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Literature summary for 2.7.4.25 extracted from

  • 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 (1997), Arch. Biochem. Biophys., 340, 144-153.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.035
-
CMP pH 7.4, 30°C Escherichia coli
0.04
-
CMP pH 7.4, 30°C Bacillus subtilis
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 Bacillus subtilis
0.094
-
dCMP pH 7.4, 30°C Escherichia coli
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 Bacillus subtilis
0.33
-
dCMP pH 7.4, 30°C Bacillus subtilis
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 Bacillus subtilis
0.36
-
araCMP pH 7.4, 30°C Escherichia coli
0.37
-
araCMP pH 7.4, 30°C Bacillus subtilis
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 Bacillus subtilis
0.93
-
UMP pH 7.4, 30°C Escherichia coli
3.6
-
UMP pH 7.4, 30°C Bacillus subtilis
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 Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + ara-CMP
-
Escherichia coli ADP + ara-CDP
-
?
ATP + ara-CMP ara-CMP is phosphorylated at rate which represents 14% of that with CMP Bacillus subtilis ADP + ara-CDP
-
?
ATP + CMP
-
Bacillus subtilis ADP + CDP
-
?
ATP + CMP
-
Escherichia coli ADP + CDP
-
?
ATP + CMP CMP and dCMP are the best phosphate acceptors Bacillus subtilis ADP + CDP
-
?
ATP + dCMP
-
Escherichia coli ADP + dCDP
-
?
ATP + dCMP CMP and dCMP are the best phosphate acceptors Bacillus subtilis ADP + dCDP
-
?
ATP + GTP GTP is a poor substrate with Bacillus subtilis CMP kinase Bacillus subtilis ADP + GDP
-
?
ATP + UMP
-
Bacillus subtilis ADP + UDP
-
?
ATP + UMP
-
Escherichia coli ADP + UDP
-
?
ATP + UMP UMP is phosphorylated at rate which represents 10% of that with CMP Bacillus subtilis ADP + UDP
-
?
dATP + CMP
-
Escherichia coli dADP + CDP
-
?
GTP + CMP poor substrate Escherichia coli GDP + CDP
-
?
GTP + CMP ATP is equally effective as ATP Bacillus subtilis GDP + CDP
-
?

Synonyms

Synonyms Comment Organism
CMP kinase
-
Bacillus subtilis
deoxycytidine monophosphate kinase
-
Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
48
-
midpoint denaturation temperature in absence of nucleotide substrates or in presence of ATP Escherichia coli
48.5 57.8 the melting temperature of CMP kinae in the absence of nucleotide substrates is at 48.5°C, the melting temperature of CMP kinae in the presence of ATP is at 57.8°C, the melting temperature of CMP kinae in the presence of CMP is at 50.5°C Bacillus subtilis
49
-
midpoint denaturation temperature in presence of CMP Escherichia coli
49
-
midpoint denaturation temperature in absence of nucleotide substrates Bacillus subtilis
51
-
midpoint denaturation temperature in presence of CMP Bacillus subtilis
58
-
midpoint denaturation temperature in presence of ATP Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
ATP
-
Bacillus subtilis