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IUBMB CommentsThe prokaryotic cytidine monophosphate kinase specifically phosphorylates CMP (or dCMP), using ATP as the preferred phosphoryl donor. Unlike EC 2.7.4.14, a eukaryotic enzyme that phosphorylates UMP and CMP with similar efficiency, the prokaryotic enzyme phosphorylates UMP with very low rates, and this function is catalysed in prokaryotes by EC 2.7.4.22, UMP kinase. The enzyme phosphorylates dCMP nearly as well as it does CMP .
Synonyms
p25 protein, dcmp kinase, bacterial cytidylate kinase, deoxycytidine monophosphate kinase, sp1603, deoxycytidine monophosphokinase,
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ATP + 2',3'-dideoxy-CMP
ADP + ?
2,3-dideoxy-CMP is a poor substrate
-
-
?
ATP + ara-CMP
ADP + ara-CDP
ATP + dGMP
ADP + dGDP
-
-
-
-
?
dATP + CMP
dADP + CDP
-
-
-
-
?
additional information
?
-
ATP + CMP
ADP + CDP
-
-
-
?
ATP + CMP
ADP + CDP
-
-
-
r
ATP + dCMP
ADP + dCDP
-
-
-
?
ATP + dCMP
ADP + dCDP
-
-
-
r
ATP + UMP
ADP + UDP
-
-
-
?
ATP + UMP
ADP + UDP
UMP is a poor substrate
-
-
r
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
-
-
-
?
ATP + dCMP
ADP + dCDP
-
-
-
-
?
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 + UMP
ADP + UDP
-
-
-
-
?
ATP + UMP
ADP + UDP
-
0.8% of the activity with CMP
-
-
?
ATP + UMP
ADP + UDP
bacterial CMP kinases phosphorylate UMP with very low rates
-
-
?
GTP + CMP
GDP + CDP
-
-
-
-
?
GTP + CMP
GDP + CDP
-
poor substrate
-
-
?
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
-
-
?
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0.15 - 0.65
2',3'-dideoxy-CMP
0.038
ATP
-
pH 7.4, reaction with CMP
0.087
dATP
-
pH 7.4, reaction with CMP
0.094
dGMP
-
reaction with ATP
0.64
GTP
-
reaction with CMP
additional information
additional information
kinetics and substrate specificities of wild-type and mutant enzymes, overview
-
0.035
CMP
wild-type enzyme
0.055
dCMP
D132H mutant
0.094
dCMP
wild-type enzyme
0.93
UMP
wild-type enzyme
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
0.47
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
0.035
CMP
-
pH 7.4, 30°C
0.035
CMP
-
reaction with ATP
0.035
CMP
wild type enzyme, at 30°C and pH 7.4
0.08
CMP
mutant enzyme S101A, at 30°C and pH 7.4
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
0.094
dCMP
-
pH 7.4, 30°C
0.094
dCMP
wild type enzyme, at 30°C and pH 7.4
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
0.93
UMP
-
pH 7.4, 30°C
0.93
UMP
-
reaction with ATP
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108
dCMP
wild-type enzyme
0.82
UMP
wild-type enzyme
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
0.08
CMP
mutant enzyme S101A, at 30°C and pH 7.4
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
103
CMP
wild type enzyme, at 30°C and pH 7.4
0.071
dCMP
mutant enzyme D185A, at 30°C and pH 7.4
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
109
dCMP
wild type enzyme, at 30°C and pH 7.4
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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
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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Li de La Sierra, I.M.; Gallay, J.; Vincent, M.; Bertrand, T.; Briozzo, P.; Barzu, O.; Gilles, A.M.
Substrate-induced fit of the ATP binding site of cytidine monophosphate kinase from Escherichia coli: time-resolved fluorescence of 3'-anthraniloyl-2'-deoxy-ADP and molecular modeling
Biochemistry
39
15870-15878
2000
Escherichia coli (P0A6I0)
brenda
Bucurenci, N.; Sakamoto, H.; Briozzo, P.; Palibroda, N.; Serina, L.; Sarfati, R.S.; Labesse, G.; Briand, G.; Danchin, A.; Barzu, O.; Gilles, A.M.
CMP kinase from Escherichia coli is structurally related to other nucleoside monophosphate kinases
J. Biol. Chem.
271
2856-2862
1996
Escherichia coli, Escherichia coli K-12 (P0A6I0)
brenda
Schultz, C.P.; Ylisastigui-Pons, L.; Serina, L.; Sakamoto, H.; Mantsch, H.H.; Neuhard, J.; Barzu, O.; Gilles, A.M.
Structural and catalytic properties of CMP kinase from Bacillus subtilis: a comparative analysis with the homologous enzyme from Escherichia coli
Arch. Biochem. Biophys.
340
144-153
1997
Bacillus subtilis, Escherichia coli
brenda
Briozzo, P.; Golinelli-Pimpaneau, B.; Gilles, A.M.; Gaucher, J.F.; Burlacu-Miron, S.; Sakamoto, H.; Janin, J.; Barzu, O.
Structures of Escherichia coli CMP kinase alone and in complex with CDP: a new fold of the nucleoside monophosphate binding domain and insights into cytosine nucleotide specificity
Structure
6
1517-1527
1998
Escherichia coli
brenda
Lee, S.; Kim, B.
Recombinant Escherichia coli-catalyzed production of cytidine 5-triphosphate from cytidine 5-monophosphate
J. Ind. Eng. Chem.
12
757-761
2006
Escherichia coli (P0A6I0)
-
brenda
Alexandre, J.A.; Roy, B.; Topalis, D.; Pochet, S.; Perigaud, C.; Deville-Bonne, D.
Enantioselectivity of human AMP, dTMP and UMP-CMP kinases
Nucleic Acids Res.
35
4895-4904
2007
Escherichia coli (P0A6I0)
brenda
Ofiteru, A.; Bucurenci, N.; Alexov, E.; Bertrand, T.; Briozzo, P.; Munier-Lehmann, H.; Gilles, A.M.
Structural and functional consequences of single amino acid substitutions in the pyrimidine base binding pocket of Escherichia coli CMP kinase
FEBS J.
274
3363-3373
2007
Escherichia coli (P0A6I0), Escherichia coli K-12 (P0A6I0)
brenda
Bertrand, T.; Briozzo, P.; Assairi, L.; Ofiteru, A.; Bucurenci, N.; Munier-Lehmann, H.; Golinelli-Pimpaneau, B.; Barzu, O.; Gilles, A.M.
Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme
J. Mol. Biol.
315
1099-1110
2002
Escherichia coli (A0A140N8S7)
brenda