Substitutions at the Asp-473 latch residue of chlamydomonas ribulosebisphosphate carboxylase/oxygenase cause decreases in carboxylation efficiency and CO(2)/O(2) specificity. (Q30164302)

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English	Substitutions at the Asp-473 latch residue of chlamydomonas ribulosebisphosphate carboxylase/oxygenase cause decreases in carboxylation efficiency and CO(2)/O(2) specificity.	scientific article

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17 November 2019

Substitutions at the Asp-473 latch residue of chlamydomonas ribulosebisphosphate carboxylase/oxygenase cause decreases in carboxylation efficiency and CO(2)/O(2) specificity (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14734540%20AND%20SRC:MED&resulttype=core&format=json

17 November 2019

Sriram Satagopan

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17 November 2019

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Robert J Spreitzer

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17 November 2019

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20 January 2004

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17 November 2019

Journal of Biological Chemistry

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17 November 2019

279

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17 November 2019

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17 November 2019

14240-14244

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17 November 2019

The TIM-barrel fold: a versatile framework for efficient enzymes

1 reference

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Rubisco: structure, regulatory interactions, and possibilities for a better enzyme

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Manipulation of Rubisco: the amount, activity, function and regulation.

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Structural framework for catalysis and regulation in ribulose-1,5-bisphosphate carboxylase/oxygenase

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Crystal structure of activated tobacco rubisco complexed with the reaction-intermediate analogue 2-carboxy-arabinitol 1,5-bisphosphate

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Large structures at high resolution: the 1.6 A crystal structure of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase complexed with 2-carboxyarabinitol bisphosphate

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Crystal structure of carboxylase reaction-oriented ribulose 1, 5-bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita

1 reference

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First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii

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The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate

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Rubisco activase - Rubisco's catalytic chaperone

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Activase region on chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Nonconservative substitution in the large subunit alters species specificity of protein interaction

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The crystal structure of rubisco from Alcaligenes eutrophus reveals a novel central eight-stranded beta-barrel formed by beta-strands from four subunits

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The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate

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X-ray structure of Galdieria Rubisco complexed with one sulfate ion per active site

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Nonsense mutations in the Chlamydomonas chloroplast gene that codes for the large subunit of ribulosebisphosphate carboxylase/oxygenase

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RbcS suppressor mutations improve the thermal stability and CO2/O2 specificity of rbcL- mutant ribulose-1,5-bisphosphate carboxylase/oxygenase

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Nucleotide sequence analysis of a gene encoding a streptomycin/spectinomycin adenylyltransferase

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Sequence of the chloroplast DNA region of Chlamydomonas reinhardii containing the gene of the large subunit of ribulose bisphosphate carboxylase and parts of its flanking genes

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Transgenic expression of aminoglycoside adenine transferase in the chloroplast: a selectable marker of site-directed transformation of chlamydomonas

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

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Complementing substitutions within loop regions 2 and 3 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase

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Reduced CO2/O2 specificity of ribulose-bisphosphate carboxylase/oxygenase in a temperature-sensitive chloroplast mutant of Chlamydomonas

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Regulation of Soybean Net Photosynthetic CO(2) Fixation by the Interaction of CO(2), O(2), and Ribulose 1,5-Diphosphate Carboxylase.

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21 January 2018

Preparative-scale enzymic synthesis of d-[14C]ribulose 1,5-bisphosphate

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21 January 2018

Interaction of ribulosebisphosphate carboxylase/oxygenase with transition-state analogues

1 reference

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21 January 2018

Status of the substrate binding sites of ribulose bisphosphate carboxylase as determined with 2-C-carboxyarabinitol 1,5-bisphosphate.

1 reference

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21 January 2018

Positive and negative selection of mutant forms of prokaryotic (cyanobacterial) ribulose-1,5-bisphosphate carboxylase/oxygenase

1 reference

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21 January 2018

Alanine-scanning mutagenesis of the small-subunit beta A-beta B loop of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase: substitution at Arg-71 affects thermal stability and CO2/O2 specificity.

1 reference

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Assessment of Structural and Functional Divergence Far from the Large Subunit Active Site of Ribulose-1,5-bisphosphate Carboxylase/Oxygenase

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Effect of mutation of lysine-128 of the large subunit of ribulose bisphosphate carboxylase/oxygenase from Anacystis nidulans

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Crystal structure of the active site of ribulose-bisphosphate carboxylase

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Species variation in the specificity of ribulose biphosphate carboxylase/oxygenase

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Specificity for activase is changed by a Pro-89 to Arg substitution in the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase

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Structural transitions during activation and ligand binding in hexadecameric Rubisco inferred from the crystal structure of the activated unliganded spinach enzyme

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Partial reduction in ribulose 1,5-bisphosphate carboxylase/oxygenase activity by carboxypeptidase A

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Thermal Instability of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase from a Temperature-Conditional Chloroplast Mutant of Chlamydomonas reinhardtii

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10.1074/JBC.M313215200

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14734540%20AND%20SRC:MED&resulttype=core&format=json

17 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14734540%20AND%20SRC:MED&resulttype=core&format=json

17 November 2019

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