(Q30176571)

9 June 2017

Complementing substitutions at the bottom of the barrel influence catalysis and stability of ribulose-bisphosphate carboxylase/oxygenase (English)

1 reference

9 June 2017

0 references

Hong S

1

1 reference

PubMed ID

9111007

9 June 2017

Spreitzer RJ

series ordinal

2

1 reference

PubMed ID

9111007

9 June 2017

language of work or name

English

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publication date

1 April 1997

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Journal of Biological Chemistry

9 June 2017

4

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based on heuristic

inferred from page(s)

published in

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9 June 2017

272

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9 June 2017

17

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9 June 2017

11114-11117

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Structure, function, regulation, and assembly of D-ribulose-1,5-bisphosphate carboxylase/oxygenase

9 June 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

The transport of proteins into chloroplasts

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

Formation of the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase by a disorder-order transition from the unactivated to the activated form.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

The mechanism of Rubisco activase: Insights from studies of the properties and structure of the enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

Complementing amino acid substitutions within loop 6 of the alpha/beta-barrel active site influence the CO2/O2 specificity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

A hybrid ribulose bisphosphate carboxylase/oxygenase enzyme exhibiting a substantial increase in substrate specificity factor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

Elimination of the Chlamydomonas gene family that encodes the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

Proteolysis and transition-state-analogue binding of mutant forms of ribulose-1,5-bisphosphate carboxylase/oxygenase from Chlamydomonas reinhardtii

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

How various factors influence the CO2/O 2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4 A resolution. Subunit interactions and active site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

Directed mutagenesis of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Loop 6 substitutions complement for structural stability but decrease catalytic efficiency

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

Pseudoreversion substitution at large-subunit residue 54 influences the CO2/O2 specificity of chloroplast ribulose-bisphosphate carboxylase/oxygenase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

Temperature-Sensitive, Photosynthesis-Deficient Mutants of Chlamydomonas reinhardtii

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

Nuclear mutation restores the reduced CO2/O2 specificity of ribulosebisphosphate carboxylase/oxygenase in a temperature-conditional chloroplast mutant of Chlamydomonas reinhardtii

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

Photosynthesis-deficient Mutants of Chlamydomonas reinhardii with Associated Light-sensitive Phenotypes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

A Sensitive Assay Procedure for Simultaneous Determination of Ribulose-1,5-bisphosphate Carboxylase and Oxygenase Activities

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.17.11114

21 January 2018

Identifiers

DOI

10.1074/JBC.272.17.11114

1 reference

9 June 2017

1 reference

PubMed ID

9111007