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
-
2.7.4.25
-
beet
-
bnyvv
-
rhizomania
-
resistance-breaking
-
roscovitine
-
polymyxa
-
2.7.4.14
-
tetragonia
-
expansa
-
biotechnology
- 2.7.4.25
- beet
- bnyvv
-
rhizomania
-
resistance-breaking
- roscovitine
-
polymyxa
-
2.7.4.14
-
tetragonia
- expansa
- biotechnology
Reaction
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
Advanced search results
Engineering
Engineering on EC 2.7.4.25 - (d)CMP kinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
S36A
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
the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP
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
the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP
D132S
the substitution results in a moderate decrease in stability without significant changes in Km value for CMP and dCMP
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
replacement of Arg188 with Met does not affect enzyme stability but dramatically decreases the kcat/Km ratio compared to the wild-type enzyme
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