Linked Life Data

16661826

Source:http://linkedlifedata.com/resource/pubmed/id/16661826

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pubmed-article:16661826pubmed:dateCreated2010-6-29lld:pubmed
pubmed-article:16661826pubmed:abstractTextStudies 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).lld:pubmed
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pubmed-article:16661826pubmed:authorpubmed-author:BadgerM RMRlld:pubmed
pubmed-article:16661826pubmed:authorpubmed-author:WatsonLLlld:pubmed
pubmed-article:16661826pubmed:authorpubmed-author:YeohH HHHlld:pubmed
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pubmed-article:16661826pubmed:volume67lld:pubmed
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pubmed-article:16661826pubmed:authorsCompleteYlld:pubmed
pubmed-article:16661826pubmed:pagination1151-5lld:pubmed
pubmed-article:16661826pubmed:dateRevised2010-9-15lld:pubmed
pubmed-article:16661826pubmed:year1981lld:pubmed
pubmed-article:16661826pubmed:articleTitleVariations in Kinetic Properties of Ribulose-1,5-bisphosphate Carboxylases among Plants.lld:pubmed
pubmed-article:16661826pubmed:affiliationResearch School of Biological Sciences, The Australian National University, P.O. Box 475, Canberra City 2601 Australia.lld:pubmed
pubmed-article:16661826pubmed:publicationTypeJournal Articlelld:pubmed
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