Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate.
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Random circular permutation leading to chain disruption within and near alpha helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability, and functionImportance of the loop at residues 230-245 in the allosteric interactions of Escherichia coli aspartate carbamoyltransferaseReplacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylaseThree-dimensional structure of carbamoyl phosphate and succinate bound to aspartate carbamoyltransferase.Effects of ciprofloxacin on eucaryotic pyrimidine nucleotide biosynthesis and cell growthAssessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunitBinding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulationArginine 54 in the active site of escherichia coli aspartate transcarbamoylase is critical for catalysis: A site-specific mutagenesis, NMR, and X-ray crystallographic studyCrystallographic Snapshots of the Complete Catalytic Cycle of the Unregulated Aspartate Transcarbamoylase from Bacillus subtilisExploring the role of conformational heterogeneity in cis-autoproteolytic activation of ThnT.Structure and mechanisms of Escherichia coli aspartate transcarbamoylaseSubstrate-induced conformational change in a trimeric ornithine transcarbamoylaseA novel mechanism for resistance to the antimetabolite N-phosphonoacetyl-L-aspartate by Helicobacter pylori.Recent Advances in Drug Design and Drug Discovery for Androgen- Dependent Diseases.Structural transitions in crystals of native aspartate carbamoyltransferase.Transcription-coupled and DNA damage-dependent ubiquitination of RNA polymerase II in vitroShared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis.A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transitionLigand-promoted weakening of intersubunit bonding domains in aspartate transcarbamolylaseDifferential requirement for p19ARF in the p53-dependent arrest induced by DNA damage, microtubule disruption, and ribonucleotide depletionStructure-activity studies on phosphonoacetate.Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase.Design, synthesis, and bioactivity of novel inhibitors of E. coli aspartate transcarbamoylase.Multiple mechanisms of N-phosphonacetyl-L-aspartate resistance in human cell lines: carbamyl-P synthetase/aspartate transcarbamylase/dihydro-orotase gene amplification is frequent only when chromosome 2 is rearranged.Allostery and cooperativity in Escherichia coli aspartate transcarbamoylaseAn active site-tail interaction in the structure of hexahistidine-tagged Thermoplasma acidophilum citrate synthase.Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase.Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure.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.Ligation alters the pathway of urea-induced denaturation of the catalytic trimer of Escherichia coli aspartate transcarbamylaseWeakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylaseThe allosteric activator ATP induces a substrate-dependent alteration of the quaternary structure of a mutant aspartate transcarbamoylase impaired in active site closureThe 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativityGross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution studyPropagation of conformational changes in Ni(II)-substituted aspartate transcarbamoylase: effect of active-site ligands on the regulatory chainsThe nucleotide synthesis enzyme CAD inhibits NOD2 antibacterial function in human intestinal epithelial cellsCharacterization of an episome produced in hamster cells that amplify a transfected CAD gene at high frequency: functional evidence for a mammalian replication originN-phosphonacetyl-L-isoasparagine a potent and specific inhibitor of Escherichia coli aspartate transcarbamoylase.Escherichia coli aspartate transcarbamylase: a novel marker for studies of gene amplification and expression in mammalian cells.Substitutions in the aspartate transcarbamoylase domain of hamster CAD disrupt oligomeric structure
P2860
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P2860
Aspartate transcarbamylase. Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate.
description
1971 nî lūn-bûn
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name
Aspartate transcarbamylase. Interaction with the transition state analogue N-
@nl
Aspartate transcarbamylase. In ...... -(phosphonacetyl)-L-aspartate.
@en
type
label
Aspartate transcarbamylase. Interaction with the transition state analogue N-
@nl
Aspartate transcarbamylase. In ...... -(phosphonacetyl)-L-aspartate.
@en
prefLabel
Aspartate transcarbamylase. Interaction with the transition state analogue N-
@nl
Aspartate transcarbamylase. In ...... -(phosphonacetyl)-L-aspartate.
@en
P1476
Aspartate transcarbamylase. In ...... -(phosphonacetyl)-L-aspartate.
@en
P2093
P304
P407
P577
1971-11-01T00:00:00Z