| pubmed-article:15983 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15983 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:15983 | lifeskim:mentions | umls-concept:C0011155 | lld:lifeskim |
| pubmed-article:15983 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:15983 | lifeskim:mentions | umls-concept:C0085845 | lld:lifeskim |
| pubmed-article:15983 | lifeskim:mentions | umls-concept:C0052397 | lld:lifeskim |
| pubmed-article:15983 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15983 | pubmed:dateCreated | 1977-6-22 | lld:pubmed |
| pubmed-article:15983 | pubmed:abstractText | Two new mutations are described which, together, eliminate essentially all the aminotransferase activity required for de novo biosynthesis of tyrosine, phenylalanine, and aspartic acid in a K-12 strain of Escherichia coli. One mutation, designated tyrB, lies at about 80 min on the E. coli map and inactivates the "tyrosine-repressible" tyrosine/phenylalanine aminotransferase. The second mutation, aspC, maps at about 20 min and inactivates a nonrespressible aspartate aminotransferase that also has activity on the aromatic amino acids. In ilvE- strains, which lack the branched-chain amino acid aminotransferase, the presence of either the tyrosine-repressible aminotransferase or the aspartate aminotransferase is sufficient for growth in the absence of exogenous tyrosine, phenylalanine, or aspartate; the tyrosine-repressible enzyme is also active in leucine biosynthesis. The ilvE gene product alone can reverse a phenylalanine requirement. Biochemical studies on extracts of strains carrying combinations of these aminotransferase mutations confirm the existence of two distinct enzymes with overlapping specificities for the alpha-keto acid analogues of tyrosine, phenylalanine, and aspartate. These enzymes can be distinguished by electrophoretic mobilities, by kinetic parameters using various substrates, and by a difference in tyrosine repressibility. In extracts of an ilvE- tyrB- aspC- triple mutant, no aminotransferase activity for the alpha-keto acids of tyrosine, phenylalanine, or aspartate could be detected. | lld:pubmed |
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| pubmed-article:15983 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15983 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15983 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15983 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15983 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15983 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:15983 | pubmed:author | pubmed-author:SteinbergR... | lld:pubmed |
| pubmed-article:15983 | pubmed:author | pubmed-author:GelfandD HDH | lld:pubmed |
| pubmed-article:15983 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15983 | pubmed:volume | 130 | lld:pubmed |
| pubmed-article:15983 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15983 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15983 | pubmed:pagination | 429-40 | lld:pubmed |
| pubmed-article:15983 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15983 | pubmed:year | 1977 | lld:pubmed |
| pubmed-article:15983 | pubmed:articleTitle | Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases. | lld:pubmed |
| pubmed-article:15983 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15983 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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