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Selectivity of DNA polymerases toward α and β nucleotide substrates of d and l series
Author(s) -
Semizarov Dmitry G.,
Victorova Lyubov S.,
Dyatkitalia B.,
von Janta-Lipinski Martin,
Krayevsky Alexander A.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01123-0
Subject(s) - terminal deoxynucleotidyl transferase , dna polymerase , nucleotide , polymerase , transferase , enzyme , nucleotidyltransferase , dna , biochemistry , nucleoside , microbiology and biotechnology , chemistry , stereochemistry , substrate (aquarium) , biology , tunel assay , rna , gene , apoptosis , ecology
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.