(Q29391897)

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Time Evolution of the Quaternary Structure of Escherichia coli Aspartate Transcarbamoylase upon Reaction with the Natural Substrates and a Slow, Tight-Binding Inhibitor

scientific article (publication date: December 2008)

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Time Evolution of the Quaternary Structure of Escherichia coli Aspartate Transcarbamoylase upon Reaction with the Natural Substrates and a Slow, Tight-Binding Inhibitor (English)

1 reference

DOI.org query endpoint

https://doi.org/10.1016%2FJ.JMB.2008.09.022

14 April 2017

Escherichia coli

1 reference

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Jay M. West

1

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https://doi.org/10.1016%2FJ.JMB.2008.09.022

14 April 2017

Jiarong Xia

2

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https://doi.org/10.1016%2FJ.JMB.2008.09.022

14 April 2017

Hiro Tsuruta

3

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https://doi.org/10.1016%2FJ.JMB.2008.09.022

14 April 2017

Wenyue Guo

4

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https://doi.org/10.1016%2FJ.JMB.2008.09.022

14 April 2017

Elizabeth M. O'Day

5

1 reference

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https://doi.org/10.1016%2FJ.JMB.2008.09.022

14 April 2017

Evan R. Kantrowitz

6

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https://doi.org/10.1016%2FJ.JMB.2008.09.022

14 April 2017

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publication date

December 2008

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https://doi.org/10.1016%2FJ.JMB.2008.09.022

14 April 2017

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13

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Journal of Molecular Biology

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https://doi.org/10.1016%2FJ.JMB.2008.09.022

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384

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https://doi.org/10.1016%2FJ.JMB.2008.09.022

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1

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https://doi.org/10.1016%2FJ.JMB.2008.09.022

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206-218

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DOI.org query endpoint

https://doi.org/10.1016%2FJ.JMB.2008.09.022

14 April 2017

Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

14 April 2017

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

14 April 2017

DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

14 April 2017

Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

14 April 2017

Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

14 April 2017

Kinetics of slow and tight-binding inhibitors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

14 April 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

14 April 2017

Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferase. X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

14 April 2017

Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8-A resolution and neutral pH

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

14 April 2017

Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

14 April 2017

A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

DISC ELECTROPHORESIS. I. BACKGROUND AND THEORY

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Is cooperative oxygen binding by hemoglobin really understood?

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Aspartate transcarbamylase from Escherichia coli: activity and regulation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Relaxation spectra of aspartate transcarbamylase. I. Interaction of 5-bromocytidine triphosphate with native enzyme and regulatory subunit

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Aspartate transcarbamylase. Kinetic studies of the catalytic subunit.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Allosteric interactions in aspartate transcarbamylase. 3. Interpretation of experimental data in terms of the model of Monod, Wyman, and Changeux

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Kinetics of the interaction of N-(phosphonacetyl)-L-aspartate with the catalytic subunit of aspartate transcarbamoylase. A slow conformational change subsequent to binding.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Effectors of Escherichia coli aspartate transcarbamoylase differentially perturb aspartate binding rather than the T-R transition.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Can a simple model account for the allosteric transition of aspartate transcarbamoylase?

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Structural kinetics of the allosteric transition of aspartate transcarbamylase produced by physiological substrates.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state model

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

The effect of pH on the cooperative behavior of aspartate transcarbamylase from Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

3 June 2018

Influence of nucleotide effectors on the kinetics of the quaternary structure transition of allosteric aspartate transcarbamylase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

26 November 2018

The conserved residues glutamate-37, aspartate-100, and arginine-269 are important for the structural stabilization of Escherichia coli aspartate transcarbamoylase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

26 November 2018

Kinetics of the quaternary structure change of aspartate transcarbamylase triggered by succinate, a competitive inhibitor

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

26 November 2018

Superproduction and rapid purification of Escherichia coli aspartate transcarbamylase and its catalytic subunit under extreme derepression of the pyrimidine pathway.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2656920

26 November 2018

Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase

1 reference

https://pubmed.ncbi.nlm.nih.gov/18823998

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Isolation and properties of a species produced by the partial dissociation of aspartate transcarbamylase from Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/18823998

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

An improved colorimetric assay for aspartate and ornithine transcarbamylases

1 reference

https://pubmed.ncbi.nlm.nih.gov/18823998

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutions

1 reference

https://pubmed.ncbi.nlm.nih.gov/18823998

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Solvent effects on allosteric equilibria: stabilization of T and R conformations of Escherichia coli aspartate transcarbamylase by organic solvents

1 reference

https://pubmed.ncbi.nlm.nih.gov/18823998

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering. Signal transmission following effector binding

1 reference

https://pubmed.ncbi.nlm.nih.gov/18823998

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Hydrogen bonding and specificity. Fluorodeoxy sugars as probes of hydrogen bonding in the glycogen phosphorylase-glucose complex

1 reference

https://pubmed.ncbi.nlm.nih.gov/18823998

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based on heuristic

inferred from PubMed ID database lookup

Molecular code for cooperativity in hemoglobin

1 reference

https://pubmed.ncbi.nlm.nih.gov/18823998

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The Purification of Aspartate Transcarbamylase of Escherichia coli and Separation of Its Protein Subunits

1 reference

https://pubmed.ncbi.nlm.nih.gov/18823998

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Allosteric interactions in aspartate transcarbamylase. I. Binding of specific ligands to the native enzyme and its isolated subunits

1 reference

https://pubmed.ncbi.nlm.nih.gov/18823998

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

X-ray Scattering Titration of the Quaternary Structure Transition of Aspartate Transcarbamylase with a Bisubstrate Analogue: Influence of Nucleotide Effectors

1 reference

https://pubmed.ncbi.nlm.nih.gov/18823998

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Aspartate Carbamyl Transferase from Escherichia coli

1 reference

31 May 2024

https://opencitations.net/index/api/v1/citations/10.3891/ACTA.CHEM.SCAND.10-0548

Identifiers

10.1016/J.JMB.2008.09.022

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https://doi.org/10.1016%2FJ.JMB.2008.09.022

14 April 2017

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