Reduced CO2/O2 specificity of ribulose-bisphosphate carboxylase/oxygenase in a temperature-sensitive chloroplast mutant of Chlamydomonas.
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Highly conserved small subunit residues influence rubisco large subunit catalysis.Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal RubiscoSubstitutions at the Asp-473 latch residue of chlamydomonas ribulosebisphosphate carboxylase/oxygenase cause decreases in carboxylation efficiency and CO(2)/O(2) specificity.Assessment of structural and functional divergence far from the large subunit active site of ribulose-1,5-bisphosphate carboxylase/oxygenase.Complementing substitutions at the bottom of the barrel influence catalysis and stability of ribulose-bisphosphate carboxylase/oxygenase.Plant-like substitutions in the large-subunit carboxy terminus of Chlamydomonas Rubisco increase CO2/O2 specificity.Disruption of the plastid ycf10 open reading frame affects uptake of inorganic carbon in the chloroplast of Chlamydomonas.Functional hybrid rubisco enzymes with plant small subunits and algal large subunits: engineered rbcS cDNA for expression in chlamydomonas.RbcS suppressor mutations improve the thermal stability and CO2/O2 specificity of rbcL- mutant ribulose-1,5-bisphosphate carboxylase/oxygenase.Elimination of the Chlamydomonas gene family that encodes the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenaseA survey of oxidative paracatalytic reactions catalyzed by enzymes that generate carbanionic intermediates: implications for ROS production, cancer etiology, and neurodegenerative diseases.A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.The CO2 concentrating mechanism and photosynthetic carbon assimilation in limiting CO2 : how Chlamydomonas works against the gradient.Synthetic CO2-fixation enzyme cascades immobilized on self-assembled nanostructures that enhance CO2/O2 selectivity of RubisCOLeucine 332 influences the CO2/O2 specificity factor of ribulose-1,5-bisphosphate carboxylase/oxygenase from Anacystis nidulans.Deletion of nine carboxy-terminal residues of the Rubisco small subunit decreases thermal stability but does not eliminate function.Substitutions at the opening of the Rubisco central solvent channel affect holoenzyme stability and CO2/O 2 specificity but not activation by Rubisco activase.Activation of interspecies-hybrid Rubisco enzymes to assess different models for the Rubisco-Rubisco activase interaction.What physiological acclimation supports increased growth at high CO2 conditions?
P2860
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P2860
Reduced CO2/O2 specificity of ribulose-bisphosphate carboxylase/oxygenase in a temperature-sensitive chloroplast mutant of Chlamydomonas.
description
1988 nî lūn-bûn
@nan
1988 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Reduced CO2/O2 specificity of ...... plast mutant of Chlamydomonas.
@ast
Reduced CO2/O2 specificity of ...... plast mutant of Chlamydomonas.
@en
Reduced CO2/O2 specificity of ...... plast mutant of Chlamydomonas.
@nl
type
label
Reduced CO2/O2 specificity of ...... plast mutant of Chlamydomonas.
@ast
Reduced CO2/O2 specificity of ...... plast mutant of Chlamydomonas.
@en
Reduced CO2/O2 specificity of ...... plast mutant of Chlamydomonas.
@nl
prefLabel
Reduced CO2/O2 specificity of ...... plast mutant of Chlamydomonas.
@ast
Reduced CO2/O2 specificity of ...... plast mutant of Chlamydomonas.
@en
Reduced CO2/O2 specificity of ...... plast mutant of Chlamydomonas.
@nl
P2093
P2860
P356
P1476
Reduced CO2/O2 specificity of ...... plast mutant of Chlamydomonas.
@en
P2093
Al-Abed SR
Chastain CJ
Spreitzer RJ
P2860
P304
P356
10.1073/PNAS.85.13.4696
P407
P577
1988-07-01T00:00:00Z