| pubmed-article:10913610 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10913610 | lifeskim:mentions | umls-concept:C0028923 | lld:lifeskim |
| pubmed-article:10913610 | lifeskim:mentions | umls-concept:C0242209 | lld:lifeskim |
| pubmed-article:10913610 | lifeskim:mentions | umls-concept:C0003240 | lld:lifeskim |
| pubmed-article:10913610 | lifeskim:mentions | umls-concept:C2349984 | lld:lifeskim |
| pubmed-article:10913610 | lifeskim:mentions | umls-concept:C1705822 | lld:lifeskim |
| pubmed-article:10913610 | lifeskim:mentions | umls-concept:C0348011 | lld:lifeskim |
| pubmed-article:10913610 | lifeskim:mentions | umls-concept:C0449830 | lld:lifeskim |
| pubmed-article:10913610 | lifeskim:mentions | umls-concept:C2827597 | lld:lifeskim |
| pubmed-article:10913610 | lifeskim:mentions | umls-concept:C0652024 | lld:lifeskim |
| pubmed-article:10913610 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:10913610 | pubmed:dateCreated | 2000-8-16 | lld:pubmed |
| pubmed-article:10913610 | pubmed:abstractText | Macrolides are a group of antibiotics structurally characterized by a macrocyclic lactone to which one or several deoxy-sugar moieties are attached. The sugar moieties are transferred to the different aglycones by glycosyltransferases (GTF). The OleI GTF of an oleandomycin producer, Streptomyces antibioticus, catalyzes the inactivation of this macrolide by glycosylation. The product of this reaction was isolated and its structure elucidated. The donor substrate of the reaction was UDP-alpha-D-glucose, but the reaction product showed a beta-glycosidic linkage. The inversion of the anomeric configuration of the transferred sugar and other data about the kinetics of the reaction and primary structure analysis of several GTFs are compatible with a reaction mechanism involving a single nucleophilic substitution at the sugar anomeric carbon in the catalytic center of the enzyme. | lld:pubmed |
| pubmed-article:10913610 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10913610 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10913610 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10913610 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10913610 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10913610 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10913610 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10913610 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10913610 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10913610 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10913610 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:10913610 | pubmed:author | pubmed-author:SalasJ AJA | lld:pubmed |
| pubmed-article:10913610 | pubmed:author | pubmed-author:QuirósL MLM | lld:pubmed |
| pubmed-article:10913610 | pubmed:author | pubmed-author:CarbajoR JRJ | lld:pubmed |
| pubmed-article:10913610 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10913610 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:10913610 | pubmed:volume | 476 | lld:pubmed |
| pubmed-article:10913610 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10913610 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10913610 | pubmed:pagination | 186-9 | lld:pubmed |
| pubmed-article:10913610 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10913610 | pubmed:meshHeading | pubmed-meshheading:10913610... | lld:pubmed |
| pubmed-article:10913610 | pubmed:meshHeading | pubmed-meshheading:10913610... | lld:pubmed |
| pubmed-article:10913610 | pubmed:meshHeading | pubmed-meshheading:10913610... | lld:pubmed |
| pubmed-article:10913610 | pubmed:meshHeading | pubmed-meshheading:10913610... | lld:pubmed |
| pubmed-article:10913610 | pubmed:meshHeading | pubmed-meshheading:10913610... | lld:pubmed |
| pubmed-article:10913610 | pubmed:meshHeading | pubmed-meshheading:10913610... | lld:pubmed |
| pubmed-article:10913610 | pubmed:meshHeading | pubmed-meshheading:10913610... | lld:pubmed |
| pubmed-article:10913610 | pubmed:meshHeading | pubmed-meshheading:10913610... | lld:pubmed |
| pubmed-article:10913610 | pubmed:meshHeading | pubmed-meshheading:10913610... | lld:pubmed |
| pubmed-article:10913610 | pubmed:meshHeading | pubmed-meshheading:10913610... | lld:pubmed |
| pubmed-article:10913610 | pubmed:meshHeading | pubmed-meshheading:10913610... | lld:pubmed |
| pubmed-article:10913610 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10913610 | pubmed:articleTitle | Inversion of the anomeric configuration of the transferred sugar during inactivation of the macrolide antibiotic oleandomycin catalyzed by a macrolide glycosyltransferase. | lld:pubmed |
| pubmed-article:10913610 | pubmed:affiliation | Departamento de Biología Funcional, Universidad de Oviedo, Spain. | lld:pubmed |
| pubmed-article:10913610 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10913610 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10913610 | lld:pubmed |
