(Q34289327)

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Quantitative relationships of site to site interaction in Escherichia coli D-3-phosphoglycerate dehydrogenase revealed by asymmetric hybrid tetramers

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scholarly article

1 reference

Europe PubMed Central

1 August 2017

Quantitative relationships of site to site interaction in Escherichia coli D-3-phosphoglycerate dehydrogenase revealed by asymmetric hybrid tetramers (English)

1 reference

Europe PubMed Central

1 August 2017

Escherichia coli

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based on heuristic

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author name string

Gregory A Grant

1

1 reference

Europe PubMed Central

1 August 2017

Xiao Lan Xu

2

1 reference

Europe PubMed Central

1 August 2017

Zhiqin Hu

3

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Europe PubMed Central

1 August 2017

language of work or name

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publication date

12 January 2004

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Europe PubMed Central

1 August 2017

Journal of Biological Chemistry

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Europe PubMed Central

1 August 2017

279

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Europe PubMed Central

1 August 2017

13452-13460

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Europe PubMed Central

1 August 2017

14

1 reference

Europe PubMed Central

1 August 2017

The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Site-directed mutagenesis of effector binding site residues.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313593200

21 January 2018

The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313593200

21 January 2018

Hybrid tetramers reveal elements of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313593200

21 January 2018

Cofactor binding to Escherichia coli D-3-phosphoglycerate dehydrogenase induces multiple conformations which alter effector binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313593200

21 January 2018

Ordered disruption of subunit interfaces during the stepwise reversible dissociation of Escherichia coli phosphofructokinase with KSCN.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313593200

21 January 2018

Isolation of an individual allosteric interaction in tetrameric phosphofructokinase from Bacillus stearothermophilus

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313593200

21 January 2018

The mechanism of velocity modulated allosteric regulation in D-3-phosphoglycerate dehydrogenase. Cross-linking adjacent regulatory domains with engineered disulfides mimics effector binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313593200

21 January 2018

A novel alpha-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313593200

21 January 2018

Amino acid residue mutations uncouple cooperative effects in Escherichia coli D-3-phosphoglycerate dehydrogenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313593200

21 January 2018

Specific interactions at the regulatory domain-substrate binding domain interface influence the cooperativity of inhibition and effector binding in Escherichia coli D-3-phosphoglycerate dehydrogenase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313593200

21 January 2018

Probing the regulatory domain interface of D-3-phosphoglycerate dehydrogenase with engineered tryptophan residues

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313593200

21 January 2018

Cooperativity in enzyme function: equilibrium and kinetic aspects

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M313593200

21 January 2018

Identifiers

10.1074/JBC.M313593200

1 reference

Europe PubMed Central

1 August 2017

1 reference

Europe PubMed Central

1 August 2017

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