| pubmed-article:3041592 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3041592 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:3041592 | lifeskim:mentions | umls-concept:C0080103 | lld:lifeskim |
| pubmed-article:3041592 | lifeskim:mentions | umls-concept:C0004006 | lld:lifeskim |
| pubmed-article:3041592 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:3041592 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:3041592 | pubmed:issue | 4866 | lld:pubmed |
| pubmed-article:3041592 | pubmed:dateCreated | 1988-9-8 | lld:pubmed |
| pubmed-article:3041592 | pubmed:abstractText | The x-ray structures of the allosteric enzyme aspartate transcarbamylase from Escherichia coli have been solved and refined for both allosteric forms. The T form was determined in the presence of the heterotropic inhibitor cytidine triphosphate, CTP, while the R form was determined in the presence of the bisubstrate analog N-phosphonacetyl-L-aspartate. These two x-ray structures provide the starting point for an understanding of how allosteric enzymes are able to control the rates of metabolic pathways. Insights into the mechanisms of both catalysis and homotropic cooperativity have been obtained by using site-directed mutagenesis to probe residues thought to be critical to the function of the enzyme based on these x-ray structures. | lld:pubmed |
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| pubmed-article:3041592 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3041592 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3041592 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3041592 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3041592 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3041592 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:3041592 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:3041592 | pubmed:author | pubmed-author:LipscombW NWN | lld:pubmed |
| pubmed-article:3041592 | pubmed:author | pubmed-author:KantrowitzE... | lld:pubmed |
| pubmed-article:3041592 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3041592 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:3041592 | pubmed:volume | 241 | lld:pubmed |
| pubmed-article:3041592 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3041592 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3041592 | pubmed:pagination | 669-74 | lld:pubmed |
| pubmed-article:3041592 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:3041592 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3041592 | pubmed:articleTitle | Escherichia coli aspartate transcarbamylase: the relation between structure and function. | lld:pubmed |
| pubmed-article:3041592 | pubmed:affiliation | Department of Chemistry, Boston College, MA 02167. | lld:pubmed |
| pubmed-article:3041592 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3041592 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3041592 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:3041592 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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