2.7.4.14	E448G	site-directed mutagenesis	693063	
2.7.4.14	G21A	mutant enzyme is degraded during the purification phase	645158	
2.7.4.14	G22A	mutant enzyme with decreased turnover-number/KmATP value. Turnover-number is 59% of that of the wild-type enzyme	645158	
2.7.4.14	G24A	mutant enzyme with decreased turnover-number/KmATP value. Turnover-number is 48% of that of the wild-type enzyme	645158	
2.7.4.14	G26A	mutant enzyme with decreased turnover-number/KmATP value	645158	
2.7.4.14	G27R	mutant enzyme is degraded during the purification phase. Turnover-number is 45% of that of the wild-type enzyme	645158	
2.7.4.14	K27E	mutant enzyme with 2600fold decreased turnover-number/KmATP value. Turnover-number is 21% of that of the wild-type enzyme	645158	
2.7.4.14	K27M	mutant enzyme with 1000fold decreased turnover-number/KmATP value. Turnover-number is 22% of that of the wild-type enzyme	645158	
2.7.4.14	additional information	construction of a UMP-CMPK2DELTA21 mutant lacking the mitochondrial targeting sequence	693063	
2.7.4.14	additional information	determination and analysis of 28 polymorphisms in DCK/CMPK enzymes, genotyping with humans of different ethnic origins, overview. Variant allozyme enzyme activities range from 32 to 105% of the wild-type enzyme for DCK and from 78 to 112% of wild-type enzyme for CMPK, with no significant differences in apparent Km values for either enzyme except for a DCK Val24/Ser122 double variant allozyme, overview	692040	
2.7.4.14	additional information	enzyme knockdown in MCF-7 cells using a CMPK shRNA lentivirus	737991	
2.7.4.14	additional information	modeling studies of the P64T and R134M amino acid changes, structure-function relationship analysis of mutant UMP/CMPK1s, effect of the two mutations on the stability of the UMP/CMPK1 protein is assessed by circular dichroism, overview	739215	
2.7.4.14	additional information	two types of chimeric enzymes have been constructed by genetic engineering of chicken cytosolic adenylate kinase and porcine brain UMP/CMP kinase. One designated as UAU carries an AMP-binding domain of AK in the remaining body of UMP/CMP kinase, and the other, designated as AUA, carries a UMP/CMP-binding domain in the remaining body of adenylate kinase. UAU is 4fold more active with AMP, 40fold less active with UMP, and 4fold less active with CMP than the parental UMP/CMP kinase, although AUA has considerably lowered reactivity for both AMP and UMP. AUA has a Tm-value 11°C lower than adenylate kinase, whereas UAU has a Tm-value similar to that of UMP/CMP kinase. Expression in Escherichia coli JM109	645157	
2.7.4.14	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	739215	
2.7.4.14	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	739215