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|Title:||Mode of operation and low-resolution structure of a multi-domain and hyperthermophilic endo-β-1,3-glucanase from thermotoga petrophila|
Alvarez, Thabata M.
Citadini, Ana P.
Santos, Camila Ramos
Oliveira Neto, Mario de
Oliveira, Renata R.
Pastore, Glaucia M.
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|
|Appears in Collections:||FEA - Artigos e Outros Documentos|
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