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Literature summary for 2.7.7.49 extracted from

  • Pandey, M.; Patel, S.; Gabriel, A.
    Insights into the role of an active site aspartate in Ty1 reverse transcriptase polymerization (2004), J. Biol. Chem., 279, 47840-47848.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D211N still capable of in vitro polymerization, although it is blocked for in vivo transposition. D211N mutation has minimal effect on nucleotide binding but reduces the kpol by about 230fold. The mutation reduces binding affinity for both Mn2+ and Mg2+ Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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mutant version of reverse trancriptase from retrotransposon Ty1, in which one of the three active site aspartates is changed to asparagine, D211N
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