[Substrate specificity of T5 bacteriophage deoxyribonucleoside monophosphate kinase and its application for the synthesis of [alpha-(32)P]d/rNTP].
Bacteriophage T5 deoxynucleoside monophosphate kinase (dNMP kinase, EC 2.7.4.13) is shown to catalyze the phosphorylation of both d(2)CMP and ribonucleotides AMP, GMP, and CMP, but does not phosphorylate UMP. For natural acceptors of the phosphoryl group, K(m) and k(cat) were found. The applicability of T5 dNMP kinase as a universal enzyme capable of the phosphorylation of labelled r/dNMP was shown for the synthesis of [alpha-(32)P]rNTP and [alpha-(32)P]dNTP.
Skoblov
A Iu
AIu
Mikulinskaia
G V
GV
Taran
S A
SA
Miroshnikov
A I
AI
Feofanov
S A
SA
Skoblov
Iu S
IuS
D007553:Isotope Labeling / Q000379:methods; D009711:Nucleotides / Q000737:chemistry*; D010759:Phosphorus Isotopes / Q000737:chemistry; D017856:Phosphotransferases (Phosphate Group Acceptor) / Q000737:chemistry*; D017906:Siphoviridae / Q000201:enzymology*; D013379:Substrate Specificity; D014764:Viral Proteins / Q000737:chemistry*
D009711:Nucleotides; D010759:Phosphorus Isotopes; D014764:Viral Proteins; D017856:Phosphotransferases (Phosphate Group Acceptor); C020015:(deoxy)nucleoside-phosphate kinase