| pubmed-article:7664122 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7664122 | lifeskim:mentions | umls-concept:C0041487 | lld:lifeskim |
| pubmed-article:7664122 | lifeskim:mentions | umls-concept:C0038592 | lld:lifeskim |
| pubmed-article:7664122 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:7664122 | pubmed:dateCreated | 1995-10-12 | lld:pubmed |
| pubmed-article:7664122 | pubmed:abstractText | Mutation of six residues of Escherichia coli aspartate aminotransferase results in substantial acquisition of the transamination properties of tyrosine amino-transferase without loss of aspartate transaminase activity. X-ray crystallographic analysis of key inhibitor complexes of the hexamutant reveals the structural basis for this substrate selectivity. It appears that tyrosine aminotransferase achieves nearly equal affinities for a wide range of amino acids by an unusual conformational switch. An active-site arginine residue either shifts its position to electrostatically interact with charged substrates or moves aside to allow access of aromatic ligands. | lld:pubmed |
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| pubmed-article:7664122 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7664122 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7664122 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7664122 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7664122 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:7664122 | pubmed:issn | 1072-8368 | lld:pubmed |
| pubmed-article:7664122 | pubmed:author | pubmed-author:KirschJ FJF | lld:pubmed |
| pubmed-article:7664122 | pubmed:author | pubmed-author:JansoniusJ... | lld:pubmed |
| pubmed-article:7664122 | pubmed:author | pubmed-author:OnufferJ JJJ | lld:pubmed |
| pubmed-article:7664122 | pubmed:author | pubmed-author:MalashkevichV... | lld:pubmed |
| pubmed-article:7664122 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7664122 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:7664122 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7664122 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7664122 | pubmed:pagination | 548-53 | lld:pubmed |
| pubmed-article:7664122 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:7664122 | pubmed:meshHeading | pubmed-meshheading:7664122-... | lld:pubmed |
| pubmed-article:7664122 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7664122 | pubmed:articleTitle | Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase. | lld:pubmed |
| pubmed-article:7664122 | pubmed:affiliation | Department of Structural Biology, University of Basel, Switzerland. | lld:pubmed |
| pubmed-article:7664122 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7664122 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7664122 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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