| pubmed-article:11042119 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11042119 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:11042119 | lifeskim:mentions | umls-concept:C0995679 | lld:lifeskim |
| pubmed-article:11042119 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:11042119 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:11042119 | lifeskim:mentions | umls-concept:C0055033 | lld:lifeskim |
| pubmed-article:11042119 | pubmed:dateCreated | 2001-1-2 | lld:pubmed |
| pubmed-article:11042119 | pubmed:abstractText | Steady-state kinetic studies of the enzymic glucosyl transfer to and from phosphate catalysed by cellobiose phosphorylase from Cellulomonas uda have shown that this enzyme operates by a ternary-complex kinetic mechanism in which beta-cellobiose binds before phosphate, and beta-D-glucose and alpha-D-glucopyranosyl phosphate are released in that order. alpha-D-Glucopyranosyl fluoride (but not beta-D-glucopyranosyl fluoride) serves as alternative glucosyl donor for beta-cellobiose synthesis with a specificity constant that is one-ninth that of the corresponding enzymic reaction with alpha-D-glucopyranosyl phosphate (approximately 20000 M(-1).s(-1) at 30 degrees C). The kinetic parameters for a complete series of deoxy and deoxyfluoro analogues of D-glucose have been determined and the data yield estimates of the net strengths of hydrogen-bonding interactions with the non-reacting hydroxy groups of D-glucose at the transition state (0.8-4.0 kcal/mol, where 1 cal identical with 4.184 J) and enable the prediction of the polarities of these hydrogen bonds. Each hydroxy group functions as donor of a hydrogen for bonding to probably a charged (at 3-OH) or neutral (at 2-OH and 6-OH) acceptor group on the enzyme. The equatorial 1-OH is essential for enzyme activity. Derivatives of D-glucose in which the 1-OH or the reacting 4-OH were replaced by hydrogen or fluorine have been tested as inhibitors to measure their affinities for the sugar-binding subsite +1 (numbered from the bond-cleaving/forming site). The data show that hydrogen-bonding interactions between the 1-OH and 4-OH and charged groups on the enzyme stabilize the ground-state ternary complex of the enzymic synthesis of beta-cellobiose by 2.3 and 0.4 kcal/mol, respectively, and assist the precise positioning of beta-D-glucose for catalysis. | lld:pubmed |
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| pubmed-article:11042119 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11042119 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11042119 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11042119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11042119 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11042119 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11042119 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:11042119 | pubmed:author | pubmed-author:AlbertMM | lld:pubmed |
| pubmed-article:11042119 | pubmed:author | pubmed-author:LiJ GJG | lld:pubmed |
| pubmed-article:11042119 | pubmed:author | pubmed-author:NidetzkyBB | lld:pubmed |
| pubmed-article:11042119 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11042119 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:11042119 | pubmed:volume | 351 Pt 3 | lld:pubmed |
| pubmed-article:11042119 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11042119 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11042119 | pubmed:pagination | 649-59 | lld:pubmed |
| pubmed-article:11042119 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11042119 | pubmed:meshHeading | pubmed-meshheading:11042119... | lld:pubmed |
| pubmed-article:11042119 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11042119 | pubmed:articleTitle | Role of non-covalent enzyme-substrate interactions in the reaction catalysed by cellobiose phosphorylase from Cellulomonas uda. | lld:pubmed |
| pubmed-article:11042119 | pubmed:affiliation | Institute of Food Technology, University of Agricultural Sciences (BOKU), Muthgasse 18, A-1190 Vienna, Austria. nide@edv2.boku.ac.at | lld:pubmed |
| pubmed-article:11042119 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11042119 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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