2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate.
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Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutaseReplacement 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.Michaelis and Menten and the long road to the discovery of cooperativityMechanism of inactivation of ornithine transcarbamoylase by Ndelta -(N'-Sulfodiaminophosphinyl)-L-ornithine, a true transition state analogue? Crystal structure and implications for catalytic mechanismBinding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulationThe conserved cis-Pro39 residue plays a crucial role in the proper positioning of the catalytic base Asp38 in ketosteroid isomerase from Comamonas testosteroniArginine 54 in the active site of escherichia coli aspartate transcarbamoylase is critical for catalysis: A site-specific mutagenesis, NMR, and X-ray crystallographic studyA single mutation in the active site swaps the substrate specificity ofN-acetyl-L-ornithine transcarbamylase andN-succinyl-L-ornithine transcarbamylaseThe first high pH structure ofEscherichia coliaspartate transcarbamoylaseMolecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolutionThe mononuclear metal center of type-I dihydroorotase from aquifex aeolicusStructure and mechanisms of Escherichia coli aspartate transcarbamoylaseCrystal structure of Pseudomonas aeruginosa catabolic ornithine transcarbamoylase at 3.0-A resolution: a different oligomeric organization in the transcarbamoylase familySubstrate-induced conformational change in a trimeric ornithine transcarbamoylaseTime Evolution of the Quaternary Structure of Escherichia coli Aspartate Transcarbamoylase upon Reaction with the Natural Substrates and a Slow, Tight-Binding InhibitorCrystal structure of the Glu-239----Gln mutant of aspartate carbamoyltransferase at 3.1-A resolution: an intermediate quaternary structure.In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase.Structural transitions in crystals of native aspartate carbamoyltransferase.Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains.Mammalian aspartate transcarbamylase (ATCase): sequence of the ATCase domain and interdomain linker in the CAD multifunctional polypeptide and properties of the isolated domain.The contribution of individual interchain interactions to the stabilization of the T and R states of Escherichia coli aspartate transcarbamoylase.Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase.Cloning and expression of the aspartate carbamoyltransferase gene from Treponema denticola.Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase.Molecular dynamics simulations and rigid body (TLS) analysis of aspartate carbamoyltransferase: evidence for an uncoupled R stateAssociation of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability.Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylaseStructural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase.The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativityThe use of nucleotide analogs to evaluate the mechanism of the heterotropic response of Escherichia coli aspartate transcarbamoylase.Fixation of allosteric states of the nicotinic acetylcholine receptor by chemical cross-linking.Subunit structure of a class A aspartate transcarbamoylase from Pseudomonas fluorescens.Aspartate transcarbamylase from the deep-sea hyperthermophilic archaeon Pyrococcus abyssi: genetic organization, structure, and expression in Escherichia coli.General base-general acid catalysis by terpenoid cyclases.1H NMR studies on the catalytic subunit of aspartate transcarbamoylase.Role of a carboxyl-terminal helix in the assembly, interchain interactions, and stability of aspartate transcarbamoylase.Heterotropic interactions in aspartate transcarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation.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.Aspartate carbamoyltransferase from the thermoacidophilic archaeon Sulfolobus acidocaldarius. Cloning, sequence analysis, enzyme purification and characterization.
P2860
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P2860
2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate.
description
1987 nî lūn-bûn
@nan
1987 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
2.5 A structure of aspartate c ...... with the bisubstrate analog N-
@nl
2.5 A structure of aspartate c ...... -(phosphonacetyl)-L-aspartate.
@ast
2.5 A structure of aspartate c ...... -(phosphonacetyl)-L-aspartate.
@en
type
label
2.5 A structure of aspartate c ...... with the bisubstrate analog N-
@nl
2.5 A structure of aspartate c ...... -(phosphonacetyl)-L-aspartate.
@ast
2.5 A structure of aspartate c ...... -(phosphonacetyl)-L-aspartate.
@en
prefLabel
2.5 A structure of aspartate c ...... with the bisubstrate analog N-
@nl
2.5 A structure of aspartate c ...... -(phosphonacetyl)-L-aspartate.
@ast
2.5 A structure of aspartate c ...... -(phosphonacetyl)-L-aspartate.
@en
P2093
P1476
2.5 A structure of aspartate c ...... -(phosphonacetyl)-L-aspartate.
@en
P2093
K L Krause
W N Lipscomb
P304
P356
10.1016/0022-2836(87)90265-8
P407
P577
1987-02-01T00:00:00Z