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2.7.4.25: (d)CMP kinase

This is an abbreviated version!
For detailed information about (d)CMP kinase, go to the full flat file.

Word Map on EC 2.7.4.25

Reaction

ATP
+
(d)CMP
=
ADP
+
(d)CDP

Synonyms

ATP:CMP phosphotransferase, bacterial cytidylate kinase, CMK, CMP kinase, CMPK, cytidine 5’-monophosphate kinase, cytidine monophosphate kinase, cytidylate kinase, dCMP kinase, deoxycytidine monophosphate kinase, deoxycytidine monophosphokinase, deoxycytidylate kinase, More, P25 protein, prokaryotic cytidylate kinase, SP1603, UCK, UMP-CMP kinase

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.4 Phosphotransferases with a phosphate group as acceptor
                2.7.4.25 (d)CMP kinase

Engineering

Engineering on EC 2.7.4.25 - (d)CMP kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D132A
D132H
D132N
D132S
D185A
the mutant shows severely decreased CMP and dCMP phosphoryation activity compared to the wild type enzyme
R110M
R181M
the mutant shows severely decreased CMP and dCMP phosphoryation activity compared to the wild type enzyme
R188M
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