| pubmed-article:2013569 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2013569 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:2013569 | lifeskim:mentions | umls-concept:C0814810 | lld:lifeskim |
| pubmed-article:2013569 | lifeskim:mentions | umls-concept:C1150904 | lld:lifeskim |
| pubmed-article:2013569 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:2013569 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:2013569 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:2013569 | pubmed:dateCreated | 1991-5-14 | lld:pubmed |
| pubmed-article:2013569 | pubmed:abstractText | We demonstrate here that Escherichia coli K-12 synthesizes two different L-serine deaminases (L-SD) catalyzing the nonoxidative deamination of L-serine to pyruvate, one coded for by the previously described sdaA gene and a second, hitherto undescribed enzyme which we call L-SD2. A strain carrying a null mutation in sdaA made no detectable L-SD in minimal medium, but had activity in Luria broth. We describe a mutation, sdaX, which affects the regulation of L-SD2 and permits its expression in minimal medium, and an insertion mutation, sdaB, which abolishes L-SD2 activity completely. Both mutations lie near 60.5 min on the E. coli genetic map. The two L-SD enzymes have similar enzyme parameters, and both require posttranslational activation. | lld:pubmed |
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| pubmed-article:2013569 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2013569 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2013569 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2013569 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2013569 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2013569 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2013569 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:2013569 | pubmed:author | pubmed-author:NewmanE BEB | lld:pubmed |
| pubmed-article:2013569 | pubmed:author | pubmed-author:ORRR SRS | lld:pubmed |
| pubmed-article:2013569 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2013569 | pubmed:volume | 173 | lld:pubmed |
| pubmed-article:2013569 | pubmed:geneSymbol | sdaA | lld:pubmed |
| pubmed-article:2013569 | pubmed:geneSymbol | sdaB | lld:pubmed |
| pubmed-article:2013569 | pubmed:geneSymbol | sdaX | lld:pubmed |
| pubmed-article:2013569 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2013569 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2013569 | pubmed:pagination | 2473-80 | lld:pubmed |
| pubmed-article:2013569 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2013569 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:2013569 | pubmed:articleTitle | A novel L-serine deaminase activity in Escherichia coli K-12. | lld:pubmed |
| pubmed-article:2013569 | pubmed:affiliation | Department of Biological Sciences, Concordia University, Montreal, Quebec, Canada. | lld:pubmed |
| pubmed-article:2013569 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2013569 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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