(Q37608042)

English

Heterotropic interactions in aspartate transcarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation

scientific article published on October 1991

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

Heterotropic interactions in aspartate transcarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation (English)

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

author name string

Van Vliet F

1

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

Xi XG

2

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

De Staercke C

3

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

de Wannemaeker B

4

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

Jacobs A

5

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

Cherfils J

6

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

Ladjimi MM

7

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

Hervé G

8

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

Cunin R

9

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

language of work or name

0 references

publication date

1 October 1991

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

Proceedings of the National Academy of Sciences of the United States of America

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

88

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

20

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

9180-9183

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

Protein measurement with the Folin phenol reagent

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

23 August 2017

Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

23 August 2017

Structure of unligated aspartate carbamoyltransferase of Escherichia coli 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=52676

23 August 2017

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=52676

23 August 2017

Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue 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=52676

23 August 2017

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=52676

23 August 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=52676

23 August 2017

5'-3' exonucleases in phosphorothioate-based oligonucleotide-directed mutagenesis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

23 August 2017

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=52676

23 August 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=52676

23 August 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=52676

23 August 2017

Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

23 August 2017

The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop containing residues 230-245 of the catalytic chain

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

23 August 2017

Escherichia coli aspartate transcarbamoylase: structure, energetics, and catalytic and regulatory mechanisms

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

6 September 2017

Heterotropic interactions in Escherichia coli aspartate transcarbamylase. Subunit interfaces involved in CTP inhibition and ATP activation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

6 September 2017

The stimulation of Escherichia coli aspartate transcarbamylase activity by adenosine triphosphate. Relation with the other regulatory conformational changes; a model

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

6 September 2017

Changes in the X-ray solution scattering of aspartate transcarbamylase following the allosteric transition

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

28 September 2017

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=52676

28 September 2017

Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by 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=52676

28 September 2017

An aspartate transcarbamylase lacking catalytic subunit interactions. Study of conformational changes by ultraviolet absorbance and circular dichroism spectroscopy

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

28 September 2017

Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli. II. Involvement of the C-terminal region of the regulatory chain in homotropic and heterotropic interactions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

25 June 2018

The pAR5 mutation and the allosteric mechanism of Escherichia coli aspartate carbamoyltransferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

25 June 2018

A possible model for the concerted allosteric transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

25 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=52676

25 June 2018

Function of arginine-234 and aspartic acid-271 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamylase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

25 June 2018

Conversion of allosteric inhibition to activation in phosphofructokinase by protein engineering.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

25 June 2018

Dissection of the effector-binding site and complementation studies of Escherichia coli phosphofructokinase using site-directed mutagenesis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=52676

25 June 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=52676

1 September 2018

Coupling of homotropic and heterotropic interactions in Escherichia coli aspartate transcarbamylase

1 reference

https://pubmed.ncbi.nlm.nih.gov/1924381

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Interactions of phosphate ligands with Escherichia coli aspartate carbamoyltransferase in the crystalline state

1 reference

https://pubmed.ncbi.nlm.nih.gov/1924381

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/1924381

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The catalytic site of Escherichia coli aspartate transcarbamylase: interaction between histidine 134 and the carbonyl group of the substrate carbamyl phosphate

1 reference

https://pubmed.ncbi.nlm.nih.gov/1924381

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Biosynthesis of an aspartate transcarbamylase lacking co-operative interactions. I. Disconnection of homotropic and heterotropic interactions under the influence of 2-thiouracil

1 reference

https://pubmed.ncbi.nlm.nih.gov/1924381

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Biosynthesis of Escherichia coli aspartate transcarbamylase. I. Parameters of gene expression and sequential biosynthesis of the subunits

1 reference

https://pubmed.ncbi.nlm.nih.gov/1924381

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.88.20.9180

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

1991PNAS...88.9180V

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

ResearchGate publication ID

0 references

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