ArticleJournal of proteome research2020
Tryp-N: A Thermostable Protease for the Production of N-terminal Argininyl and Lysinyl Peptides.
Article in Journal of proteome research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- The Enzyme Effect: Broadening the Horizon of MS Optimization to Nontryptic Digestion in Proteomics.Journal of the American Society for Mass Spectrometry · 2025Article
- Postproline Cleaving Enzymes also Show Specificity to Reduced Cysteine.Analytical chemistry · 2024Article
- Increasing the Overall Proteome Coverage by Combining Protein Digestion by Tryp-N and Trypsin.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Latency, thermal stability, and identification of an inhibitory compound of mirolysin, a secretory protease of the human periodontopathogenJournal of enzyme inhibition and medicinal chemistry · 2021Article
- A protocol for analyzing the protein terminome of human cancer cell line culture supernatants.STAR protocols · 2021Article
- Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Bottom-up proteomics is a mainstay in protein identification and analysis. These studies typically employ proteolytic treatment of biological samples to generate suitably sized peptides for tandem mass spectrometric (MS) analysis. In MS, fragmentation of peptides is largely driven by charge localization. Consequently, peptides with basic centers exclusively on their N-termini produce mainly b-ions. Thus, it was long ago realized that proteases that yield such peptides would be valuable proteomic tools for achieving simplified peptide fragmentation patterns and peptide assignment. Work by several groups has identified such proteases, however, structural analysis of these suggested that enzymatic optimization was possible. We therefore endeavored to find enzymes that could provide enhanced activity and versatility while maintaining specificity. Using these previously described proteases as informatic search templates, we discovered and then characterized a thermophilic metalloprotease with N-terminal specificity for arginine and lysine. This enzyme, dubbed Tryp-N, affords many advantages including improved thermostability, solvent and detergent tolerance, and rapid digestion time.
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Registered trials
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