(Q24648371)

21 June 2017

title

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

1 reference

21 June 2017

J E Gouaux

1

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21 June 2017

W N Lipscomb

series ordinal

2

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21 June 2017

language of work or name

English

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publication date

1 June 1988

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

21 June 2017

published in

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21 June 2017

volume

85

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21 June 2017

issue

12

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21 June 2017

page(s)

4205-4208

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Crystallographic R factor refinement by molecular dynamics

21 June 2017

cites work

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280395

Crystallographic Determination of Symmetry of Aspartate Transcarbamylase

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280395

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

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280395

A unifying concept for the active site region in aspartate transcarbamylase

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280395

Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analog N-(phosphonacetyl)-L-aspartate

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280395

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

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280395

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

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280395

Aspartate transcarbamylase. Kinetic studies of the catalytic subunit.

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280395

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

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280395

N-(phosphonacetyl)-L-aspartate, a potent transition state analog inhibitor of aspartate transcarbamylase, blocks proliferation of mammalian cells in culture.

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280395

Design and synthesis of new transition-state analogue inhibitors of aspartate transcarbamylase

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280395

The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: a molecular modelling study.

30 May 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280395

Ligand interactions at the active site of aspartate transcarbamoylase from Escherichia coli.

19 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=280395

Aspartate transcarbamylase. Studies of the catalytic subunit by ultraviolet difference spectroscopy

19 June 2018

1 reference

12 December 2020

Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering. Signal transmission following effector binding

1 reference

12 December 2020

Antitumor activity of N-(phosphonacetyl)-L-aspartic acid, a transition-state inhibitor of aspartate transcarbamylase

1 reference

12 December 2020

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

1 reference

12 December 2020

Pyrimidine biosynthesis in Escherichia coli

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.85.12.4205

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21 June 2017

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