(Q37722721)

English

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

scientific article published on March 1990

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

22 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 (English)

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

Escherichia coli

0 references

author name string

C J Newton

1

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

E R Kantrowitz

2

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

language of work or name

0 references

publication date

1 March 1990

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

number of pages

5

1 reference

based on heuristic

inferred from page(s)

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

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

87

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

6

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

2309-2313

1 reference

Europe PubMed Central

PMC publication ID

22 August 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=53676

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=53676

23 August 2017

Attenuation control of pyrBI operon expression in Escherichia coli K-12

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53676

23 August 2017

Synthesis of aspartate transcarbamoylase in Escherichia coli: transcriptional regulation of the pyrB-pyrI operon

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53676

23 August 2017

Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53676

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=53676

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=53676

23 August 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=53676

23 August 2017

Importance of the loop at residues 230-245 in the allosteric interactions 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=53676

23 August 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=53676

23 August 2017

Production of single-stranded plasmid DNA

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53676

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=53676

23 August 2017

Escherichia coli aspartate transcarbamylase: the relation between structure and function

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53676

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=53676

23 August 2017

Crystal structure of the Glu-239----Gln mutant of aspartate carbamoyltransferase at 3.1-A resolution: an intermediate quaternary structure

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53676

23 August 2017

Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53676

23 August 2017

Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase 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=53676

23 August 2017

DNA sequencing with chain-terminating inhibitors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53676

23 August 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=53676

6 September 2017

Stabilization of the relaxed state of aspartate transcarbamoylase by modification with a bifunctional reagent

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53676

6 September 2017

Oligonucleotide-directed mutagenesis using M13-derived vectors: an efficient and general procedure for the production of point mutations in any fragment of DNA.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53676

14 September 2017

Improved oligonucleotide site-directed mutagenesis using M13 vectors.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53676

14 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=53676

23 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=53676

23 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=53676

23 June 2018

Catalytic-regulatory subunit interactions and allosteric effects in aspartate transcarbamylase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53676

23 June 2018

Structural asymmetry in the CTP-liganded form of 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=53676

23 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=53676

23 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=53676

23 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=53676

23 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=53676

23 June 2018

A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms 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=53676

23 June 2018

The organization and regulation of the pyrBI operon in E. coli includes a rho-independent attenuator sequence

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=53676

1 September 2018

An improved colorimetric assay for aspartate and ornithine transcarbamylases

1 reference

https://pubmed.ncbi.nlm.nih.gov/2179954

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/2179954

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.87.6.2309

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

1990PNAS...87.2309N

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

22 August 2017

ResearchGate publication ID

0 references

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