Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamoylase (Q37673791)

From Wikidata

Jump to navigation Jump to search

scientific article published on January 1985

Language	Label	Description	Also known as
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

Statements

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

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q37673791&oldid=2015109051"