(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

0 references

publication date

1 May 1983

1 reference

21 August 2017

5

1 reference

full work available at URL

inferred from page(s)

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

file format

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

1 reference

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