Dual Stabilization of S-Adenosylmethionine for Enzymatic DNA Labeling
Bucevicius, J.; Gerasimaite, R.; Lukinavicius, G.
Show abstract
S-Adenosyl-L-methionine (AdoMet) analogues are powerful tool for site-specific biomolecular labeling via methyltransferase (MTase) catalyzed transfer reactions. However, their utility is often limited by poor chemical stability under enzymatic reaction conditions. Here, we report a new class of stabilized AdoMet analogues featuring a conformationally constrained proline side chain in place of homoalanine. This substitution inhibits intramolecular cyclization, a major decomposition pathway. Combination with selenonium modification, which suppresses depurination, yields analogues with up to a 90-fold increase half-life relative to AdoMet. These cofactors retain activity with DNA MTases, and allow sequence-specific labeling of plasmid DNA using both two-step and single-step approaches with fluorescent dyes.
Matching journals
The top 3 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Information propagation through enzyme-free catalytic templating of DNA dimerization with weak product inhibition 96%
- Synthesis and single-molecule imaging reveal stereospecific enhancement of binding kinetics by the antitumor eEF1A antagonist SR-A3 94%
- Fuscimiditide: a RiPP with {Omega}-Ester and Aspartimide Post-translational Modifications 94%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.