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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, de Oliveira Neto, Mario, Oliveira, Renata R., Pastore, Glaucia M., Ruller, Roberto, Prade, Rolf A., Murakami, Mario T., Squina, Fabio M.
Source:
Biochemical and biophysical research communications 2011 v.406 no.4 pp. 590-594
ISSN:
0006-291X
Subject:
Thermotoga, X-radiation, active sites, beta-glucans, biofuels, carbohydrate binding, drugs, enzymes, glucose
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.
Agid:
893667