Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamoylase.
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Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase.Replacement 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 transcarbamoylaseArginine 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 transcarbamoylaseCrystallographic Snapshots of the Complete Catalytic Cycle of the Unregulated Aspartate Transcarbamoylase from Bacillus subtilisNew Insight into the Transcarbamylase Family: The Structure of Putrescine Transcarbamylase, a Key Catalyst for Fermentative Utilization of AgmatineStructure and mechanisms of Escherichia coli aspartate transcarbamoylaseSubstrate-induced conformational change in a trimeric ornithine transcarbamoylaseMammalian aspartate transcarbamylase (ATCase): sequence of the ATCase domain and interdomain linker in the CAD multifunctional polypeptide and properties of the isolated domain.Subunit-destabilizing mutations in Drosophila copper/zinc superoxide dismutase: neuropathology and a model of dimer dysequilibriumShared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis.Allostery and cooperativity in Escherichia coli aspartate transcarbamoylaseIn vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains.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.Remodeling domain interfaces to enhance heterodimer formationSubunit structure of a class A aspartate transcarbamoylase from Pseudomonas fluorescens.Protein engineering. The design, synthesis and characterization of factitious proteins.Dissociation of enzyme oligomers: a mechanism for allosteric regulation.240s loop interactions stabilize the T state of Escherichia coli aspartate transcarbamoylase.Aspartate Transcarbamylase from Escherichia Coli: Activity and Regulation
P2860
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P2860
Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamoylase.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on January 1985
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Regeneration of active enzyme ...... f aspartate transcarbamoylase.
@en
Regeneration of active enzyme ...... f aspartate transcarbamoylase.
@nl
type
label
Regeneration of active enzyme ...... f aspartate transcarbamoylase.
@en
Regeneration of active enzyme ...... f aspartate transcarbamoylase.
@nl
prefLabel
Regeneration of active enzyme ...... f aspartate transcarbamoylase.
@en
Regeneration of active enzyme ...... f aspartate transcarbamoylase.
@nl
P2860
P356
P1476
Regeneration of active enzyme ...... f aspartate transcarbamoylase.
@en
P2093
H K Schachman
P2860
P304
P356
10.1073/PNAS.82.2.361
P407
P577
1985-01-01T00:00:00Z