ArticleProtein science : a publication of the Protein Society2018
Illuminating structure and acyl donor sites of a physiological transglutaminase substrate from Streptomyces mobaraensis.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 19 citations in OpenAlex.
- SANS investigation of fungal loosenins reveals substrate-dependent impacts of protein action on the inter-microfibril arrangement of cellulosic substrates.Biotechnology for biofuels and bioproducts · 2025Article
- APlants (Basel, Switzerland) · 2025Article
- Enhancing substrate specificity of microbial transglutaminase for precise nanobody labeling.Synthetic and systems biotechnology · 2025Article
- Structural characterization of a soil viral auxiliary metabolic gene product - a functional chitosanase.Nature communications · 2022Article
- Enzymatic Methods for the Site-Specific Radiolabeling of Targeting Proteins.Molecules (Basel, Switzerland) · 2021Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transglutaminase from Streptomyces mobaraensis (MTG) has become a powerful tool to covalently and highly specifically link functional amines to glutamine donor sites of therapeutic proteins. However, details regarding the mechanism of substrate recognition and interaction of the enzyme with proteinaceous substrates still remain mostly elusive. We have determined the crystal structure of the Streptomyces papain inhibitory protein (SPI
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