http://www.cnr.it/ontology/cnr/individuo/prodotto/ID8834
Preparation of a glycosynthase from the beta-glycosidase of the Archaeon Pyrococcus horikoshii (Articolo in rivista)
- Type
- Label
- Preparation of a glycosynthase from the beta-glycosidase of the Archaeon Pyrococcus horikoshii (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1080/10242420500518581 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Perugino G.; Falcicchio P.; Corsaro M.M.; Matsui I.; Parrilli M.; Rossi M.; Moracci M. (literal)
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- Proceedings of the 6th Carbohydrate Bioengineering Meeting Location: Barcelona, SPAIN Date: APR 03-06, 2005;
selected and revised paper (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
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- Special Issue: Sixth Carbohydrate Bioengineering Meeting (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Institute of Protein Biochemistry ?/ Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131, Naples, Italy
Dipartimento di Chimica Organica e Biochimica, Universita` di Napoli ''Federico II'', Via Cinthia 4, 80126, Naples, Italy
Biological Information Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki
305-8566, Japan
Dipartimento di Biologia Strutturale e Funzionale, Universita` di Napoli ''Federico II'', Via Cinthia 4, 80126, Naples, Italy (literal)
- Titolo
- Preparation of a glycosynthase from the beta-glycosidase of the Archaeon Pyrococcus horikoshii (literal)
- Abstract
- The beta-glycosidase from the hyperthermophilic Archaeon Pyrococcus horikoshii (Phobeta-gly) is a monomeric enzyme with wide substrate specificity belonging to family 1 of glycoside hydrolases classification. Inspection of the three-dimensional structure of the enzyme, recently resolved, showed that Phobeta-gly is membrane bound and that the residues putatively involved in the catalytic activity are Glu155 and Glu324 working as the general acid/base and the nucleophile of the reaction, respectively. We show here that mutation of the latter completely eliminated the activity of the enzyme and that it could be reactivated in the presence of sodium formate. Analysis of the products obtained in the presence of sodium formate buffer pH 4.0 at 75°C showed that the Glu324Gly mutant acts as a hyperthermophilic glycosynthase. (literal)
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