pubmed-article:7556224 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7556224 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
pubmed-article:7556224 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
pubmed-article:7556224 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
pubmed-article:7556224 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
pubmed-article:7556224 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:7556224 | pubmed:dateCreated | 1995-11-14 | lld:pubmed |
pubmed-article:7556224 | pubmed:abstractText | The electron distribution in the coenzyme-substrate adduct of aspartate aminotransferase was changed by replacing active-site Arg386 with alanine and introducing a new arginine residue nearby. [Y225R, R386A]Aspartate aminotransferase decarboxylates L-aspartate to L-alanine (kcat = 0.04 s-1), while its transaminase activity towards dicarboxylic amino acids is decreased by three orders of magnitude (kcat = 0.19 s-1). Molecular-dynamics simulations based on the crystal structure of the mutant enzyme suggest that a new hydrogen bond to the imine N atom of the pyridoxal-5'-phosphate- aspartate adduct and an altered electrostatic potential around its beta-carboxylate group underlie the 650,000-fold increase in the ratio of beta-decarboxylase/transaminase activity. | lld:pubmed |
pubmed-article:7556224 | pubmed:language | eng | lld:pubmed |
pubmed-article:7556224 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7556224 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7556224 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7556224 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7556224 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7556224 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7556224 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7556224 | pubmed:month | Sep | lld:pubmed |
pubmed-article:7556224 | pubmed:issn | 0014-2956 | lld:pubmed |
pubmed-article:7556224 | pubmed:author | pubmed-author:ChristenPP | lld:pubmed |
pubmed-article:7556224 | pubmed:author | pubmed-author:GehringHH | lld:pubmed |
pubmed-article:7556224 | pubmed:author | pubmed-author:BergerPP | lld:pubmed |
pubmed-article:7556224 | pubmed:author | pubmed-author:JansoniusJ... | lld:pubmed |
pubmed-article:7556224 | pubmed:author | pubmed-author:KasperPP | lld:pubmed |
pubmed-article:7556224 | pubmed:author | pubmed-author:GraberRR | lld:pubmed |
pubmed-article:7556224 | pubmed:author | pubmed-author:MalashkevichV... | lld:pubmed |
pubmed-article:7556224 | pubmed:author | pubmed-author:SandmeierEE | lld:pubmed |
pubmed-article:7556224 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7556224 | pubmed:day | 1 | lld:pubmed |
pubmed-article:7556224 | pubmed:volume | 232 | lld:pubmed |
pubmed-article:7556224 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7556224 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7556224 | pubmed:pagination | 686-90 | lld:pubmed |
pubmed-article:7556224 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
pubmed-article:7556224 | pubmed:meshHeading | pubmed-meshheading:7556224-... | lld:pubmed |
pubmed-article:7556224 | pubmed:meshHeading | pubmed-meshheading:7556224-... | lld:pubmed |
pubmed-article:7556224 | pubmed:meshHeading | pubmed-meshheading:7556224-... | lld:pubmed |
pubmed-article:7556224 | pubmed:meshHeading | pubmed-meshheading:7556224-... | lld:pubmed |
pubmed-article:7556224 | pubmed:meshHeading | pubmed-meshheading:7556224-... | lld:pubmed |
pubmed-article:7556224 | pubmed:meshHeading | pubmed-meshheading:7556224-... | lld:pubmed |
pubmed-article:7556224 | pubmed:meshHeading | pubmed-meshheading:7556224-... | lld:pubmed |
pubmed-article:7556224 | pubmed:meshHeading | pubmed-meshheading:7556224-... | lld:pubmed |
pubmed-article:7556224 | pubmed:meshHeading | pubmed-meshheading:7556224-... | lld:pubmed |
pubmed-article:7556224 | pubmed:meshHeading | pubmed-meshheading:7556224-... | lld:pubmed |
pubmed-article:7556224 | pubmed:meshHeading | pubmed-meshheading:7556224-... | lld:pubmed |
pubmed-article:7556224 | pubmed:meshHeading | pubmed-meshheading:7556224-... | lld:pubmed |
pubmed-article:7556224 | pubmed:meshHeading | pubmed-meshheading:7556224-... | lld:pubmed |
pubmed-article:7556224 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7556224 | pubmed:articleTitle | Changing the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme. | lld:pubmed |
pubmed-article:7556224 | pubmed:affiliation | Biochemisches Institut, Universität Zürich, Switzerland. | lld:pubmed |
pubmed-article:7556224 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7556224 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:945553 | entrezgene:pubmed | pubmed-article:7556224 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7556224 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7556224 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7556224 | lld:pubmed |