylation only moderately, but dramatically reduces dCMP phosphorylation
D132A
the mutant shows reduced activity compared to the wild type enzyme, the mutation has the most dramatic consequences on the protein stability as Tm decreases by 9°C in comparison with the wild type protein, an increase in the specificity of the D132A variant for UMP over CMP and dCMP is observed
D132H
the mutant shows reduced activity compared to the wild type enzyme
D132N
the mutant shows reduced activity compared to the wild type enzyme
D132S
the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP
R110M
the mutant shows reduced activity compared to the wild type enzyme
R188M
the mutation does not affect enzyme stability but dramatically decreases the kcat_Km ratio compared with wild type enzyme, the mutant has no activity towards UMP
S36A
the S36A substitution mainly changes the Km value for the two natural substrates, which increases by a factor of 70 (CMP) and 37 (dCMP) compared with the parent molecule and decreases kcat of 1.6fold (CMP) and 7.4fold (dCMP) with respect to the wild type enzyme
V164E
substitution of Val164 by a Glu residue apparently does not affect the catalytic properties of Escherichia coli CMP kinase
D132A
site directed mutagenesis
D132A
the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP
D132H
site directed mutagenesis
D132H
the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP, the D132H variant does not introduce charge reversal, because His is calculated to be deprotonated
D132N
site directed mutagenesis
D132N
the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP
D132S
site directed mutagenesis
D132S
the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP
R110M
site directed mutagenesis
R110M
the side chains of Arg110 cannot establish hydrogen bonds with UMP, and its substitution by hydrophobic amino acids simultaneously affects the Km of CMP/dCMP and the kcat value
R188M
site directed mutagenesis
R188M
replacement of Arg188 with Met does not affect enzyme stability but dramatically decreases the kcat/Km ratio compared to the wild-type enzyme
S36A
site directed mutagenesis
S36A
the side chains of Arg110 cannot establish hydrogen bonds with UMP, and its substitution by hydrophobic amino acids simultaneously affects the Km of CMP/dCMP and the kcat value
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