ArticleJournal of the American Chemical Society2015
Phosphoserine Lyase Deoxyribozymes: DNA-Catalyzed Formation of Dehydroalanine Residues in Peptides.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- DNA Catalysis: Design, Function, and Optimization.Molecules (Basel, Switzerland) · 2024Review
- Cleaving DNA with DNA: Cooperative Tuning of Structure and Reactivity Driven by Copper Ions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Discovery of Dehydroamino Acid Residues in the Capsid and Matrix Structural Proteins of HIV-1.Journal of proteome research · 2022Article
- DNA polymerases η and κ bypass NThe Journal of biological chemistry · 2021Article
- DNAmoreDB, a database of DNAzymes.Nucleic acids research · 2021Article
- 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
- DNA Catalysis: The Chemical Repertoire of DNAzymes.Molecules (Basel, Switzerland) · 2015Review
- Enzymatic bypass of an NThe Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Dehydroalanine (Dha) is a nonproteinogenic electrophilic amino acid that is a synthetic intermediate or product in the biosynthesis of several bioactive cyclic peptides such as lantibiotics, thiopeptides, and microcystins. Dha also enables labeling of proteins and synthesis of post-translationally modified proteins and their analogues. However, current chemical approaches to introducing Dha into peptides have substantial limitations. Using in vitro selection, here we show that DNA can catalyze Zn(2+) or Zn(2+)/Mn(2+)-dependent formation of Dha from phosphoserine (pSer), i.e., exhibit pSer lyase activity, a fundamentally new DNA-catalyzed reaction. Two new pSer lyase deoxyribozymes, named Dha-forming deoxyribozymes 1 and 2 (DhaDz1 and DhaDz2), each function with multiple turnover on the model hexapeptide substrate that was used during selection. Using DhaDz1, we generated Dha from pSer within an unrelated linear 13-mer peptide. Subsequent base-promoted intramolecular cyclization of homocysteine into Dha formed a stable cystathionine (thioether) analogue of the complement inhibitor compstatin. These findings establish the fundamental catalytic ability of DNA to eliminate phosphate from pSer to form Dha and suggest that with further development, pSer lyase deoxyribozymes will have broad practical utility for site-specific enzymatic synthesis of Dha from pSer in peptide substrates.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.