Allosteric signal transmission involves synergy between discrete structural units of the regulatory subunit of aspartate transcarbamoylase (Q39897141)

15 September 2017

Allosteric signal transmission involves synergy between discrete structural units of the regulatory subunit of aspartate transcarbamoylase (English)

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15 September 2017

L Liu

1

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15 September 2017

M E Wales

series ordinal

2

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15 September 2017

J R Wild

series ordinal

3

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15 September 2017

language of work or name

English

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publication date

1 January 2000

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15 September 2017

9

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Archives of Biochemistry and Biophysics

inferred from page(s)

published in

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15 September 2017

373

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15 September 2017

2

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15 September 2017

352-360

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Temperature effects on the allosteric responses of native and chimeric aspartate transcarbamoylases

15 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

Conversion of the allosteric regulatory patterns of aspartate transcarbamoylase by exchange of a single beta-strand between diverged regulatory chains

22 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

Molecular dynamics simulations and rigid body (TLS) analysis of aspartate carbamoyltransferase: evidence for an uncoupled R state

22 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

Aspartate transcarbamylase from Escherichia coli: activity and regulation

22 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

RASMOL: biomolecular graphics for all

22 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

In vivo formation of hybrid aspartate transcarbamoylases from native subunits of divergent members of the family Enterobacteriaceae

22 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

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

22 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

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

22 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

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

22 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

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

22 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

Molecular evolution and genetic engineering of protein domains involving aspartate transcarbamoylase

22 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

Heterotropic interactions in aspartate transcarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation

22 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

Comparison of the aspartate transcarbamoylases from Serratia marcescens and Escherichia coli.

22 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

Site-directed mutagenesis of virtually any plasmid by eliminating a unique site

15 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

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

15 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3241997

Modified methods for the determination of carbamyl aspartate

20 August 2018

1 reference

12 December 2020

Buffers of constant ionic strength for studying pH-dependent processes

1 reference

12 December 2020

Properties of hybrid aspartate transcarbamoylase formed with native subunits from divergent bacteria

1 reference

12 December 2020

Site-specific substitutions of the Tyr-165 residue in the catalytic chain of aspartate transcarbamoylase promotes a T-state preference in the holoenzyme

1 reference

12 December 2020

The activation of Escherichia coli aspartate transcarbamylase by ATP. Specific involvement of helix H2' at the hydrophobic interface between the two domains of the regulatory chains

1 reference

12 December 2020

Large differences are observed between the crystal and solution quaternary structures of allosteric aspartate transcarbamylase in the R state

1 reference

12 December 2020

Coupling of homotropic and heterotropic interactions in Escherichia coli aspartate transcarbamylase

1 reference

12 December 2020

Identifiers

DOI

10.1006/ABBI.1999.1570

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15 September 2017

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15 September 2017

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