| pubmed-article:16229482 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16229482 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:16229482 | lifeskim:mentions | umls-concept:C0061510 | lld:lifeskim |
| pubmed-article:16229482 | lifeskim:mentions | umls-concept:C0033727 | lld:lifeskim |
| pubmed-article:16229482 | lifeskim:mentions | umls-concept:C0178812 | lld:lifeskim |
| pubmed-article:16229482 | lifeskim:mentions | umls-concept:C1709305 | lld:lifeskim |
| pubmed-article:16229482 | lifeskim:mentions | umls-concept:C0056530 | lld:lifeskim |
| pubmed-article:16229482 | pubmed:issue | 42 | lld:pubmed |
| pubmed-article:16229482 | pubmed:dateCreated | 2005-10-18 | lld:pubmed |
| pubmed-article:16229482 | pubmed:abstractText | The protonation of crotonyl-CoA dienolate following decarboxylation of glutaconyl-CoA by glutaryl-CoA dehydrogenase was investigated. Although it is generally held that the active sites of acyl-CoA dehydrogenases are desolvated when substrate binds, recent evidence has established that water has access to the active site in these binary complexes of glutaryl-CoA dehydrogenase. The present investigation shows that the dehydrogenase catalyzes (a) a rapid exchange of C-4 methyl protons of crotonyl-CoA with bulk solvent and (b) protonation of crotonyl-CoA dienolate by solvent-derived protons under single turnover conditions. Both of the reactions require the catalytic base, Glu370. These findings indicate that decarboxylation proceeds via a dienolate intermediate. The involvement of water in catalysis by glutaryl-CoA dehydrogenase was previously unrecognized and is in conflict with a classically held intramolecular 1,3-prototropic shift for protonation of crotonyl-CoA dienolate. | lld:pubmed |
| pubmed-article:16229482 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16229482 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16229482 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16229482 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16229482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16229482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16229482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16229482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16229482 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16229482 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16229482 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:16229482 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:16229482 | pubmed:author | pubmed-author:RaoK... | lld:pubmed |
| pubmed-article:16229482 | pubmed:author | pubmed-author:Vander... | lld:pubmed |
| pubmed-article:16229482 | pubmed:author | pubmed-author:FrermanFrank... | lld:pubmed |
| pubmed-article:16229482 | pubmed:author | pubmed-author:JonesDavid... | lld:pubmed |
| pubmed-article:16229482 | pubmed:author | pubmed-author:AlbroMarkM | lld:pubmed |
| pubmed-article:16229482 | pubmed:author | pubmed-author:ZirrolliJosep... | lld:pubmed |
| pubmed-article:16229482 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16229482 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:16229482 | pubmed:volume | 44 | lld:pubmed |
| pubmed-article:16229482 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16229482 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16229482 | pubmed:pagination | 13932-40 | lld:pubmed |
| pubmed-article:16229482 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:16229482 | pubmed:meshHeading | pubmed-meshheading:16229482... | lld:pubmed |
| pubmed-article:16229482 | pubmed:meshHeading | pubmed-meshheading:16229482... | lld:pubmed |
| pubmed-article:16229482 | pubmed:meshHeading | pubmed-meshheading:16229482... | lld:pubmed |
| pubmed-article:16229482 | pubmed:meshHeading | pubmed-meshheading:16229482... | lld:pubmed |
| pubmed-article:16229482 | pubmed:meshHeading | pubmed-meshheading:16229482... | lld:pubmed |
| pubmed-article:16229482 | pubmed:meshHeading | pubmed-meshheading:16229482... | lld:pubmed |
| pubmed-article:16229482 | pubmed:meshHeading | pubmed-meshheading:16229482... | lld:pubmed |
| pubmed-article:16229482 | pubmed:meshHeading | pubmed-meshheading:16229482... | lld:pubmed |
| pubmed-article:16229482 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16229482 | pubmed:articleTitle | Protonation of crotonyl-CoA dienolate by human glutaryl-CoA dehydrogenase occurs by solvent-derived protons. | lld:pubmed |
| pubmed-article:16229482 | pubmed:affiliation | Department of Pediatrics, University of Colorado Health Sciences Center, Aurora, Colorado 80010, USA. | lld:pubmed |
| pubmed-article:16229482 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16229482 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16229482 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
