Substrate-induced conformational change in a trimeric ornithine transcarbamoylase (Q27742450)

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M T McCann

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M Tuchman

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N M Allewell

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

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language of work or name

English

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publication date

2 September 1997

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published in

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volume

94

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issue

18

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page(s)

9550-5

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cites work

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Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase

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A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer

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Association of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability

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Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association

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Pathways of assembly of aspartate transcarbamoylase from catalytic and regulatory subunits

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

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

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

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A 70-amino acid zinc-binding polypeptide from the regulatory chain of aspartate transcarbamoylase forms a stable complex with the catalytic subunit leading to markedly altered enzyme activity

29 September 2017

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

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Differential scanning calorimetry of asparate transcarbamoylase and its isolate subunits

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Calorimetric analysis of aspartate transcarbamylase from Escherichia coli. Binding of substrates and substrate analogs to the native enzyme and catalytic subunit

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

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Ornithine Carbamoyltransferase from Escherichia coli W. Purification, Structure and Steady-State Kinetic Analysis

29 September 2017

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29 September 2017

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Homologous control sites and DNA transcription starts in the related argF and argI genes of Escherichia coli K12

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Conformational changes in proteins as measured by difference sedimentation studies. II. Effect of stereospecific ligands on the catalytic subunit of aspartate transcarbamylase

2 June 2018

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Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate

2 June 2018

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2 June 2018

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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

2 June 2018

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From allostery to mutagenesis: 20 years with aspartate transcarbamoylase

2 June 2018

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X-ray diffraction analysis on single crystals of recombinant Escherichia coli ornithine transcarbamoylase.

2 June 2018

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Effects of ATP and CTP on the conformation of the regulatory subunit of Escherichia coli aspartate transcarbamylase in solution: a medium-resolution hydrogen exchange study.

2 June 2018

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Triggering of allostery in an enzyme by a point mutation: ornithine transcarbamoylase.

2 June 2018

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Molecular evolution of enzyme structure: construction of a hybrid hamster/Escherichia coli aspartate transcarbamoylase.

2 June 2018

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Zn2+ regulation of ornithine transcarbamoylase. I. Mechanism of action.

2 June 2018

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Converting catabolic ornithine carbamoyltransferase to an anabolic enzyme.

2 June 2018

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Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylase.

2 June 2018

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Identification of 'private' mutations in patients with ornithine transcarbamylase deficiency.

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Mutations and polymorphisms in the human ornithine transcarbamylase gene

21 January 2018

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Expression, purification and kinetic characterization of wild-type human ornithine transcarbamylase and a recurrent mutant that produces 'late onset' hyperammonaemia

21 January 2018

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'Late onset' ornithine transcarbamylase deficiency: function of three purified recombinant mutant enzymes.

21 January 2018

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

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Relative frequency of mutations causing ornithine transcarbamylase deficiency in 78 families

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Ligand-induced isomerizations of Escherichia coli ornithine transcarbamoylase. An ultraviolet difference analysis

21 January 2018

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27 November 2018

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Reconstruction of an enzyme by domain substitution effectively switches substrate specificity

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Crystallization and preliminary X-ray study of the catalytic subunit of aspartate transcarbamylase

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Zn2+ regulation of ornithine transcarbamoylase. II. Metal binding site

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Effect of succinate on the translational diffusion coefficient of aspartate transcarbamylase

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

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

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