Oligomeric Structure of Yeast and Other Invertases Governs Specificity
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Publisher
Springer International Publishing
Link
https://link.springer.com/content/pdf/10.1007/978-3-031-58843-3_19
Reference32 articles.
1. Alberto F, Bignon C, Sulzenbacher G et al (2004) The three-dimensional structure of Invertase (β-Fructosidase) from Thermotoga maritima reveals a Bimodular arrangement and an evolutionary relationship between retaining and inverting Glycosidases. J Biol Chem 279:18903–18910. https://doi.org/10.1074/jbc.M313911200
2. Alegre ACP, Teixeira d L, de Moraes Polizeli M, Terenzi HF et al (2009) Production of thermostable invertases by Aspergillus caespitosus under submerged or solid state fermentation using agroindustrial residues as carbon source. Braz J Microbiol 40:612–622. https://doi.org/10.1590/S1517-838220090003000025
3. Álvaro-Benito M, Polo A, González B et al (2010) Structural and kinetic analysis of Schwanniomyces occidentalis invertase reveals a new oligomerization pattern and the role of its supplementary domain in substrate binding. J Biol Chem 285:13930–13941. https://doi.org/10.1074/jbc.M109.095430
4. Álvaro-Benito M, Sainz-Polo MA, González-Pérez D et al (2012) Structural and kinetic insights reveal that the amino acid pair Gln-228/Asn-254 modulates the transfructosylating specificity of Schwanniomyces occidentalis β-fructofuranosidase, an enzyme that produces prebiotics. J Biol Chem 287:19674–19686. https://doi.org/10.1074/jbc.M112.355503
5. Bujacz A, Jedrzejczak-Krzepkowska M, Bielecki S et al (2011) Crystal structures of the apo form of β-fructofuranosidase from Bifidobacterium longum and its complex with fructose. FEBS J 278:1728–1744. https://doi.org/10.1111/j.1742-4658.2011.08098.x
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