Source:http://linkedlifedata.com/resource/pubmed/id/16661826
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2010-6-29
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pubmed:abstractText |
Studies of ribulose-1,5-bisphosphate (RuBP) carboxylase from taxonomically diverse plants show that the enzyme from C(3) and crassulacean acid metabolism pathway species exhibits lower K(m)(CO(2)) values (12-25 micromolar) than does that from C(4) species (28-34 micromolar). RuBP carboxylase from aquatic angiosperms, an aquatic bryophyte, fresh water and marine algae has yielded consistently high K(m)(CO(2)) values (30-70 micromolar), similar in range to that of the enzyme from C(4) terrestrial plants. This variation in K(m)(CO(2)) is discussed in relation to the correlation between the existence of CO(2)-concentrating mechanisms for photosynthesis and the affinity of the enzyme for CO(2). The K(m)(RuBP) of the enzyme from various sources ranges from 10 to 136 micromolar; mean +/- sd = 36 +/- 20 micromolar. This variation in K(m)(RuBP) does not correlate with different photosynthetic pathways, but shows taxonomic patterns. Among the dicotyledons, the enzyme from crassinucellate species exhibits lower K(m)(RuBP) (18 +/- 4 micromolar) than does that from tenuinucellate species (25 +/- 7 micromolar). Among the Poaceae, RuBP carboxylase from Triticeae, chloridoids, andropogonoids, Microlaena, and Tetrarrhena has yielded lower K(m)(RuBP) values (29 +/- 11 micromolar) than has that from other members of the grass family (46 +/- 10 micromolar).
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661826-13785321,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661826-16659762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661826-16661220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661826-16661446,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661826-16661586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661826-464606,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16661826-6772105
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pubmed:language |
eng
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pubmed:journal | |
pubmed:status |
PubMed-not-MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0032-0889
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
67
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1151-5
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pubmed:dateRevised |
2010-9-15
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pubmed:year |
1981
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pubmed:articleTitle |
Variations in Kinetic Properties of Ribulose-1,5-bisphosphate Carboxylases among Plants.
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pubmed:affiliation |
Research School of Biological Sciences, The Australian National University, P.O. Box 475, Canberra City 2601 Australia.
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pubmed:publicationType |
Journal Article
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