Crystallographic determination of symmetry of aspartate transcarbamylase.
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Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutaseStructure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolutionThree-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase.Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolutionDihydroorotase from the Hyperthermophile Aquifiex aeolicus Is Activated by Stoichiometric Association with Aspartate Transcarbamoylase and Forms a One-Pot Reactor for Pyrimidine Biosynthesis † ‡The Pathway of Product Release from the R State of Aspartate TranscarbamoylaseStructure of the catalytic chain ofMethanococcus jannaschiiaspartate transcarbamoylase in a hexagonal crystal form: insights into the path of carbamoyl phosphate to the active site of the enzymeStructure and mechanisms of Escherichia coli aspartate transcarbamoylaseX-ray Scattering Studies of Protein Structural Dynamics.Crystal structure of the Glu-239----Gln mutant of aspartate carbamoyltransferase at 3.1-A resolution: an intermediate quaternary structure.Ligand depletion in vivo modulates the dynamic range and cooperativity of signal transduction.Genetics and biochemistry of carbamoyl phosphate biosynthesis and its utilization in the pyrimidine biosynthetic pathwayStatistical Mechanics of Allosteric Enzymes.Hybridization of native and chemically modified enzymes. 3. The catalytic subunits of aspartate transcarbamylaseStructural transitions in crystals of native aspartate carbamoyltransferase.Mammalian aspartate transcarbamylase (ATCase): sequence of the ATCase domain and interdomain linker in the CAD multifunctional polypeptide and properties of the isolated domain.Aspartate transcarbamoylase from Escherichia coli: electron density at 5.5 A resolution.An intermediate complex in the dissociation of aspartate transcarbamylase.Complex of aspartate carbamoyltransferase from Escherichia coli with its allosteric inhibitor, cytidine triphosphate: electron density at 5.9-angstroms resolution.Pyrimidine metabolism in microorganismsLigand-promoted weakening of intersubunit bonding domains in aspartate transcarbamolylaseCooperative interactions in aspartate transcarbamoylase. 1. Hybrids composed of native and chemically inactivated catalytic polypeptide chains.Allostery and cooperativity in Escherichia coli aspartate transcarbamoylaseAssociation of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability.Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution studyAssembly of the aspartate transcarbamoylase holoenzyme from transcriptionally independent catalytic and regulatory cistrons.Genes encoding Escherichia coli aspartate transcarbamoylase: the pyrB-pyrI operon.Isolation and preliminary characterization of single amino acid substitution mutants of aspartate carbamoyltransferase.Communication between catalytic subunits in hybrid aspartate transcarbamoylase molecules: effect of ligand binding to active chains on the conformation of unliganded, inactive chains.Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: genetic organization, structure, and expression in Escherichia coli.Solution NMR Spectroscopy for the Study of Enzyme Allostery.Communication between dissimilar subunits in aspartate transcarbamoylase: effect of inhibitor and activator on the conformation of the catalytic polypeptide chains.Allosteric cofactor-mediated enzyme cooperativity: a theoretical treatment.Expression, purification, crystallization and preliminary X-ray diffraction analysis of the aspartate transcarbamoylase domain of human CAD.Aspartate transcarbamoylase molecules lacking one regulatory subunit.Pathways of assembly of aspartate transcarbamoylase from catalytic and regulatory subunits.Quaternary constraint in hybrid of aspartate transcarbamylase containing wild-type and mutant catalytic subunits.Localization of the zinc binding site of aspartate transcarbamoylase in the regulatory subunit.The thiol group in the catalytic chains of aspartate transcarbamoylase.Partial cDNA sequence to a hamster gene corrects defect in Escherichia coli pyrB mutant
P2860
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P2860
Crystallographic determination of symmetry of aspartate transcarbamylase.
description
1968 nî lūn-bûn
@nan
1968 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1968 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1968年の論文
@ja
1968年論文
@yue
1968年論文
@zh-hant
1968年論文
@zh-hk
1968年論文
@zh-mo
1968年論文
@zh-tw
1968年论文
@wuu
name
Crystallographic determination of symmetry of aspartate transcarbamylase.
@ast
Crystallographic determination of symmetry of aspartate transcarbamylase.
@en
Crystallographic determination of symmetry of aspartate transcarbamylase.
@nl
type
label
Crystallographic determination of symmetry of aspartate transcarbamylase.
@ast
Crystallographic determination of symmetry of aspartate transcarbamylase.
@en
Crystallographic determination of symmetry of aspartate transcarbamylase.
@nl
prefLabel
Crystallographic determination of symmetry of aspartate transcarbamylase.
@ast
Crystallographic determination of symmetry of aspartate transcarbamylase.
@en
Crystallographic determination of symmetry of aspartate transcarbamylase.
@nl
P356
P1433
P1476
Crystallographic determination of symmetry of aspartate transcarbamylase.
@en
P2093
P2507
P2888
P304
P356
10.1038/2181119A0
P407
P577
1968-06-01T00:00:00Z
P6179
1002348448