about
Cooperative bindingAllosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutaseStructure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolutionDynamic dissociating homo-oligomers and the control of protein functionReplacement 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 transcarbamoylaseMethods for the Measurement of a Bacterial Enzyme Activity in Cell Lysates and Extracts.Zinc as Allosteric Ion Channel Modulator: Ionotropic Receptors as MetalloproteinsThe concept of allosteric interaction and its consequences for the chemistry of the brainBinding 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 studyThe first high pH structure ofEscherichia coliaspartate transcarbamoylaseThe Pathway of Product Release from the R State of Aspartate TranscarbamoylaseA Cooperative Escherichia coli Aspartate Transcarbamoylase without Regulatory Subunits,Crystallographic Snapshots of the Complete Catalytic Cycle of the Unregulated Aspartate Transcarbamoylase from Bacillus subtilisMetal Ion Involvement in the Allosteric Mechanism of Escherichia coli Aspartate TranscarbamoylaseAllosteric regulation and substrate activation in cytosolic nucleotidase II fromLegionella pneumophilaStructure and mechanisms of Escherichia coli aspartate transcarbamoylaseSubstrate-induced conformational change in a trimeric ornithine transcarbamoylaseRegulation of pyrimidine biosynthesis in Saccharomyces cerevisiae.Crystal structure of the Glu-239----Gln mutant of aspartate carbamoyltransferase at 3.1-A resolution: an intermediate quaternary structure.Purification and properties of 3-deoxy-d-arabinoheptulosonic acid-7-phosphate synthetase (phe) from a lambda aroG+ transductant of Escherichia coli.Statistical mechanics of Monod-Wyman-Changeux (MWC) models.Directed evolution of protein switches and their application to the creation of ligand-binding proteins.EFFECTS OF HYDROSTATIC PRESSURE ON MICROBIAL SYSTEMSLigand depletion in vivo modulates the dynamic range and cooperativity of signal transduction.Achieving optimal growth through product feedback inhibition in metabolismGenetics and biochemistry of carbamoyl phosphate biosynthesis and its utilization in the pyrimidine biosynthetic pathwayStatistical Mechanics of Allosteric Enzymes.Bacterial and protozoal communities and fatty acid profile in the rumen of sheep fed a diet containing added tannins.Kinetics and regulation of the salt-dependent aspartate transcarbamylase of Halobacterium cutirubrum.Sequence of enzyme synthesis and gene replication during the cell cycle of Bacillus subtilisHybridization of native and chemically modified enzymes. 3. The catalytic subunits of aspartate transcarbamylaseIn 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.RNA polymerase involvement in the regulation of expression of Salmonella typhimurium pyr genes. Isolation and characterization of a fluorouracil-resistant mutant with high, constitutive expression of the pyrB and pyrE genes due to a mutation in rpoBA 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase.pryB mutations as suppressors of arginine auxotrophy in Salmonella typhimurium.Aspartate transcarbamoylase from Escherichia coli: electron density at 5.5 A resolution.
P2860
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P2860
description
1962 nî lūn-bûn
@nan
1962 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1962 թվականի մարտին հրատարակված գիտական հոդված
@hy
1962年の論文
@ja
1962年論文
@yue
1962年論文
@zh-hant
1962年論文
@zh-hk
1962年論文
@zh-mo
1962年論文
@zh-tw
1962年论文
@wuu
name
The enzymology of control by feedback inhibition.
@ast
The enzymology of control by feedback inhibition.
@en
type
label
The enzymology of control by feedback inhibition.
@ast
The enzymology of control by feedback inhibition.
@en
prefLabel
The enzymology of control by feedback inhibition.
@ast
The enzymology of control by feedback inhibition.
@en
P1476
The enzymology of control by feedback inhibition
@en
P2093
P304
P407
P577
1962-03-01T00:00:00Z