(Q44164525)

30 November 2017

title

Stabilization of the R allosteric structure of Escherichia coli aspartate transcarbamoylase by disulfide bond formation (English)

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30 November 2017

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Jay M West

1

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30 November 2017

Hiro Tsuruta

series ordinal

2

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30 November 2017

Evan R Kantrowitz

series ordinal

3

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30 November 2017

language of work or name

English

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publication date

30 September 2002

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Journal of Biological Chemistry

30 November 2017

published in

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30 November 2017

volume

277

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30 November 2017

issue

49

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30 November 2017

page(s)

47300-47304

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In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase

30 November 2017

cites work

1 reference

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

21 January 2018

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

21 January 2018

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Escherichia coli aspartate transcarbamylase: the relation between structure and function

21 January 2018

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

21 January 2018

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Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition

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

21 January 2018

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Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure

21 January 2018

1 reference

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Unlike the quaternary structure transition, the tertiary structure change of the 240s loop in allosteric aspartate transcarbamylase requires active site saturation by substrate for completion

21 January 2018

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Rapid and efficient site-specific mutagenesis without phenotypic selection

21 January 2018

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Propagation of allosteric changes through the catalytic-regulatory interface of Escherichia coli aspartate transcarbamylase

21 January 2018

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The conserved residues glutamate-37, aspartate-100, and arginine-269 are important for the structural stabilization of Escherichia coli aspartate transcarbamoylase.

21 January 2018

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Production of single-stranded plasmid DNA

21 January 2018

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

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DISC ELECTROPHORESIS. I. BACKGROUND AND THEORY

21 January 2018

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

21 January 2018

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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

21 January 2018

1 reference

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The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop containing residues 230-245 of the catalytic chain

21 January 2018

1 reference

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

21 January 2018

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

21 January 2018

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Kinetic mechanism of native Escherichia coli aspartate transcarbamylase.

21 January 2018

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Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism.

21 January 2018

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

21 January 2018

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

21 January 2018

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Hybrid aspartate transcarbamoylase containing cross-linked subunits

21 January 2018

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NEGATIVE AND POSITIVE ION MASS ANALYSIS OF DICARBOXYLIC ACIDS IN STUDIES ON THE MECHANISM OF THE METHYLMALONYL ISOMERASE REACTION

21 January 2018

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An improved colorimetric assay for aspartate and ornithine transcarbamylases

21 January 2018

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

21 January 2018

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Analysis of two purified mutants of Escherichia coli aspartate transcarbamylase with single amino acid substitutions

21 January 2018

1 reference

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Three of the six possible intersubunit stabilizing interactions involving Glu-239 are sufficient for restoration of the homotropic and heterotropic properties of Escherichia coli aspartate transcarbamoylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209913200

Kinetic consequences of site-specific mutation of Glu-239----Gln in E. coli aspartate transcarbamylase: comparison with catalytic subunits and Phe-240 mutant enzyme

21 January 2018

1 reference

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Coupling of homotropic and heterotropic interactions in Escherichia coli aspartate transcarbamylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M209913200

21 January 2018

Identifiers

DOI

10.1074/JBC.M209913200

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30 November 2017

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