(Q36279554)

English

The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure

scientific article

In more languages

default for all languages

No label defined

No description defined

Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

The allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closure (English)

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

author name string

D P Baker

1

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

L Fetler

2

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

P Vachette

3

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

E R Kantrowitz

4

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

publication date

1 November 1996

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

Protein Science

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

5

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

11

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

2276-2286

1 reference

Europe PubMed Central

PMC publication ID

13 August 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=2143294

30 September 2017

The enzymology of control by feedback inhibition.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143294

30 September 2017

Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143294

30 September 2017

Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143294

30 September 2017

Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143294

30 September 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=2143294

30 September 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=2143294

30 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143294

30 September 2017

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=2143294

30 September 2017

Aspartate transcarbamylase. Interaction with the transition state 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=2143294

29 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=2143294

29 June 2018

Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with an adenosine 5'-triphosphate analog

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143294

29 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=2143294

29 June 2018

Relationship between domain closure and binding, catalysis, and regulation 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=2143294

29 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=2143294

29 June 2018

Propagation of allosteric changes through the catalytic-regulatory interface of 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=2143294

29 June 2018

Three residues involved in binding and catalysis in the carbamyl phosphate binding site of 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=2143294

29 June 2018

Importance of domain closure for homotropic cooperativity 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=2143294

29 June 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=2143294

22 September 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=2143294

22 September 2018

Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143294

22 September 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=2143294

22 September 2018

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/8931146

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/8931146

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/8931146

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/8931146

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Modified methods for the determination of carbamyl aspartate

1 reference

https://pubmed.ncbi.nlm.nih.gov/8931146

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/8931146

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1002/PRO.5560051114

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

13 August 2017

ResearchGate publication ID

0 references

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q36279554&oldid=1519841633"