Identification of key amino acid residues inNeisseria polysacchareaamylosucrase
| العنوان: | Identification of key amino acid residues inNeisseria polysacchareaamylosucrase |
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| المؤلفون: | Birte Svensson, Pierre Monsan, Gabrielle Potocki de Montalk, René-Marc Willemot, Patricia Sarçabal, Magali Remaud-Simeon |
| المساهمون: | Unité mixte de recherche biotechnologies bioprocédés, Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS) |
| المصدر: | FEBS Letters FEBS Letters, 2000, 474, pp.33-37 FEBS Letters, Wiley, 2000, 474, pp.33-37 Technical University of Denmark Orbit |
| بيانات النشر: | Wiley, 2000. |
| سنة النشر: | 2000 |
| مصطلحات موضوعية: | Molecular Sequence Data, Biophysics, Glutamic Acid, Sequence alignment, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biochemistry, Catalysis, Structure-Activity Relationship, 03 medical and health sciences, Amylosucrase, Structural Biology, Genetics, Histidine, Glycoside hydrolase, Amino Acid Sequence, Amino Acids, SYNTHESE, Site-directed mutagenesis, Catalytic nucleophile, Molecular Biology, Peptide sequence, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, chemistry.chemical_classification, Aspartic Acid, 0303 health sciences, Binding Sites, Base Sequence, biology, 030306 microbiology, Chemistry, Active site, Cell Biology, General acid catalyst, Amino acid, Glucosyltransferases, Mutagenesis, Site-Directed, biology.protein, Neisseria, Sequence Alignment |
| الوصف: | Amylosucrase from Neisseria polysaccharea catalyzes the synthesis of an amylose-like polymer from sucrose. Sequence alignment revealed that it belongs to the glycoside hydrolase family 13. Site-directed mutagenesis enabled the identification of functionally important amino acid residues located at the active center. Asp-294 is proposed to act as the catalytic nucleophile and Glu-336 as general acid base catalyst in amylosucrase. The conserved Asp-401, His-195 and His-400 residues are critical for the enzymatic activity. These results provide strong support for the predicted close structural and functional relationship between the sucrose-glucosyltransferases and enzymes of the α-amylase family. |
| تدمد: | 0014-5793 1873-3468 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20be7a40176c33dca8456d08f264684e https://doi.org/10.1016/s0014-5793(00)01567-2 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....20be7a40176c33dca8456d08f264684e |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 00145793 18733468 |
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