(Q34339261)

1 August 2017

1 reference

title

Aspartate transcarbamylase from Escherichia coli: activity and regulation (English)

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1 August 2017

Aspartate Transcarbamylase from Escherichia Coli: Activity and Regulation (English)

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W N Lipscomb

1

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1 August 2017

William N. Lipscomb

series ordinal

1

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publication date

1 January 1994

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Advances in Enzymology and Related Areas of Molecular Biology

1 August 2017

22 November 2006

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published in

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1 August 2017

volume

68

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1 August 2017

page(s)

67-151

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CARBAMYL PHOSPHATE, THE CARBAMYL DONOR IN ENZYMATIC CITRULLINE SYNTHESIS1

1 August 2017

cites work

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Aspartate Carbamyl Transferase from Escherichia coli

21 January 2018

1 reference

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

21 January 2018

1 reference

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Ueber einen in biologischer Beziehung wichtigen Einfluss, den die Kohlensäurespannung des Blutes auf dessen Sauerstoffbindung übt1

21 January 2018

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Allosteric proteins and cellular control systems

21 January 2018

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

21 January 2018

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https://api.crossref.org/works/10.1002%2F9780470123140.CH3

The Oxygen Equilibrium of Hemoglobin and Its Structural Interpretation

21 January 2018

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https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Allosteric interactions in aspartate transcarbamylase. 3. Interpretation of experimental data in terms of the model of Monod, Wyman, and Changeux

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Crystallographic Determination of Symmetry of Aspartate Transcarbamylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

The structure of aspartate transcarbamylase, I. A molecular twofold axis in the complex with cytidine triphosphate

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

The 5.5 A Resolution Structure of the Regulatory Enzyme, Aspartate Transcarbamylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Escherichia coli aspartate transcarbamylase: the relation between structure and function

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Escherichia coli aspartate carbamoyltransferase: the probing of crystal structure analysis via site-specific mutagenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Allosteric control of quaternary states in E. coli aspartate transcarbamylase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Mechanisms of cooperativity and allosteric regulation in proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Molecular evolution and genetic engineering of protein domains involving aspartate transcarbamoylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Enzyme forms produced from aspartate transcarbamoylase by digestion with trypsin

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Binding of cytidine triphosphate to aspartate transcarbamylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Calorimetric analysis of aspartate transcarbamylase from Escherichia coli. Binding of cytosine 5'-triphosphate and adenosine 5'-triphosphate

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

L-alanosine: a noncooperative substrate for Escherichia coli aspartate transcarbamylase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

The Combinations of Haemoglobin with Oxygen and with Carbon Monoxide. I

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Conformational changes in proteins as measured by difference sedimentation studies. I. Technique for measuring small changes in sedimentation coefficient

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Relaxation spectra of aspartate transcarbamylase. I. Interaction of 5-bromocytidine triphosphate with native enzyme and regulatory subunit

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Local and gross conformational changes in aspartate transcarbamylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution study

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Nucleotide sequence of the structural gene (pyrB) that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

From allostery to mutagenesis: 20 years with aspartate transcarbamoylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Concerted allosteric transition in hybrids of aspartate transcarbamoylase containing different arrangements of active and inactive sites.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8-A resolution and neutral pH

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Three-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Carbon-13 and nitrogen-15 isotope effects as a probe of the chemical mechanism of Escherichia coli aspartate transcarbamylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Ionization of amino acid residues involved in the catalytic mechanism of aspartate transcarbamoylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Oligonucleotide-directed mutagenesis using M13-derived vectors: an efficient and general procedure for the production of point mutations in any fragment of DNA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Function of serine-52 and serine-80 in the catalytic mechanism of Escherichia coli aspartate transcarbamoylase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Function of threonine-55 in the carbamoyl phosphate binding site of Escherichia coli aspartate transcarbamoylase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Effects of replacement of active site residue glutamine 231 on activity and allosteric properties of aspartate transcarbamoylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8-A resolution and neutral pH

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Importance of a conserved residue, aspartate-162, for the function of Escherichia coli aspartate transcarbamoylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Importance of the loop at residues 230-245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Structural transitions in crystals of native aspartate carbamoyltransferase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Crystal structure of the Glu-239----Gln mutant of aspartate carbamoyltransferase at 3.1-A resolution: an intermediate quaternary structure

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Structural consequences of the replacement of Glu239 by Gln in the catalytic chain of Escherichia coli aspartate transcarbamylase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Topology of Binding Sites for Carbamyl Phosphate in Aspartate Transcarbamylase from Escherichia coli. The Use of Pyridoxal Phosphate as Covalent Probe

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Heterotropic interactions in aspartate transcarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Heat capacity and entropy changes in processes involving proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Structural energetics of peptide recognition: Angiotensin II/antibody binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

A molecular mechanism for pyrimidine and purine nucleotide control of aspartate transcarbamoylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residue

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

An aspartate transcarbamylase lacking catalytic subunit interactions. II. Regulatory subunits are responsible for the lack of co-operative interactions between catalytic sites. Drastic feedback inhibition does not restore these interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Interaction of tetraiodofluorescein with a modified form of aspartate transcarbamylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Spin-labeling studies of aspartate transcarbamylase. I. Effects of nucleotide binding and subunit separation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Interaction of aspartate transcarbamylase with 5-bromocytidine 5'-tri-, di-, and monophosphates

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Modes of modifier action in E. coli aspartate transcarbamylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Interactions of ionizable groups in Escherichia coli aspartate transcarbamylase with adenosine and cytidine 5'-triphosphates.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Ligand binding and protein dynamics: a fluorescence depolarization study of aspartate transcarbamylase from Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Communication between dissimilar subunits in aspartate transcarbamoylase: Effect of inhibitor and activator on the conformation of the catalytic polypeptide chains

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Heterotropic interactions in Escherichia coli aspartate transcarbamylase. Subunit interfaces involved in CTP inhibition and ATP activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Lysine-60 in the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for the discrimination between CTP and ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

ATP-liganded form of aspartate transcarbamoylase, the logical regulatory target for allosteric control in divergent bacterial systems

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Protein differentiation: a comparison of aspartate transcarbamoylase and ornithine transcarbamoylase from Escherichia coli K-12

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Zn(II)-induced cooperativity of Escherichia coli ornithine transcarbamoylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Wheat-germ aspartate transcarbamoylase. Kinetic behaviour suggesting an allosteric mechanism of regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

New Structural Model of E. coli Aspartate Transcarbamylase and the Amino-acid Sequence of the Regulatory Polypeptide Chain

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

Mutation of gene encoding regulatory polypeptide of aspartate carbamoyltransferase

21 January 2018

1 reference

https://api.crossref.org/works/10.1002%2F9780470123140.CH3

10.1002/9780470123140.CH3

21 January 2018

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1 reference