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2.7.4.14: UMP/CMP kinase

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

Word Map on EC 2.7.4.14

Reaction

ATP
+
UMP
=
ADP
+
UDP

Synonyms

ATP:UMP-CMP phosphotransferase, CMP kinase, CMP/UMP kinase, CMPK, CMPK1, CMPK2, CTP:CMP phosphotransferase, cytidine monophosphate kinase, cytidine/uridine monophosphate kinase 2, cytidylate kinase, dCK, deoxycytidine kinase, EC 2.7.4.5, kinase, cytidylate (phosphorylating), More, MssA protein, nucleoside monophosphate kinase, P25, pyrimidine nucleoside monophosphate kinase, UCK, UMP-CMP kinase, UMP-CMP kinase 2, UMP-CMPK2, UMP/CMP kinase, UMP/CMP kinase 1, UMP/CMPK1, UMPK, uridine monophosphate/cytidine monophosphate kinase

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.4 Phosphotransferases with a phosphate group as acceptor
                2.7.4.14 UMP/CMP kinase

Engineering

Engineering on EC 2.7.4.14 - UMP/CMP kinase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G21A
-
mutant enzyme is degraded during the purification phase
G22A
-
mutant enzyme with decreased turnover-number/KmATP value. Turnover-number is 59% of that of the wild-type enzyme
G24A
-
mutant enzyme with decreased turnover-number/KmATP value. Turnover-number is 48% of that of the wild-type enzyme
G26A
-
mutant enzyme with decreased turnover-number/KmATP value
G27R
-
mutant enzyme is degraded during the purification phase. Turnover-number is 45% of that of the wild-type enzyme
K27E
-
mutant enzyme with 2600fold decreased turnover-number/KmATP value. Turnover-number is 21% of that of the wild-type enzyme
K27M
-
mutant enzyme with 1000fold decreased turnover-number/KmATP value. Turnover-number is 22% of that of the wild-type enzyme
E448G
site-directed mutagenesis
P64T
naturally occuring mutation, involved in alterations of cidofovir metabolism and resistance against cidofovir in cervical tumour cell lines, thermoresistant mutant compared to the wild-type enzyme. The P64T substitution may modify the distance between Ile62, Val63 and CMP, and therefore reduce the intensity or abolish the interactions observed in the wild-type UMP/CMPK1 at this position
R134M
naturally occuring mutation, involved in alterations of cidofovir metabolism and resistance against cidofovir in cervical tumour cell lines, thermosensitive similar to the wild-type enzyme. The typical interactions established between an arginine to bridge the phosphate of ATP and CMP for the enzymatic reaction are abolished in the presence of Met134
additional information