(Q45965954)

English

Long range effects of amino acid substitutions in the catalytic chain of aspartate transcarbamoylase. Localized replacements in the carboxyl-terminal alpha-helix cause marked alterations in allosteric properties and intersubunit interactions

scientific article published on February 5, 1992

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scholarly article

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/1733944

Long range effects of amino acid substitutions in the catalytic chain of aspartate transcarbamoylase. Localized replacements in the carboxyl-terminal alpha-helix cause marked alterations in allosteric properties and intersubunit interactions (English)

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

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10.1016/S0021-9258(18)45899-1

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11 November 2022

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10.1016/S0021-9258(18)45899-1

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11 November 2022

author name string

C. B. Peterson

1

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1733944

11 November 2022

H. K. Schachman

2

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PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1733944

11 November 2022

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publication date

1 February 1992

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18 December 2017

http://europepmc.org/abstract/MED/1733944

5 February 1992

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National Center for Biotechnology Information

PubMed publication ID

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=1733944

11 November 2022

full work available at URL

http://intl.jbc.org/cgi/content/abstract/267/4/2443

online access status

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A1733944

11 November 2022

https://api.elsevier.com/content/article/PII:S0021925818458991?httpAccept=text/xml

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10.1016/S0021-9258(18)45899-1

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11 November 2022

https://api.elsevier.com/content/article/PII:S0021925818458991?httpAccept=text/plain

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/1733944

267

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/1733944

4

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/1733944

2443-2450

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Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/1733944

Role of a carboxyl-terminal helix in the assembly, interchain interactions, and stability of aspartate transcarbamoylase

1

1 reference

10.1016/S0021-9258(18)45899-1

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11 November 2022

Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains

2

1 reference

10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase

3

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

High-resolution differential scanning calorimetric analysis of the subunits of Escherichia coli aspartate transcarbamoylase.

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Differential scanning calorimetric study of the thermal denaturation of aspartate transcarbamoylase of Escherichia coli

9

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

Differential scanning calorimetric studies of E. coli aspartate transcarbamylase. III. The denaturational thermodynamics of the holoenzyme with single-site mutations in the catalytic chain

10

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state model

12

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

Allosteric Interactions in Aspartate Transcarbamylase. II. Evidence for Different Conformational States of the Protein in the Presence and Absence of Specific Ligands

14

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylase. Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments

15

1 reference

10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

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

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

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

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

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

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10.1016/S0021-9258(18)45899-1

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11 November 2022

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

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10.1016/S0021-9258(18)45899-1

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11 November 2022

5 Aspartate transcarbamoylase (Escherichia coli): Preparation of subunits

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10.1016/S0021-9258(18)45899-1

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11 November 2022

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

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

Allosteric regulation of aspartate transcarbamoylase. Effect of active site ligands on the reactivity of sulfhydryl groups of the regulatory subunits

22

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

AN APPARATUS FOR PREPARATIVE TEMPERATURE-REGULATED POLYACRYLAMIDE GEL ELECTROPHORESIS

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase

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10.1016/S0021-9258(18)45899-1

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11 November 2022

A simple model for proteins with interacting domains. Applications to scanning calorimetry data

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Study of strong to ultratight protein interactions using differential scanning calorimetry

31

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10.1016/S0021-9258(18)45899-1

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11 November 2022

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

32

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

Ligand-promoted weakening of intersubunit bonding domains in aspartate transcarbamoylase

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion

35

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

Genetic analysis of protein stability and function

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Functionally acceptable substitutions in two alpha-helical regions of lambda repressor.

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Mutational effects on protein stability

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Amino acid substitutions which stabilize aspartate transcarbamoylase in the R state disrupt both homotropic and heterotropic effects

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

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

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10.1016/S0021-9258(18)45899-1

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11 November 2022

A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamylase

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Importance of domain closure for homotropic cooperativity in Escherichia coli aspartate transcarbamylase.

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10.1016/S0021-9258(18)45899-1

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11 November 2022

Identification of residues involved in a conformational change accompanying substitutions for glutamate-43 in staphylococcal nuclease

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10.1016/S0021-9258(18)45899-1

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11 November 2022

A mutant T4 lysozyme displays five different crystal conformations

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution

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10.1016/S0021-9258(18)45899-1

https://api.crossref.org/works/10.1016/S0021-9258(18)45899-1

11 November 2022

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PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

18 December 2017

http://europepmc.org/abstract/MED/1733944

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