pubmed-article:1540130 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1540130 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:1540130 | lifeskim:mentions | umls-concept:C0005220 | lld:lifeskim |
pubmed-article:1540130 | lifeskim:mentions | umls-concept:C0015219 | lld:lifeskim |
pubmed-article:1540130 | lifeskim:mentions | umls-concept:C0525038 | lld:lifeskim |
pubmed-article:1540130 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
pubmed-article:1540130 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
pubmed-article:1540130 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:1540130 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:1540130 | lifeskim:mentions | umls-concept:C1517004 | lld:lifeskim |
pubmed-article:1540130 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
pubmed-article:1540130 | lifeskim:mentions | umls-concept:C0686907 | lld:lifeskim |
pubmed-article:1540130 | pubmed:dateCreated | 1992-3-31 | lld:pubmed |
pubmed-article:1540130 | pubmed:abstractText | 1. The ratio of ebgA-gene product of ebgC-gene product in the functional aggregate of ebg beta-galactosidases was determined to be 1:1 by isolation of the enzyme from bacteria grown on uniformly radiolabelled amino acids and separation of the subunits by gel-permeation chromatography under denaturing conditions. 2. This datum, taken together with a recalculation of the previous ultracentrifuge data [Hall (1976) J. Mol. Biol. 107, 71-84], analytical gel-permeation chromatography and electron microscopy, strongly suggests an alpha 4 beta 4 quaternary structure for the enzyme. 3. The second chemical step in the enzyme turnover sequence, hydrolysis of the galactosyl-enzyme intermediate, is markedly slower for ebgab, having both Asp-97----Asn and Trp-977----Cys changes in the large subunit, than for ebga (having only the first change) and ebgb (having only the second), and is so slow as to be rate-determining even for an S-glycoside, beta-D-galactopyranosyl thiopicrate, as is shown by nucleophilic competition with methanol. 4. The selectivity of galactosyl-ebgab between water and methanol on a molar basis is 57, similar to the value for galactosyl-ebgb. 5. The equilibrium constant for the hydrolysis of lactose at 37 degrees C is 152 +/- 19 M, that for hydrolysis of allolactose is approx. 44 M and that for hydrolysis of lactulose is approx. 40 M. 6. A comparison of the free-energy profiles for the hydrolyses of lactose catalysed by the double mutant with those for the wild-type and the single mutants reveals that free-energy changes from the two mutations are not in general independently additive, but that the changes generally are in the direction predicted by the theory of Burbaum, Raines, Albery & Knowles [(1989) Biochemistry 28, 9283-9305] for an enzyme catalysing a thermodynamically irreversible reaction. 7. Michaelis-Menten parameters for the hydrolysis of six beta-D-galactopyranosylpyridinium ions and ten aryl beta-galactosides by ebgab were measured. 8. The derived beta 1g values are the same as those for ebgb (which has only the Trp-977----Cys change) and significantly different from those for ebgo (the wild-type enzyme) and ebga. 9. The alpha- and beta-deuterium secondary isotope effects on the hydrolysis of the galactosyl-enzyme of 1.08 and 1.00 are difficult to reconcile with the pyranose ring in this intermediate being in the 4C1 conformation. | lld:pubmed |
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pubmed-article:1540130 | pubmed:language | eng | lld:pubmed |
pubmed-article:1540130 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1540130 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1540130 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1540130 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1540130 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1540130 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1540130 | pubmed:month | Feb | lld:pubmed |
pubmed-article:1540130 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:1540130 | pubmed:author | pubmed-author:GuyPP | lld:pubmed |
pubmed-article:1540130 | pubmed:author | pubmed-author:SinnottM LML | lld:pubmed |
pubmed-article:1540130 | pubmed:author | pubmed-author:SmithP JPJ | lld:pubmed |
pubmed-article:1540130 | pubmed:author | pubmed-author:HallB GBG | lld:pubmed |
pubmed-article:1540130 | pubmed:author | pubmed-author:AYY | lld:pubmed |
pubmed-article:1540130 | pubmed:author | pubmed-author:ZhangYY | lld:pubmed |
pubmed-article:1540130 | pubmed:author | pubmed-author:ElliottA CAC | lld:pubmed |
pubmed-article:1540130 | pubmed:author | pubmed-author:BommuswamyJJ | lld:pubmed |
pubmed-article:1540130 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1540130 | pubmed:day | 15 | lld:pubmed |
pubmed-article:1540130 | pubmed:volume | 282 ( Pt 1) | lld:pubmed |
pubmed-article:1540130 | pubmed:geneSymbol | ebgA | lld:pubmed |
pubmed-article:1540130 | pubmed:geneSymbol | ebgC | lld:pubmed |
pubmed-article:1540130 | pubmed:geneSymbol | ebg | lld:pubmed |
pubmed-article:1540130 | pubmed:geneSymbol | ebg<up>ab</up> | lld:pubmed |
pubmed-article:1540130 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1540130 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1540130 | pubmed:pagination | 155-64 | lld:pubmed |
pubmed-article:1540130 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
pubmed-article:1540130 | pubmed:meshHeading | pubmed-meshheading:1540130-... | lld:pubmed |
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pubmed-article:1540130 | pubmed:meshHeading | pubmed-meshheading:1540130-... | lld:pubmed |
pubmed-article:1540130 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1540130 | pubmed:articleTitle | The catalytic consequences of experimental evolution. Studies on the subunit structure of the second (ebg) beta-galactosidase of Escherichia coli, and on catalysis by ebgab, an experimental evolvant containing two amino acid substitutions. | lld:pubmed |
pubmed-article:1540130 | pubmed:affiliation | Department of Organic Chemistry, University of Bristol, U.K. | lld:pubmed |
pubmed-article:1540130 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1540130 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:1540130 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
literatureCitation:129_1540... | literatureCitation:pubmed | pubmed-article:1540130 | lld:drugbank |
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