Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/107869
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
Author: Cota J.
Alvarez T.M.
Citadini A.P.
Santos C.R.
de Oliveira Neto M.
Oliveira R.R.
Pastore G.M.
Ruller R.
Prade R.A.
Murakami M.T.
Squina F.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.
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Rights: fechado
Identifier DOI: 10.1016/j.bbrc.2011.02.098
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-79953029268&partnerID=40&md5=112139d7793f0de50ede3865db648595
Date Issue: 2011
Appears in Collections:Unicamp - Artigos e Outros Documentos

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