Selectivity of DNA polymerases toward alpha and beta nucleotide substrates of D and L series.
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-beta and L-beta series were found to be terminating substrates for these enzymes, while the derivatives of the D-alpha and L-alpha 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.
Semizarov
D G
DG
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow.
Victorova
L S
LS
Dyatkina
N B
NB
von Janta-Lipinski
M
M
Krayevsky
A A
AA
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D009189:Avian Myeloblastosis Virus / Q000201:enzymology*; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000096:biosynthesis; D004253:DNA Nucleotidylexotransferase / Q000378:metabolism*; D017931:DNA Primers / Q000737:chemistry / Q000378:metabolism; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D006678:HIV / Q000201:enzymology*; D008969:Molecular Sequence Data; D012313:RNA / Q000378:metabolism; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism*; D013379:Substrate Specificity; D013698:Templates, Genetic
D017931:DNA Primers; C034477:RNA primers; D012313:RNA; D000255:Adenosine Triphosphate; D004247:DNA; D004253:DNA Nucleotidylexotransferase; D012194:RNA-Directed DNA Polymerase; D004259:DNA-Directed DNA Polymerase