http://www.cnr.it/ontology/cnr/individuo/prodotto/ID271727
The identification and molecular characterization of the first archaeal bifunctional exo-beta-glucosidase/N-acetyl-beta-glucosaminidase demonstrate that family GH116 is made of three functionally distinct subfamilies (Articolo in rivista)
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- The identification and molecular characterization of the first archaeal bifunctional exo-beta-glucosidase/N-acetyl-beta-glucosaminidase demonstrate that family GH116 is made of three functionally distinct subfamilies (Articolo in rivista) (literal)
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- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.bbagen.2013.09.022 (literal)
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Ferrara M.C., Cobucci-Ponzano B., Carpentieri A., Henrissat, B., Rossi M., Amoresano A., Moracci M. (2014)
The identification and molecular characterization of the first archaeal bifunctional exo-beta-glucosidase/N-acetyl-beta-glucosaminidase demonstrate that family GH116 is made of three functionally distinct subfamilies
in Biochimica et biophysica acta. G, General subjects (Print)
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- Ferrara M.C., Cobucci-Ponzano B., Carpentieri A., Henrissat, B., Rossi M., Amoresano A., Moracci M. (literal)
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- Institute of Protein Biochemistry, Consiglio Nazionale Delle Ricerche, Via P. Castellino 111, 80131 Naples, Italy; Dipartimento di Scienze Chimiche, Università di Napoli Federico II, Complesso Universitario di Monte S. Angelo, via Cinthia 4 80126 Napoli, Italy; Architecture et Fonction des Macromolécules Biologiques, CNRS UMR 7257, Aix-Marseille University, Case 932, 163 Avenue de Luminy, 13288 Marseille cedex 9, France (literal)
- Titolo
- The identification and molecular characterization of the first archaeal bifunctional exo-beta-glucosidase/N-acetyl-beta-glucosaminidase demonstrate that family GH116 is made of three functionally distinct subfamilies (literal)
- Abstract
- Background ?-N-acetylhexosaminidases, which are involved in a variety of biological processes including energy metabolism, cell proliferation, signal transduction and in pathogen-related inflammation and autoimmune diseases, are widely distributed in Bacteria and Eukaryotes, but only few examples have been found in Archaea so far. However, N-acetylgluco- and galactosamine are commonly found in the extracellular storage polymers and in the glycans decorating abundantly expressed glycoproteins from different Crenarchaeota Sulfolobus sp., suggesting that ?-N-acetylglucosaminidase activities could be involved in the modification/recycling of these cellular components. Methods A thermophilic ?-N-acetylglucosaminidase was purified from cellular extracts of S. solfataricus, strain P2, identified by mass spectrometry, and cloned and expressed in E. coli. Glycosidase assays on different strains of S. solfataricus, steady state kinetic constants, substrate specificity analysis, and the sensitivity to two inhibitors of the recombinant enzyme were also reported. Results A new ?-N-acetylglucosaminidase from S. solfataricus was unequivocally identified as the product of gene sso3039. The detailed enzymatic characterization demonstrates that this enzyme is a bifunctional ?-glucosidase/?-N-acetylglucosaminidase belonging to family GH116 of the carbohydrate active enzyme (CAZy) classification. Conclusions This study allowed us to propose that family GH116 is composed of three subfamilies, which show distinct substrate specificities and inhibitor sensitivities. General significance The characterization of SSO3039 allows, for the first time in Archaea, the identification of an enzyme involved in the metabolism ?-N-acetylhexosaminide, an essential component of glycoproteins in this domain of life, and substantially increases our knowledge on the functional role and phylogenetic relationships amongst the GH116 CAZy family members. © 2013 Elsevier B.V. All rights reserved. (literal)
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