EC Number   |
Protein Variants |
Reference |
|---|
    2.7.4.14 | more |
enzyme knockdown in MCF-7 cells using a CMPK shRNA lentivirus |
737991 |
| 2.7.4.14 | more |
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 | more |
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 |
