نتایج جستجو برای: rubisco

تعداد نتایج: 1869  

2017
B. Kacar V. Hanson‐Smith Z. R. Adam N. Boekelheide

Ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (RuBisCO, or Rubisco) catalyzes a key reaction by which inorganic carbon is converted into organic carbon in the metabolism of many aerobic and anaerobic organisms. Across the broader Rubisco protein family, homologs exhibit diverse biochemical characteristics and metabolic functions, but the evolutionary origins of this diversity are uncle...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2016
Luke C M Mackinder Moritz T Meyer Tabea Mettler-Altmann Vivian K Chen Madeline C Mitchell Oliver Caspari Elizabeth S Freeman Rosenzweig Leif Pallesen Gregory Reeves Alan Itakura Robyn Roth Frederik Sommer Stefan Geimer Timo Mühlhaus Michael Schroda Ursula Goodenough Mark Stitt Howard Griffiths Martin C Jonikas

Biological carbon fixation is a key step in the global carbon cycle that regulates the atmosphere's composition while producing the food we eat and the fuels we burn. Approximately one-third of global carbon fixation occurs in an overlooked algal organelle called the pyrenoid. The pyrenoid contains the CO2-fixing enzyme Rubisco and enhances carbon fixation by supplying Rubisco with a high conce...

Journal: :AMB Express 2021

Abstract The oxygenase activity of Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) converts ribulose-1,5-bisphosphate (RuBP) into 2-phosphoglycolate, which in turn channels photorespiration, resulting carbon and energy loss higher plants. We observed that glycolate can be accumulated extracellularly when two genes encoding the dehydrogenase cyanobacteria Synechocystis sp. PCC 6803 wer...

Journal: :The Journal of biological chemistry 2010
Todor Genkov Moritz Meyer Howard Griffiths Robert J Spreitzer

There has been much interest in the chloroplast-encoded large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) as a target for engineering an increase in net CO(2) fixation in photosynthesis. Improvements in the enzyme would lead to an increase in the production of food, fiber, and renewable energy. Although the large subunit contains the active site, a family of rbcS nuclea...

Journal: :Plant physiology 2009
Spencer Michael Whitney Heather Jean Kane Robert L Houtz Robert Edward Sharwood

Manipulation of Rubisco within higher plants is complicated by the different genomic locations of the large (L; rbcL) and small (S; RbcS) subunit genes. Although rbcL can be accurately modified by plastome transformation, directed genetic manipulation of the multiple nuclear-encoded RbcS genes is more challenging. Here we demonstrate the viability of linking the S and L subunits of tobacco (Nic...

Journal: :The Journal of biological chemistry 1999
Z Ying R M Mulligan N Janney R L Houtz

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco)is methylated at the alpha-amino group of the N-terminal methionine of the processed form of the small subunit (SS), and at the epsilon-amino group of lysine-14 of the large subunit (LS) in some species. The Rubisco LS methyltransferase (LSMT) gene has been cloned and expressed from pea and specifically methylates lysine-14 of the LS of R...

2009
Spencer Michael Whitney Heather Jean Kane Robert L. Houtz Robert Edward Sharwood

Manipulation of Rubisco within higher plants is complicated by the different genomic locations of the large (L; rbcL) and small (S; RbcS) subunit genes. Although rbcL can be accurately modified by plastome transformation, directed genetic manipulation of the multiple nuclear-encoded RbcS genes is more challenging. Here we demonstrate the viability of linking the S and L subunits of tobacco (Nic...

Journal: :Plant physiology 1989
S Yelle R C Beeson M J Trudel A Gosselin

Lycopersicon esculentum Mill. cv Vedettos and Lycopersicon chmielewskii Rick, LA 1028, were exposed to two CO(2) concentrations (330 or 900 microliters per liter) for 10 weeks. The elevated CO(2) concentrations increased the initial ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activity of both species for the first 5 weeks of treatment but the difference did not persist during the ...

Journal: :Plant physiology 1999
Law Crafts-Brandner

Increasing the leaf temperature of intact cotton (Gossypium hirsutum L.) and wheat (Triticum aestivum L.) plants caused a progressive decline in the light-saturated CO2-exchange rate (CER). CER was more sensitive to increased leaf temperature in wheat than in cotton, and both species demonstrated photosynthetic acclimation when leaf temperature was increased gradually. Inhibition of CER was not...

Journal: :Journal of experimental botany 2008
Spencer M Whitney Robert E Sharwood

The inability to assemble Rubisco from any photosynthetic eukaryote within Escherichia coli has hampered structure-function studies of higher plant Rubisco. Precise genetic manipulation of the tobacco chloroplast genome (plastome) by homologous recombination has facilitated the successful production of transplastomic lines that have either mutated the Rubisco large subunit (L) gene, rbcL, or re...

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