ArticleThe Journal of biological chemistry2010
Structural and kinetic analysis of Schwanniomyces occidentalis invertase reveals a new oligomerization pattern and the role of its supplementary domain in substrate binding.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 79 citations in OpenAlex.
- Evolutionary diversification of invertase paralogs couples carbon metabolism and sexual reproduction in fission yeasts.Molecular biology and evolution · 2026Article
- Enhanced fructooligosaccharides synthesis by engineered Trichoderma atroviride β-fructofuranosidase.Applied microbiology and biotechnology · 2026Article
- Oligomeric Structure of Yeast and Other Invertases Governs Specificity.Sub-cellular biochemistry · 2024Review
- Protein engineering of invertase for enhancing yeast dough fermentation under high-sucrose conditions.Folia microbiologica · 2023Article
- Insights into the Structure of the Highly Glycosylated Ffase fromInternational journal of molecular sciences · 2022Article
- Tailoring fructooligosaccharides composition with engineered Zymomonas mobilis ZM4.Applied microbiology and biotechnology · 2022Article
- Enzymatic and structural characterization of β-fructofuranosidase from the honeybee gut bacterium Frischella perrara.Applied microbiology and biotechnology · 2022Article
- Enzymatic synthesis of novel fructosylated compounds by Ffase fromRSC advances · 2021Article
- Effects on Brood Development in the Carpenter AntInsects · 2021Article
- New insights into the molecular mechanism behind mannitol and erythritol fructosylation by β-fructofuranosidase from Schwanniomyces occidentalis.Scientific reports · 2021Article
- Chance or Necessity-The Fungi Co-Occurring withInsects · 2021Article
- Insect derived extra oral GH32 plays a role in susceptibility of wheat to Hessian fly.Scientific reports · 2021Article
- The Important Roles Played in Substrate Binding of Aromatic Amino Acids in Exo-Inulinase FromFrontiers in molecular biosciences · 2020Article
- UniqueJournal of biological engineering · 2019Article
- Structural Analysis of the Catalytic Mechanism and Substrate Specificity of Anabaena Alkaline Invertase InvA Reveals a Novel Glucosidase.The Journal of biological chemistry · 2016Article
- Characterization of a novel low-temperature-active, alkaline and sucrose-tolerant invertase.Scientific reports · 2016Article
- Structural Analysis of β-Fructofuranosidase from Xanthophyllomyces dendrorhous Reveals Unique Features and the Crucial Role of N-Glycosylation in Oligomerization and Activity.The Journal of biological chemistry · 2016Article
- Saprophytic and pathogenic fungi in the Ceratocystidaceae differ in their ability to metabolize plant-derived sucrose.BMC evolutionary biology · 2015Article
- Semirational Directed Evolution of Loop Regions in Aspergillus japonicus β-Fructofuranosidase for Improved Fructooligosaccharide Production.Applied and environmental microbiology · 2015Article
- 1-FFT amino acids involved in high DP inulin accumulation in Viguiera discolor.Frontiers in plant science · 2015Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Schwanniomyces occidentalis invertase is an extracellular enzyme that hydrolyzes sucrose and releases beta-fructose from various oligosaccharides and essential storage fructan polymers such as inulin. We report here the three-dimensional structure of Sw. occidentalis invertase at 2.9 A resolution and its complex with fructose at 1.9 A resolution. The monomer presents a bimodular arrangement common to other GH32 enzymes, with an N-terminal 5-fold beta-propeller catalytic domain and a C-terminal beta-sandwich domain for which the function has been unknown until now. However, the dimeric nature of Sw. occidentalis invertase reveals a unique active site cleft shaped by both subunits that may be representative of other yeast enzymes reported to be multimeric. Binding of the tetrasaccharide nystose and the polymer inulin was explored by docking analysis, which suggested that medium size and long substrates are recognized by residues from both subunits. The identified residues were mutated, and the enzymatic activity of the mutants against sucrose, nystose, and inulin were investigated by kinetic analysis. The replacements that showed the largest effect on catalytic efficiency were Q228V, a residue putatively involved in nystose and inulin binding, and S281I, involved in a polar link at the dimer interface. Moreover, a significant decrease in catalytic efficiency against inulin was observed in the mutants Q435A and Y462A, both located in the beta-sandwich domain of the second monomer. This highlights the essential function that oligomerization plays in substrate specificity and assigns, for the first time, a direct catalytic role to the supplementary domain of a GH32 enzyme.
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