A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration. - Wikidata - wikimedia - TriplyDB

A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.

A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.

http://www.wikidata.org/entity/Q37367116

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Structure and Identification of a Pterin Dehydratase-like Protein as a Ribulose-bisphosphate Carboxylase/Oxygenase (RuBisCO) Assembly Factor in the α-Carboxysome Structure-function studies with the unique hexameric form II ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from Rhodopseudomonas palustris.Functional metagenomic selection of ribulose 1, 5-bisphosphate carboxylase/oxygenase from uncultivated bacteria Rubisco Accumulation Factor 1 from Thermosynechococcus elongatus participates in the final stages of ribulose-1,5-bisphosphate carboxylase/oxygenase assembly in Escherichia coli cells and in vitro Functional prokaryotic RubisCO from an oceanic metagenomic library.Development of an activity-directed selection system enabled significant improvement of the carboxylation efficiency of Rubisco In Vivo Studies in Rhodospirillum rubrum Indicate That Ribulose-1,5-bisphosphate Carboxylase/Oxygenase (Rubisco) Catalyzes Two Obligatorily Required and Physiologically Significant Reactions for Distinct Carbon and Sulfur Metabolic Pathways.Serine 363 of a Hydrophobic Region of Archaeal Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase from Archaeoglobus fulgidus and Thermococcus kodakaraensis Affects CO2/O2 Substrate Specificity and Oxygen Sensitivity.Metabolic Regulation as a Consequence of Anaerobic 5-Methylthioadenosine Recycling in Rhodospirillum rubrum RubisCO of a nucleoside pathway known from Archaea is found in diverse uncultivated phyla in bacteria.Global metabolic rewiring for improved CO2 fixation and chemical production in cyanobacteria.The mechanism of Rubisco-catalysed oxygenation.Back to the future: function-first metagenomics returns to the fore.RubisCO selection using the vigorously aerobic and metabolically versatile bacterium Ralstonia eutropha.Directed -in vitro- evolution of Precambrian and extant Rubiscos.

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A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.

http://www.wikidata.org/entity/Q37367116

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on September 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

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name

A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.

@en

A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.

@nl

type

label

A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.

@en

A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.

@nl

prefLabel

A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.

@en

A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.

@nl

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P1476

A Rubisco mutant that confers growth under a normally "inhibitory" oxygen concentration.

@en

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F Robert Tabita

http://www.w3.org/2001/XMLSchema#string

Sriram Satagopan

http://www.w3.org/2001/XMLSchema#string

Stephanie S Scott

http://www.w3.org/2001/XMLSchema#string

Todd G Smith

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P2860

Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized

Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Crystal structure of a novel-type archaeal rubisco with pentagonal symmetry

Structural analysis of altered large-subunit loop-6/carboxy-terminus interactions that influence catalytic efficiency and CO2/O2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase

Function, Structure, and Evolution of the RubisCO-Like Proteins and Their RubisCO Homologs

Crystallographic studies of Xe and Kr binding within the large internal cavity of cytochrome ba3 from Thermus thermophilus: structural analysis and role of oxygen transport channels in the heme-Cu oxidases

Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate

Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco

P304

9076-9083

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P31

scholarly article

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10.1021/BI9006385

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P407

P433

38

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P478

48

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P577

2009-09-01T00:00:00Z

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P5875

26765912

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P698

19705820

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2753866

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