(Q37673791)

English

Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamoylase

scientific article published on January 1985

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamoylase (English)

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

author name string

E A Robey

1

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

H K Schachman

2

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

language of work or name

0 references

publication date

1 January 1985

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

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

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

82

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

2

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

361-365

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

23 August 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

23 August 2017

Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

23 August 2017

Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

23 August 2017

Synthesis of aspartate transcarbamoylase in Escherichia coli: transcriptional regulation of the pyrB-pyrI operon

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

23 August 2017

Cooperative Interactions in Aspartate Transcarbamoylase. 1. Hybrids Composed of Native and Chemically Inactivated Catalytic Polypeptide Chains

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

23 August 2017

A method for the separation of hybrids of chromatographically identical oligomeric proteins. Use of 3,4,5,6-tetrahydrophthaloyl groups as a reversible "chromatographic handle"

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

23 August 2017

Crystallographic structure analysis of glucose 6-phosphate isomerase at 3-5 A resolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

23 August 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

23 August 2017

Protein Complementation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

23 August 2017

The structure of the flavoenzyme glutathione reductase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

23 August 2017

Primary structure and properties of an inactive mutant aspartate transcarbamoylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

28 September 2017

5 Aspartate transcarbamoylase (Escherichia coli): Preparation of subunits

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

28 September 2017

Modification of three active site lysine residues in the catalytic subunit of aspartate transcarbamylase by D- and L-bromosuccinate.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

25 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

25 June 2018

Aspartate transcarbamylase. Kinetic studies of the catalytic subunit.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

25 June 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

25 June 2018

Concerted allosteric transition in hybrids of aspartate transcarbamoylase containing different arrangements of active and inactive sites.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

25 June 2018

Genetic characterization of the folding domains of the catalytic chains in aspartate transcarbamoylase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=397038

1 September 2018

An ultraviolet spectrophotometric assay for aspartate transcarbamylase

1 reference

https://pubmed.ncbi.nlm.nih.gov/3881763

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/3881763

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/3881763

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Site-specific mutagenesis of aspartate transcarbamoylase. Replacement of tyrosine 165 in the catalytic chain by serine reduces enzymatic activity

1 reference

https://pubmed.ncbi.nlm.nih.gov/3881763

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/3881763

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Assembly of the catalytic trimers of aspartate transcarbamoylase from folded monomers

1 reference

https://pubmed.ncbi.nlm.nih.gov/3881763

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Assembly of the catalytic trimers of aspartate transcarbamoylase from unfolded polypeptide chains

1 reference

https://pubmed.ncbi.nlm.nih.gov/3881763

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Interactions of phosphate ligands with Escherichia coli aspartate carbamoyltransferase in the crystalline state

1 reference

https://pubmed.ncbi.nlm.nih.gov/3881763

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.82.2.361

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

1985PNAS...82..361R

0 references

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

21 August 2017

ResearchGate publication ID

0 references

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