Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase (Q36277784)

13 August 2017

Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase (English)

1 reference

13 August 2017

B B Zhou

1

1 reference

13 August 2017

H K Schachman

series ordinal

2

1 reference

13 August 2017

1 January 1993

1 reference

13 August 2017

1 reference

13 August 2017

2

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13 August 2017

1

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13 August 2017

103-112

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

13 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

The enzymology of control by feedback inhibition.

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

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

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

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

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

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

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

Escherichia coli aspartate transcarbamylase: the relation between structure and function

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

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

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

Amino acid substitutions which stabilize aspartate transcarbamoylase in the R state disrupt both homotropic and heterotropic effects

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

A 70-amino acid zinc-binding polypeptide from the regulatory chain of aspartate transcarbamoylase forms a stable complex with the catalytic subunit leading to markedly altered enzyme activity

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

Purification and characterization of a mutant aspartate transcarbamoylase lacking enzyme activity

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

5 Aspartate transcarbamoylase (Escherichia coli): Preparation of subunits

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

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

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

Ligand-promoted weakening of intersubunit bonding domains in aspartate transcarbamoylase

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

Subunit Structure of Aspartate Transcarbamylase from Escherichia coli

29 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

Aspartate transcarbamylase. Stereospecific restrictions on the binding site for L-aspartate.

29 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

Allosteric Interactions in Aspartate Transcarbamylase. II. Evidence for Different Conformational States of the Protein in the Presence and Absence of Specific Ligands

29 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

Cooperative binding of the bisubstrate analog N-(phosphonacetyl)-L-aspartate to aspartate transcarbamoylase and the heterotropic effects of ATP and CTP.

29 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase

29 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

Effects of replacement of active site residue glutamine 231 on activity and allosteric properties of aspartate transcarbamoylase

29 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

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

29 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2142301

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

22 September 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/8443583

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Structure and arrangement of the regulatory subunits in aspartate transcarbamylase

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/8443583

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1002/PRO.5560020111

1 reference

release_yglrkkh2qjdipo4e66mym4iyye

13 August 2017

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/yglrkkh2qjdipo4e66mym4iyye

mapped directly with Wikidata item

24 November 2022

based on heuristic

1 reference

13 August 2017

PubMed publication ID

8443583

1 reference