(Q54706019)

English

Co-operative interactions between the catalytic sites in Escherichia coli aspartate transcarbamylase. Role of the C-terminal region of the regulatory chains.

scientific article

In more languages

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

Co-operative interactions between the catalytic sites in Escherichia coli aspartate transcarbamylase. Role of the C-terminal region of the regulatory chains. (English)

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

Escherichia coli

0 references

author name string

X G Xi

1

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

F Van Vliet

2

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

M M Ladjimi

3

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

B De Wannemaeker

4

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

C De Staercke

5

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

A Piérard

6

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

N Glansdorff

7

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

G Hervé

8

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

R Cunin

9

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

language of work or name

0 references

publication date

1 November 1990

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

Journal of Molecular Biology

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

216

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

2

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

375-384

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

Escherichia coli aspartate transcarbamoylase: structure, energetics, and catalytic and regulatory mechanisms

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli. I. Primary structure of a pyrI gene encoding a modified regulatory subunit

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Homotropic effects in aspartate transcarbamoylase. What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl-L-aspartate?

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: a molecular modelling study.

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering. Signal transmission following effector binding

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Allosteric regulation of aspartate transcarbamoylase. Changes in the sedimentation coefficient promoted by the bisubstrate analog N-(phosphonacetyl)-L-aspartate

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Kinetic mechanism of native Escherichia coli aspartate transcarbamylase.

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Interactions of Cibacron Blue F3GA and nucleotides with Escherichia coli aspartate carbamoyltransferase and its subunits.

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Biosynthesis of an aspartate transcarbamylase lacking co-operative interactions. I. Disconnection of homotropic and heterotropic interactions under the influence of 2-thiouracil

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Structural asymmetry in the CTP-liganded form of aspartate carbamoyltransferase from Escherichia coli.

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

The gapped duplex DNA approach to oligonucleotide-directed mutation construction.

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

A possible model for the concerted allosteric transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies.

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli. II. Involvement of the C-terminal region of the regulatory chain in homotropic and heterotropic interactions

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Relationship between domain closure and binding, catalysis, and regulation in Escherichia coli aspartate transcarbamylase.

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments

2 references

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Function of arginine-234 and aspartic acid-271 in domain closure, cooperativity, and catalysis in Escherichia coli aspartate transcarbamylase.

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Changes in the X-ray solution scattering of aspartate transcarbamylase following the allosteric transition

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Biosynthesis of Escherichia coli aspartate transcarbamylase. I. Parameters of gene expression and sequential biosynthesis of the subunits

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

The organization and regulation of the pyrBI operon in E. coli includes a rho-independent attenuator sequence

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

The stimulation of Escherichia coli aspartate transcarbamylase activity by adenosine triphosphate. Relation with the other regulatory conformational changes; a model

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1016%2FS0022-2836%2805%2980328-6

7 January 2021

based on heuristic

inferred from DOI database lookup

Protein measurement with the Folin phenol reagent

1 reference

31 May 2024

https://opencitations.net/index/api/v1/citations/10.1016/S0021-9258(19)52451-6

Identifiers

10.1016/S0022-2836(05)80328-6

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

3 June 2018

http://europepmc.org/abstract/MED/2254935

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=Q54706019&oldid=2169398527"