ArticleThe Journal of biological chemistry2011
Engineering bifunctional laccase-xylanase chimeras for improved catalytic performance.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Expression, Solubilization, and Refolding Recovery of a Novel l‑Asparaginase-Arginase 1 Chimera fromACS omega · 2026Article
- Structure-Function Relationship of the β-Hairpin ofInternational journal of molecular sciences · 2025Article
- Artificial Fusions between P450 BM3 and an Alcohol Dehydrogenase for Efficient (+)-Nootkatone Production.Chembiochem : a European journal of chemical biology · 2022Article
- Review
- Structural Characterization of Multienzyme Assemblies: An Overview.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Biochemical Characterization of a Bifunctional Enzyme Constructed by the Fusion of a Glucuronan Lyase and a Chitinase fromLife (Basel, Switzerland) · 2020Article
- Genetically Engineered Proteins to Improve Biomass Conversion: New Advances and Challenges for Tailoring Biocatalysts.Molecules (Basel, Switzerland) · 2019Review
- Enzyme Fusion Removes Competition for Geranylgeranyl Diphosphate in Carotenogenesis.Plant physiology · 2019Article
- Converting a Periplasmic Binding Protein into a Synthetic Biosensing Switch through Domain Insertion.BioMed research international · 2019Review
- An Insight Into Ameliorating Production, Catalytic Efficiency, Thermostability and Starch Saccharification of Acid-Stable α-Amylases From Acidophiles.Frontiers in bioengineering and biotechnology · 2018Review
- Protein Engineering Strategies to Expand CRISPR-Cas9 Applications.International journal of genomics · 2018Review
- Microbial lipolytic fusion enzymes: current state and future perspectives.World journal of microbiology & biotechnology · 2017Review
- A review on chimeric xylanases: methods and conditions.3 Biotech · 2017Review
- The urea carboxylase and allophanate hydrolase activities of urea amidolyase are functionally independent.Protein science : a publication of the Protein Society · 2016Article
- A xylose-stimulated xylanase-xylose binding protein chimera created by random nonhomologous recombination.Biotechnology for biofuels · 2016Article
- Fast and reliable production, purification and characterization of heat-stable, bifunctional enzyme chimeras.AMB Express · 2015Article
- Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.Cellular and molecular life sciences : CMLS · 2015Review
- Insertion of a xylanase in xylose binding protein results in a xylose-stimulated xylanase.Biotechnology for biofuels · 2015Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two bifunctional enzymes exhibiting combined xylanase and laccase activities were designed, constructed, and characterized by biochemical and biophysical methods. The Bacillus subtilis cotA and xynA genes were used as templates for gene fusion, and the xynA coding sequence was inserted into a surface loop of the cotA. A second chimera was built replacing the wild-type xynA gene by a thermostable variant (xynAG3) previously obtained by in vitro molecular evolution. Kinetic measurements demonstrated that the pH and temperature optima of the catalytic domains in the chimeras were altered by less than 0.5 pH units and 5 °C, respectively, when compared with the parental enzymes. In contrast, the catalytic efficiency (k(cat)/K(m)) of the laccase activity in both chimeras was 2-fold higher than for the parental laccase. Molecular dynamics simulations of the CotA-XynA chimera indicated that the two domains are in close contact, which was confirmed by the low resolution structure obtained by small angle x-ray scattering. The simulation also indicates that the formation of the inter-domain interface causes the dislocation of the loop comprising residues Leu-558 to Lys-573 in the laccase domain, resulting in a more accessible active site and exposing the type I Cu(2+) ion to the solvent. These structural changes are consistent with the results from UV-visible electronic and EPR spectroscopy experiments of the type I copper between the native and chimeric enzymes and are likely to contribute to the observed increase in catalytic turnover number.
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