| pubmed-article:12590598 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12590598 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:12590598 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:12590598 | lifeskim:mentions | umls-concept:C0386636 | lld:lifeskim |
| pubmed-article:12590598 | lifeskim:mentions | umls-concept:C0060447 | lld:lifeskim |
| pubmed-article:12590598 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:12590598 | pubmed:dateCreated | 2003-2-19 | lld:pubmed |
| pubmed-article:12590598 | pubmed:abstractText | UDP-galactopyranose mutase is a flavoprotein which catalyses the interconversion of UDP-galactopyranose and UDP-galactofuranose. The enzyme is of interest because it provides the activated biosynthetic precursor of galactofuranose, a key cell wall component of many bacterial pathogens. The reaction mechanism of this mutase is intriguing because the anomeric oxygen forms a glycosidic bond, which means that the reaction must proceed by a novel mechanism involving ring breakage and closure. The structure of the enzyme is known, but the mechanism, although speculated on, is not resolved. The overall reaction is electrically neutral but a crypto-redox reaction is suggested by the requirement that the flavin must adopt the reduced form for activity. Herein we report a thermodynamic analysis of the enzyme's flavin cofactor with the objective of defining the system and setting parameters for possible reaction schemes. The analysis shows that the neutral semiquinone (FADH(*)) is stabilized in the presence of substrate and the fully reduced flavin is the anionic FADH(-) rather than the neutral FADH(2). The anionic FADH(-) has the potential to act as a rapid 1-electron donor/acceptor without being slowed by a coupled proton transfer and is therefore an ideal crypto-redox cofactor. | lld:pubmed |
| pubmed-article:12590598 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12590598 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12590598 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12590598 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12590598 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12590598 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12590598 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12590598 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12590598 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12590598 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12590598 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12590598 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12590598 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12590598 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12590598 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:12590598 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:12590598 | pubmed:author | pubmed-author:NaismithJames... | lld:pubmed |
| pubmed-article:12590598 | pubmed:author | pubmed-author:WhitfieldChri... | lld:pubmed |
| pubmed-article:12590598 | pubmed:author | pubmed-author:ChapmanStephe... | lld:pubmed |
| pubmed-article:12590598 | pubmed:author | pubmed-author:DaffSimonS | lld:pubmed |
| pubmed-article:12590598 | pubmed:author | pubmed-author:IngledewW... | lld:pubmed |
| pubmed-article:12590598 | pubmed:author | pubmed-author:FullertonStep... | lld:pubmed |
| pubmed-article:12590598 | pubmed:author | pubmed-author:SandersDavid... | lld:pubmed |
| pubmed-article:12590598 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12590598 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:12590598 | pubmed:volume | 42 | lld:pubmed |
| pubmed-article:12590598 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12590598 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12590598 | pubmed:pagination | 2104-9 | lld:pubmed |
| pubmed-article:12590598 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:12590598 | pubmed:meshHeading | pubmed-meshheading:12590598... | lld:pubmed |
| pubmed-article:12590598 | pubmed:meshHeading | pubmed-meshheading:12590598... | lld:pubmed |
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| pubmed-article:12590598 | pubmed:meshHeading | pubmed-meshheading:12590598... | lld:pubmed |
| pubmed-article:12590598 | pubmed:meshHeading | pubmed-meshheading:12590598... | lld:pubmed |
| pubmed-article:12590598 | pubmed:meshHeading | pubmed-meshheading:12590598... | lld:pubmed |
| pubmed-article:12590598 | pubmed:meshHeading | pubmed-meshheading:12590598... | lld:pubmed |
| pubmed-article:12590598 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12590598 | pubmed:articleTitle | Potentiometric analysis of UDP-galactopyranose mutase: stabilization of the flavosemiquinone by substrate. | lld:pubmed |
| pubmed-article:12590598 | pubmed:affiliation | Centre for Biomolecular Sciences, The University, St. Andrews KY16 9ST, UK. | lld:pubmed |
| pubmed-article:12590598 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12590598 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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