Please use this identifier to cite or link to this item:
|Type:||Artigo de periódico|
|Title:||Mode Of Operation And Low-resolution Structure Of A Multi-domain And Hyperthermophilic Endo-β-1,3-glucanase From Thermotoga Petrophila|
de Oliveira Neto M.
|Abstract:||1,3-β-Glucan depolymerizing enzymes have considerable biotechnological applications including biofuel production, feedstock-chemicals and pharmaceuticals. Here we describe a comprehensive functional characterization and low-resolution structure of a hyperthermophilic laminarinase from Thermotoga petrophila (TpLam). We determine TpLam enzymatic mode of operation, which specifically cleaves internal β-1,3-glucosidic bonds. The enzyme most frequently attacks the bond between the 3rd and 4th residue from the non-reducing end, producing glucose, laminaribiose and laminaritriose as major products. Far-UV circular dichroism demonstrates that TpLam is formed mainly by beta structural elements, and the secondary structure is maintained after incubation at 90. °C. The structure resolved by small angle X-ray scattering, reveals a multi-domain structural architecture of a V-shape envelope with a catalytic domain flanked by two carbohydrate-binding modules. © 2011.|
|Citation:||Biochemical And Biophysical Research Communications. , v. 406, n. 4, p. 590 - 594, 2011.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.