The relationship between side reactions and slow inhibition of ribulose-bisphosphate carboxylase revealed by a loop 6 mutant of the tobacco enzyme.
about
Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimizedRubisco activity and regulation as targets for crop improvementConserved main-chain peptide distortions: A proposed role for Ile203 in catalysis by dihydrodipicolinate synthaseStructure of Arabidopsis thaliana Rubisco activaseSmall oligomers of ribulose-bisphosphate carboxylase/oxygenase (Rubisco) activase are required for biological activity.Development of an activity-directed selection system enabled significant improvement of the carboxylation efficiency of RubiscoCatalytic by-product formation and ligand binding by ribulose bisphosphate carboxylases from different phylogenies.Protein oligomerization monitored by fluorescence fluctuation spectroscopy: self-assembly of rubisco activase.Improved analysis of C4 and C3 photosynthesis via refined in vitro assays of their carbon fixation biochemistryA RuBisCO-mediated carbon metabolic pathway in methanogenic archaea.Maintaining photosynthetic CO2 fixation via protein remodelling: the Rubisco activases.Optimizing Rubisco and its regulation for greater resource use efficiency.The drug-target residence time model: a 10-year retrospective.Rubisco activities, properties, and regulation in three different C4 grasses under drought.The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites.Leaf proteome alterations in the context of physiological and morphological responses to drought and heat stress in barley (Hordeum vulgare L.).Conformational adaptation in drug-target interactions and residence time.Construction of a tobacco master line to improve Rubisco engineering in chloroplasts.Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase: product inhibition, cooperativity, and magnesium activation.Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria.Slow deactivation of ribulose 1,5-bisphosphate carboxylase/oxygenase elucidated by mathematical models.Oxygen-dependent H2O2 production by Rubisco.Metabolic fluxes in an illuminated Arabidopsis rosette.Differences in carbon isotope discrimination of three variants of D-ribulose-1,5-bisphosphate carboxylase/oxygenase reflect differences in their catalytic mechanisms.Surveying the expanding prokaryotic Rubisco multiverse.Activation of interspecies-hybrid Rubisco enzymes to assess different models for the Rubisco-Rubisco activase interaction.Down-regulation of Rubisco activity under combined increases of CO2 and temperature minimized by changes in Rubisco kcat in wheat
P2860
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P2860
The relationship between side reactions and slow inhibition of ribulose-bisphosphate carboxylase revealed by a loop 6 mutant of the tobacco enzyme.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh
2003年學術文章
@zh-hant
name
The relationship between side ...... mutant of the tobacco enzyme.
@en
The relationship between side ...... mutant of the tobacco enzyme.
@nl
type
label
The relationship between side ...... mutant of the tobacco enzyme.
@en
The relationship between side ...... mutant of the tobacco enzyme.
@nl
prefLabel
The relationship between side ...... mutant of the tobacco enzyme.
@en
The relationship between side ...... mutant of the tobacco enzyme.
@nl
P2860
P356
P1476
The relationship between side ...... 6 mutant of the tobacco enzyme
@en
P2093
T John Andrews
P2860
P304
32526-32536
P356
10.1074/JBC.M305493200
P407
P577
2003-06-03T00:00:00Z