Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli (Q37610006)

21 August 2017

Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli (English)

1 reference

21 August 2017

0 references

W. H. Konigsberg

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A6341995

3 October 2023

L. Henderson

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A6341995

3 October 2023

language of work or name

English

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publication date

1 May 1983

1 reference

21 August 2017

5

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full work available at URL

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https://europepmc.org/articles/pmc393846?pdf=render

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Portable Document Format

online access status

open access

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A6341995

https://europepmc.org/articles/PMC393846

3 October 2023

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A6341995

https://europepmc.org/articles/PMC393846?pdf=render

3 October 2023

file format

Portable Document Format

online access status

open access

content deliverer

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A6341995

https://pnas.org/doi/pdf/10.1073/pnas.80.9.2467

3 October 2023

1 reference

Crossref

DOI

10.1073/PNAS.80.9.2467

https://api.crossref.org/works/10.1073/PNAS.80.9.2467

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

3 October 2023

published in

1 reference

21 August 2017

80

1 reference

21 August 2017

9

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21 August 2017

2467-2471

1 reference

The enzymology of control by feedback inhibition.

21 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution study

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Nucleotide sequence of the structural gene (pyrB) that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Amino acid sequence of the T4 DNA helix-destabilizing protein

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Crystallographic Determination of Symmetry of Aspartate Transcarbamylase

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Hybridization of native and chemically modified enzymes. 3. The catalytic subunits of aspartate transcarbamylase

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

An essential residue at the active site of aspartate transcarbamylase

23 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Pyridoxal 5'-phosphate, a fluorescent probe in the active site of aspartate transcarbamylase

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Primary structure and properties of an inactive mutant aspartate transcarbamoylase

14 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Purification and characterization of a mutant aspartate transcarbamoylase lacking enzyme activity

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Comparison of the N-terminal sequences of aspartate and ornithine carbamoyltransferases ofEscherichia coli

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Aspartate transcarbamylase from Escherichia coli. Characterization of the polypeptide chains by molecular weight, amino acid composition, and amino-terminal residues.

28 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Aspartate transcarbamylase from Escherichia coli. The use of pyridoxal 5'-phosphate as a probe in the active site.

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

Reaction of the catalytic subunit of Escherichia coli aspartate transcarbamylase with permanganate ion, a reactive structural analogue of phosphate ion.

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

A study of the sulfhydryl groups of the catalytic subunit of Escherichia coli aspartate transcarbamylase. The use of enzyme--5-thio-2-nitrobenzoate mixed disulfides as intermediates in modifying enzyme sulfhydryl groups

25 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=393846

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

1 September 2018

1 reference

12 December 2020

Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide Groups

1 reference

12 December 2020

New Structural Model of E. coli Aspartate Transcarbamylase and the Amino-acid Sequence of the Regulatory Polypeptide Chain

1 reference

12 December 2020

Inactivation of the catalytic subunit of aspartate transcarbamylase by nitration with tetranitromethane

1 reference

12 December 2020

The Purification of Aspartate Transcarbamylase of Escherichia coli and Separation of Its Protein Subunits

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.80.9.2467

1 reference

21 August 2017

0 references

1 reference

PMC publication ID

393846

21 August 2017

1 reference

PMC publication ID

393846