| pubmed-article:7883719 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7883719 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:7883719 | lifeskim:mentions | umls-concept:C0251211 | lld:lifeskim |
| pubmed-article:7883719 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:7883719 | lifeskim:mentions | umls-concept:C1150836 | lld:lifeskim |
| pubmed-article:7883719 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:7883719 | pubmed:dateCreated | 1995-4-13 | lld:pubmed |
| pubmed-article:7883719 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:abstractText | The phosphoenolpyruvate carboxykinase in Escherichia coli (encoded by pck) catalyzes the conversion from oxaloacetate (OAA) to phosphoenolpyruvate under gluconeogenic conditions. We report here the characterization of two mutant alleles, pck-51 and pck-53, both of which are point mutations leading to single amino acid changes (D to N at position 268 and G to S at position 284, respectively). Pck51 is an altered-activity mutant that catalyzes the conversion from OAA to pyruvate (OAA decarboxylase activity). This new activity was not detected from the wild-type Pck, and it complements the pck null mutation only in a pps+ background. Pck53 is a reduced-activity mutant that complements the pck null mutation in a strain-dependent fashion. | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7883719 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7883719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7883719 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7883719 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7883719 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:7883719 | pubmed:author | pubmed-author:LiaoJ CJC | lld:pubmed |
| pubmed-article:7883719 | pubmed:author | pubmed-author:HouS YSY | lld:pubmed |
| pubmed-article:7883719 | pubmed:author | pubmed-author:ChanY OYO | lld:pubmed |
| pubmed-article:7883719 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7883719 | pubmed:volume | 177 | lld:pubmed |
| pubmed-article:7883719 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7883719 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7883719 | pubmed:pagination | 1620-3 | lld:pubmed |
| pubmed-article:7883719 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:meshHeading | pubmed-meshheading:7883719-... | lld:pubmed |
| pubmed-article:7883719 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7883719 | pubmed:articleTitle | A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring oxaloacetate decarboxylase activity. | lld:pubmed |
| pubmed-article:7883719 | pubmed:affiliation | Department of Chemical Engineering, Texas A&M University, College Station 77843-3122. | lld:pubmed |
| pubmed-article:7883719 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7883719 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:7883719 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:945667 | entrezgene:pubmed | pubmed-article:7883719 | lld:entrezgene |
