ArticleProtein engineering, design & selection : PEDS2009
Substrate specificity of microbial transglutaminase as revealed by three-dimensional docking simulation and mutagenesis.
Article in Protein engineering, design & selection : PEDS, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 52 citations in OpenAlex.
- Microbial transglutaminase in food biotechnology: from biochemical mechanisms to industrial applications.Applied microbiology and biotechnology · 2026Review
- Design of highly active substrates using molecular docking for microbial transglutaminase detection.RSC advances · 2023Article
- Enzymatic Methods for the Site-Specific Radiolabeling of Targeting Proteins.Molecules (Basel, Switzerland) · 2021Review
- Processed Food Additive Microbial Transglutaminase and Its Cross-Linked Gliadin Complexes Are Potential Public Health Concerns in Celiac Disease.International journal of molecular sciences · 2020Review
- Microbial Transglutaminase Is Immunogenic and Potentially Pathogenic in Pediatric Celiac Disease.Frontiers in pediatrics · 2018Review
- Engineered, highly reactive substrates of microbial transglutaminase enable protein labeling within various secondary structure elements.Protein science : a publication of the Protein Society · 2017Article
- ProteinJournal of biomolecular NMR · 2017Article
- Possible association between celiac disease and bacterial transglutaminase in food processing: a hypothesis.Nutrition reviews · 2015Article
- Evaluating factor XIII specificity for glutamine-containing substrates using a matrix-assisted laser desorption/ionization time-of-flight mass spectrometry assay.Analytical biochemistry · 2014Article
- Biotechnological applications of transglutaminases.Biomolecules · 2013Article
- Enhancement of Streptomyces transglutaminase activity and pro-peptide cleavage efficiency by introducing linker peptide in the C-terminus of the pro-peptide.Journal of industrial microbiology & biotechnology · 2013Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transglutaminases (TGases) are used in fields such as food and pharmaceuticals. Unlike other TGases, microbial transglutaminase (MTG) activity is Ca(2+)-independent, broadening its application. Here, a three-dimensional docking model of MTG binding to a peptide substrate, CBZ-Gln-Gly, was simulated. The data reveal CBZ-Gln-Gly to be stretched along the MTG active site cleft with hydrophobic and/or aromatic residues interacting directly with the substrate. Moreover, an oxyanion binding site for TGase activity may be constructed from the amide groups of Cys64 and/or Val65. Alanine mutagenesis verified the simulated binding region and indicated that large molecules can be widely recognized on the MTG cleft.
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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.