ArticleScientific reports2018
Thermal stabilization of the deglycating enzyme Amadoriase I by rational design.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
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- Tailoring FPOX enzymes for enhanced stability and expanded substrate recognition.Scientific reports · 2023Article
- In Silico Analysis of Nanoplastics' and β-amyloid Fibrils' Interactions.Molecules (Basel, Switzerland) · 2023Article
- Improving Both the Thermostability and Catalytic Efficiency of Phospholipase D fromInternational journal of molecular sciences · 2022Article
- Rational design of a disulfide bridge increases the thermostability of microbial transglutaminase.Applied microbiology and biotechnology · 2022Article
- A Simple Strategy to Eliminate Hexosylation Bias in the Relative Quantification of N-Glycosylation in Biopharmaceuticals.Angewandte Chemie (International ed. in English) · 2020Article
- The Anti-Amyloidogenic Action of Doxycycline: A Molecular Dynamics Study on the Interaction with Aβ42.International journal of molecular sciences · 2019Article
- Ts2631 Endolysin from the ExtremophilicViruses · 2019Article
- Molecular dynamics investigation of halogenated amyloidogenic peptides.Journal of molecular modeling · 2019Article
- Disulfide Bond Engineering of an Endoglucanase fromInternational journal of molecular sciences · 2019Article
Corrections and comments
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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
Amadoriases are a class of FAD-dependent enzymes that are found in fungi, yeast and bacteria and that are able to hydrolyze glycated amino acids, cleaving the sugar moiety from the amino acidic portion. So far, engineered Amadoriases have mostly found practical application in the measurement of the concentration of glycated albumin in blood samples. However, these engineered forms of Amadoriases show relatively low absolute activity and stability levels, which affect their conditions of use. Therefore, enzyme stabilization is desirable prior to function-altering molecular engineering. In this work, we describe a rational design strategy based on a computational screening method to evaluate a library of potentially stabilizing disulfide bonds. Our approach allowed the identification of two thermostable Amadoriase I mutants (SS03 and SS17) featuring a significantly higher T
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