| pubmed-article:11749542 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11749542 | lifeskim:mentions | umls-concept:C0007054 | lld:lifeskim |
| pubmed-article:11749542 | lifeskim:mentions | umls-concept:C0069660 | lld:lifeskim |
| pubmed-article:11749542 | lifeskim:mentions | umls-concept:C0681841 | lld:lifeskim |
| pubmed-article:11749542 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:11749542 | lifeskim:mentions | umls-concept:C1523987 | lld:lifeskim |
| pubmed-article:11749542 | pubmed:issue | 51 | lld:pubmed |
| pubmed-article:11749542 | pubmed:dateCreated | 2001-12-25 | lld:pubmed |
| pubmed-article:11749542 | pubmed:abstractText | Orotidine 5'-phosphate decarboxylase (ODCase) is the most proficient enzyme known, enhancing the rate of decarboxylation of orotidine 5'-phosphate (OMP) by a factor of 10(17), which corresponds to a DeltaDeltaG++ of approximately 24 kcal/mol. Ground-state destabilization through local electrostatic stress has been recently proposed as the basis of catalytic rate enhancement for a mechanism that is the same as in solution. We have carried out gas-phase ab initio quantum mechanical calculations combined with a free energy method, a continuum solvent model, and molecular dynamics simulations to assess an alternative mechanism. Although we are not able to reproduce the experimentally observed DeltaDeltaG++ quantitatively, we present evidence that this DeltaDeltaG++ is very large, in the range found experimentally. We thus conclude that the preferred mechanism may well be different from that in solution, involving an equilibrium pre-protonation of OMP C5 by a catalytic lysine residue that greatly reduces the barrier to subsequent decarboxylation. | lld:pubmed |
| pubmed-article:11749542 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11749542 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11749542 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11749542 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11749542 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11749542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11749542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11749542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11749542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11749542 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11749542 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11749542 | pubmed:issn | 0002-7863 | lld:pubmed |
| pubmed-article:11749542 | pubmed:author | pubmed-author:KollmanP APA | lld:pubmed |
| pubmed-article:11749542 | pubmed:author | pubmed-author:LeeT STS | lld:pubmed |
| pubmed-article:11749542 | pubmed:author | pubmed-author:ChoderaJ DJD | lld:pubmed |
| pubmed-article:11749542 | pubmed:author | pubmed-author:ChongL TLT | lld:pubmed |
| pubmed-article:11749542 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11749542 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:11749542 | pubmed:volume | 123 | lld:pubmed |
| pubmed-article:11749542 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11749542 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11749542 | pubmed:pagination | 12837-48 | lld:pubmed |
| pubmed-article:11749542 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:11749542 | pubmed:meshHeading | pubmed-meshheading:11749542... | lld:pubmed |
| pubmed-article:11749542 | pubmed:meshHeading | pubmed-meshheading:11749542... | lld:pubmed |
| pubmed-article:11749542 | pubmed:meshHeading | pubmed-meshheading:11749542... | lld:pubmed |
| pubmed-article:11749542 | pubmed:meshHeading | pubmed-meshheading:11749542... | lld:pubmed |
| pubmed-article:11749542 | pubmed:meshHeading | pubmed-meshheading:11749542... | lld:pubmed |
| pubmed-article:11749542 | pubmed:meshHeading | pubmed-meshheading:11749542... | lld:pubmed |
| pubmed-article:11749542 | pubmed:meshHeading | pubmed-meshheading:11749542... | lld:pubmed |
| pubmed-article:11749542 | pubmed:meshHeading | pubmed-meshheading:11749542... | lld:pubmed |
| pubmed-article:11749542 | pubmed:meshHeading | pubmed-meshheading:11749542... | lld:pubmed |
| pubmed-article:11749542 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11749542 | pubmed:articleTitle | An alternative explanation for the catalytic proficiency of orotidine 5'-phosphate decarboxylase. | lld:pubmed |
| pubmed-article:11749542 | pubmed:affiliation | Accelrys, Inc., 9685 Scranton Road, San Diego, California 92121-3752, USA. | lld:pubmed |
| pubmed-article:11749542 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11749542 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11749542 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:11749542 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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