dNTP modified at triphosphate residues: substrate properties towards DNA polymerases and stability in human serum.
Substrate and terminating substrate properties of dNTP with phosphate groups replaced by phosphonates at alpha-, gamma-, beta, gamma-, and alpha, beta, gamma-positions towards different human DNA polymerases and retroviral reverse transcriptases are reviewed. Substitution of the phosphate group by the phosphonate at any of the three phosphate positions of dNTP increased their stability towards dephosphorylating enzymes of human blood. In some cases hydrophobicity of these compounds was markedly enhanced.
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia. AAK@imb.imb.ac.ru
A
A
Krayevsky
A
A
Arzumanov
E
E
Shirokova
N
N
Dyatkina
L
L
Victorova
M
M
Jasko
L
L
Alexandrova
D017766:Acid Anhydride Hydrolases / Q000097:blood; D001798:Blood Proteins / Q000378:metabolism; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D003854:Deoxyribonucleotides / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D015394:Molecular Structure; D043583:Nucleoside-Triphosphatase; D063065:Organophosphonates / Q000737:chemistry*; D012194:RNA-Directed DNA Polymerase; D013379:Substrate Specificity; D013942:Thymine Nucleotides; D014780:Viruses / Q000201:enzymology
D001798:Blood Proteins; D003854:Deoxyribonucleotides; D063065:Organophosphonates; D013942:Thymine Nucleotides; D012194:RNA-Directed DNA Polymerase; D004259:DNA-Directed DNA Polymerase; D017766:Acid Anhydride Hydrolases; D043583:Nucleoside-Triphosphatase