Aspartate transcarbamylase from Escherichia coli: activity and regulation.
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In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assemblyRandom circular permutation leading to chain disruption within and near alpha helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability, and functionAllosteric 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 transcarbamoylaseAssessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunitELISA: structure-function inferences based on statistically significant and evolutionarily inspired observationsFrom Genome to Structure and Back Again: A Family Portrait of the TranscarbamylasesBinding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulationHuman ornithine transcarbamylase: crystallographic insights into substrate recognition and conformational changesStructure of the catalytic trimer ofMethanococcus jannaschiiaspartate transcarbamoylase in an orthorhombic crystal formCrystallographic Snapshots of the Complete Catalytic Cycle of the Unregulated Aspartate Transcarbamoylase from Bacillus subtilisTrapping and structure determination of an intermediate in the allosteric transition 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 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 transcarbamoylaseThe crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperaturesTime Evolution of the Quaternary Structure of Escherichia coli Aspartate Transcarbamoylase upon Reaction with the Natural Substrates and a Slow, Tight-Binding InhibitorA mutation in the S-switch region of the Runt domain alters the dynamics of an allosteric network responsible for CBFbeta regulation.Ligand depletion in vivo modulates the dynamic range and cooperativity of signal transduction.Asymmetric allosteric signaling in aspartate transcarbamoylase.Natural selection of more designable folds: a mechanism for thermophilic adaptation.Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase.A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase.Cytoophidium assembly reflects upregulation of IMPDH activity.Glu-50 in the catalytic chain of Escherichia coli aspartate transcarbamoylase plays a crucial role in the stability of the R quaternary structure.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.In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.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.Conformational selection or induced fit? 50 years of debate resolved.Temperature effects on the allosteric responses of native and chimeric aspartate transcarbamoylases.Conversion of the allosteric regulatory patterns of aspartate transcarbamoylase by exchange of a single beta-strand between diverged regulatory chains.Structure and expression of a pyrimidine gene cluster from the extreme thermophile Thermus strain ZO5Allosteric signal transmission involves synergy between discrete structural units of the regulatory subunit of aspartate transcarbamoylase.Expression, purification, crystallization and preliminary X-ray crystallographic studies of a cold-adapted aspartate carbamoyltransferase from Moritella profunda.Overexpression, purification, crystallization and preliminary structural studies of catabolic ornithine transcarbamylase from Lactobacillus hilgardii.New experimental approaches for investigating interactions between Pyrococcus furiosus carbamate kinase and carbamoyltransferases, enzymes involved in the channeling of thermolabile carbamoyl phosphate.Aspartate-90 and arginine-269 of hamster aspartate transcarbamylase affect the oligomeric state of a chimaeric protein with an Escherichia coli maltose-binding domain.
P2860
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P2860
Aspartate transcarbamylase from Escherichia coli: activity and regulation.
description
1994 nî lūn-bûn
@nan
1994 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Aspartate transcarbamylase from Escherichia coli: activity and regulation.
@ast
Aspartate transcarbamylase from Escherichia coli: activity and regulation.
@en
Aspartate transcarbamylase from Escherichia coli: activity and regulation.
@nl
type
label
Aspartate transcarbamylase from Escherichia coli: activity and regulation.
@ast
Aspartate transcarbamylase from Escherichia coli: activity and regulation.
@en
Aspartate transcarbamylase from Escherichia coli: activity and regulation.
@nl
prefLabel
Aspartate transcarbamylase from Escherichia coli: activity and regulation.
@ast
Aspartate transcarbamylase from Escherichia coli: activity and regulation.
@en
Aspartate transcarbamylase from Escherichia coli: activity and regulation.
@nl
P1476
Aspartate transcarbamylase from Escherichia coli: activity and regulation.
@en
P2093
W N Lipscomb
P304
P577
1994-01-01T00:00:00Z