ArticleRSC advances2023
Design of highly active substrates using molecular docking for microbial transglutaminase detection.
Article in RSC advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Functional Characterization of a Novel Flavonoid O-methyltransferase From Polar Pedobacter sp. PAMC26386 and Bioactivity Assessment of Flavonoids.Applied biochemistry and biotechnology · 2026Article
- Magnesium chelation of low molecular weight peptides from protein-rich industrial wastes: Production and properties.Journal, genetic engineering & biotechnology · 2025Article
- Computational-guided discovery of UDP-glycosyltransferases for lauryl glucoside production using engineered E. coli.Bioresources and bioprocessing · 2024Article
- Characterization of a unique catechol-O-methyltransferase as a molecular drug target in parasitic filarial nematodes.PLoS neglected tropical diseases · 2024Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transglutaminase (TGase) family catalyzes a transamidation reaction between glutamine (Gln) and lysine (Lys) residues on protein substrates. Highly active substrates are important for cross-linking and modifying proteins of TGase. In the present work, high-activity substrates have been designed based on the principles of enzyme-substrate interaction, using microbial transglutaminase (mTGase) as a research model of the TGase family. Substrates with high activity were screened using a combination of molecular docking and traditional experiments. Twenty-four sets of peptide substrates all produced good catalytic activity with mTGase. FFKKAYAV as the acyl acceptor and VLQRAY as the acyl donor group had the best reaction efficiency with highly sensitive detection of 26 nM mTGase. In addition, the substrate grouping, KAYAV and AFQSAY, detected 130 nM mTGase under physiological conditions (37 °C, pH 7.4), producing 20-fold higher activity than the natural substrate, collagen. The experimental results confirmed the potential for design of high-activity substrates by a combination of molecular docking and traditional experiments under physiological conditions.
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Registered trials
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