Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/345055
Type: Artigo
Title: Mode of operation and low-resolution structure of a multi-domain and hyperthermophilic endo-β-1,3-glucanase from thermotoga petrophila
Author: Cota, Junio
Alvarez, Thabata M.
Citadini, Ana P.
Santos, Camila Ramos
Oliveira Neto, Mario de
Oliveira, Renata R.
Pastore, Glaucia M.
Ruller, Roberto
Prade, Rolf A.
Murakami, Mario T.
Squina, Fabio 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
Subject: Eletroforese capilar
Country: Estados Unidos
Editor: Elsevier
Rights: Fechado
Identifier DOI: 10.1016/j.bbrc.2011.02.098
Address: https://www.sciencedirect.com/science/article/pii/S0006291X11003032
Date Issue: 2011
Appears in Collections:FEA - Artigos e Outros Documentos

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