ArticleJournal of molecular evolution2015
Identification of Sequence-Selective Tyrosine Kinase Deoxyribozymes.
Article in Journal of molecular evolution, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Probing the Specificity of Fluorescent Deoxyribozymes Using Single-Step Selections and Machine Learning.ACS chemical biology · 2026Article
- Sequence-Dependent Acylation of Peptide Lysine Residues by DNAzymes.Chembiochem : a European journal of chemical biology · 2024Article
- Site-specific N-alkylation of DNA oligonucleotide nucleobases by DNAzyme-catalyzed reductive amination.Nucleic acids research · 2024Article
- DNAmoreDB, a database of DNAzymes.Nucleic acids research · 2021Article
- DNAzymes for amine and peptide lysine acylation.Organic & biomolecular chemistry · 2021Article
- DNA-Catalyzed Introduction of Azide at Tyrosine for Peptide Modification.Angewandte Chemie (International ed. in English) · 2016Article
- DNA-catalyzed glycosylation using aryl glycoside donors.Chemical communications (Cambridge, England) · 2016Article
- Catalytic DNA: Scope, Applications, and Biochemistry of Deoxyribozymes.Trends in biochemical sciences · 2016Review
- Assessing histidine tags for recruiting deoxyribozymes to catalyze peptide and protein modification reactions.Organic & biomolecular chemistry · 2016Article
- DNA Oligonucleotide 3'-Phosphorylation by a DNA Enzyme.Biochemistry · 2016Article
- DNA-Catalyzed Amide Hydrolysis.Journal of the American Chemical Society · 2016Article
- A Quarter Century of In Vitro Selection.Journal of molecular evolution · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Deoxyribozymes (DNA enzymes) have been developed for a growing variety of chemical reactions, including with peptide substrates. We recently described the first tyrosine kinase deoxyribozymes, which lacked the ability to discriminate among peptide substrates on the basis of the amino acids surrounding the tyrosine residue. Those deoxyribozymes were identified by in vitro selection using a DNA-anchored peptide substrate in which the residues neighboring tyrosine were all alanine. Here, we performed in vitro selection for tyrosine kinase activity using three peptide substrates in which the neighboring residues included a variety of side chains. For one of these three peptides, we found numerous deoxyribozymes that discriminate strongly in favor of phosphorylating tyrosine when the surrounding residues are specifically those used in the selection process. Three different short peptide sequence motifs of 2-4 amino acids were required for catalysis by three unique deoxyribozymes. For a second peptide substrate, the selection process led to one deoxyribozyme which exhibits partial discrimination among peptide sequences. These findings establish the feasibility of identifying DNA enzymes that catalyze sequence-selective tyrosine phosphorylation, which suggests the downstream practical utility of such deoxyribozymes. More broadly, this outcome reinforces the conclusion that nucleic acid catalysts can discriminate among peptide substrates in the context of biochemically relevant reactions.
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