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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1995-4-13
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pubmed:databankReference |
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-1331067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-14018314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-1701430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-1720862,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-1993674,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-2183002,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-238534,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-2671940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-3060853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-3549457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-4590472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-4965256,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-6434512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-6986370,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-6988403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-7993080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-8226637,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7883719-8285716
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9193
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
177
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1620-3
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7883719-Base Sequence,
pubmed-meshheading:7883719-Binding Sites,
pubmed-meshheading:7883719-Carboxy-Lyases,
pubmed-meshheading:7883719-Decarboxylation,
pubmed-meshheading:7883719-Escherichia coli,
pubmed-meshheading:7883719-Models, Biological,
pubmed-meshheading:7883719-Molecular Sequence Data,
pubmed-meshheading:7883719-Oxaloacetates,
pubmed-meshheading:7883719-Oxaloacetic Acids,
pubmed-meshheading:7883719-Phosphoenolpyruvate Carboxykinase (GTP),
pubmed-meshheading:7883719-Point Mutation,
pubmed-meshheading:7883719-Sequence Homology, Nucleic Acid,
pubmed-meshheading:7883719-Structure-Activity Relationship,
pubmed-meshheading:7883719-Substrate Specificity
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pubmed:year |
1995
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pubmed:articleTitle |
A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring oxaloacetate decarboxylase activity.
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pubmed:affiliation |
Department of Chemical Engineering, Texas A&M University, College Station 77843-3122.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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