A Second Allosteric Site in Escherichia coli Aspartate Transcarbamoylase (Q27679509)

scientific article

Language	Label	Description	Also known as
English	A Second Allosteric Site in Escherichia coli Aspartate Transcarbamoylase	scientific article

Statements

instance of

scholarly article

0 references

title

A Second Allosteric Site in Escherichia coli Aspartate Transcarbamoylase (English)

0 references

1 reference

Alexis W Peterson

1

0 references

Gregory M Cockrell

series ordinal

2

0 references

Evan R Kantrowitz

series ordinal

3

0 references

language of work or name

English

0 references

publication date

19 June 2012

0 references

published in

Biochemistry

0 references

volume

51

0 references

issue

24

0 references

page(s)

4776-8

0 references

cites work

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

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3428212

retrieved

20 March 2017

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3428212

retrieved

20 March 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

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3428212

retrieved

20 March 2017

Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolution

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3428212

retrieved

20 March 2017

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3428212

retrieved

29 September 2017

Asymmetric allosteric signaling in aspartate transcarbamoylase

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3428212

retrieved

29 September 2017

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3428212

retrieved

29 September 2017

Asymmetry of binding and physical assignments of CTP and ATP sites in aspartate transcarbamoylase

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3428212

retrieved

29 September 2017

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3428212

retrieved

29 September 2017

Involvement of the gamma-phosphate of UTP in the synergistic inhibition of Escherichia coli aspartate transcarbamylase by CTP and UTP.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3428212

retrieved

2 June 2018

Tryptophan residues at subunit interfaces used as fluorescence probes to investigate homotropic and heterotropic regulation of aspartate transcarbamylase

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3428212

retrieved

27 November 2018

Distinct Subunits for the Regulation and Catalytic Activity of Aspartate Transcarbamylase*

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/22667327

retrieved

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

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/22667327

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Discrimination between nucleotide effector responses of aspartate transcarbamoylase due to a single site substitution in the allosteric binding site

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/22667327

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The synergistic inhibition of Escherichia coli aspartate carbamoyltransferase by UTP in the presence of CTP is due to the binding of UTP to the low affinity CTP sites

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/22667327

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Probing the regulatory site of Escherichia coli aspartate transcarbamoylase by site-specific mutagenesis

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/22667327

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Synergistic inhibition of Escherichia coli aspartate transcarbamylase by CTP and UTP: binding studies using continuous-flow dialysis

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/22667327

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

0 references

0 references

PubMed publication ID

22667327

0 references

A Second Allosteric Site in Escherichia coli Aspartate Transcarbamoylase (Q27679509)

Statements

Identifiers

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)

Navigation menu

A Second Allosteric Site in Escherichia coli Aspartate Transcarbamoylase (Q27679509)

Statements

Identifiers

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)

Navigation menu

Search