| pubmed-article:9860840 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9860840 | lifeskim:mentions | umls-concept:C0995927 | lld:lifeskim |
| pubmed-article:9860840 | lifeskim:mentions | umls-concept:C0205101 | lld:lifeskim |
| pubmed-article:9860840 | lifeskim:mentions | umls-concept:C0441472 | lld:lifeskim |
| pubmed-article:9860840 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:9860840 | lifeskim:mentions | umls-concept:C0439857 | lld:lifeskim |
| pubmed-article:9860840 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:9860840 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:9860840 | pubmed:issue | 49 | lld:pubmed |
| pubmed-article:9860840 | pubmed:dateCreated | 1999-1-12 | lld:pubmed |
| pubmed-article:9860840 | pubmed:abstractText | The beta-glycosidase from the hyperthermophilic Archaeon Sulfolobus solfataricus hydrolyzes beta-glycosides following a retaining mechanism based upon the action of two amino acids: Glu387, which acts as the nucleophile of the reaction, and Glu206, which acts as the general acid/base catalyst. The activities of inactive mutants of the catalytic nucleophile Glu387Ala/Gly were restored by externally added nucleophiles. Sodium azide and sodium formate were used as external nucleophiles and the products of their reaction were characterized. Glu387Ala/Gly mutants were reactivated with 2, 4-DNP-beta-Glc substrate and the Glu387Gly mutant showed recovered activity, with the same nucleophiles, also on 2-NP-beta-Glc. The reaction catalyzed by the Glu387Gly mutant proceeded differently depending on the type of externally added nucleophile. Sodium azide restored the catalytic activity of the mutant by attacking the alpha-side of the anomeric carbon of the substrates, thereby yielding an inverting glycosidase. Sodium formate promoted the opposite behavior (retaining) in the mutant, producing 3-O-beta-linked disaccharide derivative of the substrates. A possible role of sodium formate as a biomimicking agent in replacing the natural nucleophile Glu387 is also discussed. | lld:pubmed |
| pubmed-article:9860840 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9860840 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860840 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9860840 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860840 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860840 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860840 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860840 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860840 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860840 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860840 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860840 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860840 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860840 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9860840 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9860840 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:9860840 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:9860840 | pubmed:author | pubmed-author:RossiMM | lld:pubmed |
| pubmed-article:9860840 | pubmed:author | pubmed-author:TrinconeAA | lld:pubmed |
| pubmed-article:9860840 | pubmed:author | pubmed-author:CiaramellaMM | lld:pubmed |
| pubmed-article:9860840 | pubmed:author | pubmed-author:MoracciMM | lld:pubmed |
| pubmed-article:9860840 | pubmed:author | pubmed-author:PeruginoGG | lld:pubmed |
| pubmed-article:9860840 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9860840 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:9860840 | pubmed:volume | 37 | lld:pubmed |
| pubmed-article:9860840 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9860840 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9860840 | pubmed:pagination | 17262-70 | lld:pubmed |
| pubmed-article:9860840 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:9860840 | pubmed:meshHeading | pubmed-meshheading:9860840-... | lld:pubmed |
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| pubmed-article:9860840 | pubmed:meshHeading | pubmed-meshheading:9860840-... | lld:pubmed |
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| pubmed-article:9860840 | pubmed:meshHeading | pubmed-meshheading:9860840-... | lld:pubmed |
| pubmed-article:9860840 | pubmed:meshHeading | pubmed-meshheading:9860840-... | lld:pubmed |
| pubmed-article:9860840 | pubmed:meshHeading | pubmed-meshheading:9860840-... | lld:pubmed |
| pubmed-article:9860840 | pubmed:meshHeading | pubmed-meshheading:9860840-... | lld:pubmed |
| pubmed-article:9860840 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9860840 | pubmed:articleTitle | Restoration of the activity of active-site mutants of the hyperthermophilic beta-glycosidase from Sulfolobus solfataricus: dependence of the mechanism on the action of external nucleophiles. | lld:pubmed |
| pubmed-article:9860840 | pubmed:affiliation | Institute of Protein Biochemistry and Enzymology, Consiglio Nazionale delle Ricerche, Naples, Italy. | lld:pubmed |
| pubmed-article:9860840 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9860840 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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