Selectivity of DNA polymerases toward α and β nucleotide substrates of d and l series

FEBS Letters

von Janta-Lipinski, Martin¹  Semizarov, Dmitry G.²  Krayevsky, Alexander A.²  Victorova, Lyubov S.²  Dyatkina, Natalia B.² 

[1] Max-Delbrück Centre of Molecular Medicine, Berlin D-13125, Germany;Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilov Str., Moscow 117984, Russian Federation

关键词: Reverse transcriptase;    Terminal deoxynucleotidyl transferase;    Modified nucleoside 5′-triphosphate;    Stereomer;    RT;    reverse transcriptase;    HIV;    human immunodeficiency virus;    AMV;    avian myeloblastosis virus;    TdT;    terminal deoxynucleotidyl transferase;    dNTP;    2′-deoxynucleoside 5′-triphosphate;    d2NTP;    2′;    3′-dideoxynucleoside 5′-triphosphate;   

DOI  :  10.1016/0014-5793(94)01123-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The substrate properties of four carbocyclic d and l nucleoside 5′-triphosphate analogs toward HIV and AMV reverse transcriptases and terminal deoxynucleotidyl transferase were evaluated. The compounds of the d-β and l-β series were found to be terminating substrates for these enzymes, while the derivatives of the d-α and l-α series were recognized only by terminal deoxynucleotidyl transferase, suggesting that for the template-independent enzyme the mutual orientation of the two fragments is of no significance. A hypothesis for binding of nucleotides to the DNA polymerase active center was proposed.

【 授权许可】

Unknown