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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2008-8-29
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pubmed:abstractText |
Ribulose-1,5-bisphosphate is the rate-limiting enzyme in photosynthesis. The catalytic large subunit of the green-algal enzyme from Chlamydomonas reinhardtii is approxiamtely 90% identical to the flowering-plant sequences, although they confer diverse kinetic properties. To identify the regions that may account for species variation in kinetic properties, directed mutagenesis and chloroplast transformation were used to create four amino-acid substitutions in the carboxy terminus of the Chlamydomonas large subunit to mimic the sequence of higher-specificity plant enzymes.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-10779514,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-10801357,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-11011141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-11641402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-12221984,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-12781764,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-12781765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-14506244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-14734540,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-16026157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-16282373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-16658951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-16661654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-16661715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-17274986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-3133659,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-8172885,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-8245022,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-8307949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-8463309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18664299-8648644
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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:issn |
1471-2229
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
85
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pubmed:dateRevised |
2010-9-22
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pubmed:meshHeading |
pubmed-meshheading:18664299-Amino Acid Substitution,
pubmed-meshheading:18664299-Animals,
pubmed-meshheading:18664299-Carbon Dioxide,
pubmed-meshheading:18664299-Chlamydomonas,
pubmed-meshheading:18664299-Enzyme Stability,
pubmed-meshheading:18664299-Holoenzymes,
pubmed-meshheading:18664299-Kinetics,
pubmed-meshheading:18664299-Mutant Proteins,
pubmed-meshheading:18664299-Mutation,
pubmed-meshheading:18664299-Oxygen,
pubmed-meshheading:18664299-Phenotype,
pubmed-meshheading:18664299-Plants,
pubmed-meshheading:18664299-Protein Structure, Secondary,
pubmed-meshheading:18664299-Protein Subunits,
pubmed-meshheading:18664299-Ribulose-Bisphosphate Carboxylase,
pubmed-meshheading:18664299-Structure-Activity Relationship
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pubmed:year |
2008
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pubmed:articleTitle |
Plant-like substitutions in the large-subunit carboxy terminus of Chlamydomonas Rubisco increase CO2/O2 specificity.
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pubmed:affiliation |
Department of Microbiology, Ohio State University, Columbus, OH 43210, USA. satagopan.1@osu.edu
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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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