Recombinant Human CMPK1 was expressed in E. coli.
UMP-CMP kinase plays a critical role in supplying cells with nucleotides by catalysing the phosphorylation of CMP, UMP and dCMP to their respective diphosphates. CMK plays also an important role in the activation of cytidine analogues, aracytidine and gemcitabine, a mainstay of leukaemia and lymphoma therapy. CMK has a remarkable ability of to phosphorylate L-nucleotides from their monophosphate to diphosphate forms as shown for β-L-2’3’-dideoxy-3’thiacytidine (L-SSdC, 3-TC or lamividune), an anti-HIV and anti-hepatitis B drug.
150mM KCl, 50mM Tris-Hcl, pH7,5, 2mM β-mercaptoethanol, 50% glycerol.
≥1 unit/mg protein.
One unit of UMP-CMP kinase converts 1.0 µmole of UMP and ATP to UDP and ADP per minute at pH 7.6 at 25 centigrade, using a coupled enzyme system with PK/LDH.
CMK enzyme is a highly pure and active cloned human UMP-CMP Kinase which can be used:• to characterize a monophosphorylated nucleotide analogue as a potential substrate of CMK• to quantify UMP, CMP, dUMP or dCMP in a sample• to synthesize enzymatically the di-phosphate form of nucleotide analogue from its monophosphate form (e.g. dFdC-DP)
Store at–20 centigrade