Subunit structure of aspartate transcarbamylase from Escherichia coli.
about
Genetics and biochemistry of carbamoyl phosphate biosynthesis and its utilization in the pyrimidine biosynthetic pathwayAmine cations promote concurrent conversion of prohistidine decarboxylase from Lactobacillus 30a to active enzyme and a modified proenzyme.Mammalian aspartate transcarbamylase (ATCase): sequence of the ATCase domain and interdomain linker in the CAD multifunctional polypeptide and properties of the isolated domain.An intermediate complex in the dissociation of aspartate transcarbamylase.Complex of aspartate carbamoyltransferase from Escherichia coli with its allosteric inhibitor, cytidine triphosphate: electron density at 5.9-angstroms resolution.Ligand-promoted weakening of intersubunit bonding domains in aspartate transcarbamolylaseCooperative interactions in aspartate transcarbamoylase. 1. Hybrids composed of native and chemically inactivated catalytic polypeptide chains.Evolutionary divergence of genes for ornithine and aspartate carbamoyl-transferases--complete sequence and mode of regulation of the Escherichia coli argF gene; comparison of argF with argI and pyrB.Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase.Association of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability.Genes encoding Escherichia coli aspartate transcarbamoylase: the pyrB-pyrI operon.Communication between catalytic subunits in hybrid aspartate transcarbamoylase molecules: effect of ligand binding to active chains on the conformation of unliganded, inactive chains.Communication between dissimilar subunits in aspartate transcarbamoylase: effect of inhibitor and activator on the conformation of the catalytic polypeptide chains.Aspartate transcarbamoylase molecules lacking one regulatory subunit.Pathways of assembly of aspartate transcarbamoylase from catalytic and regulatory subunits.Quaternary constraint in hybrid of aspartate transcarbamylase containing wild-type and mutant catalytic subunits.Localization of the zinc binding site of aspartate transcarbamoylase in the regulatory subunit.The thiol group in the catalytic chains of aspartate transcarbamoylase.Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residue.Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphateA 70-amino acid zinc-binding polypeptide from the regulatory chain of aspartate transcarbamoylase forms a stable complex with the catalytic subunit leading to markedly altered enzyme activityA kinetic model of cooperativity in aspartate transcarbamylase.Experimental evidence for the role of cross-relaxation in proton nuclear magnetic resonance spin lattice relaxation time measurements in proteins.Wheat-germ aspartate transcarbamoylase. Kinetic behaviour suggesting an allosteric mechanism of regulation.Enzyme forms produced from aspartate transcarbamoylase by digestion with trypsin.Activation of Latent Dihydroorotase from Aquifex aeolicus by Pressure.
P2860
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P2860
Subunit structure of aspartate transcarbamylase from Escherichia coli.
description
1971 nî lūn-bûn
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name
Subunit structure of aspartate transcarbamylase from Escherichia coli.
@en
Subunit structure of aspartate transcarbamylase from Escherichia coli.
@nl
type
label
Subunit structure of aspartate transcarbamylase from Escherichia coli.
@en
Subunit structure of aspartate transcarbamylase from Escherichia coli.
@nl
prefLabel
Subunit structure of aspartate transcarbamylase from Escherichia coli.
@en
Subunit structure of aspartate transcarbamylase from Escherichia coli.
@nl
P1476
Subunit structure of aspartate transcarbamylase from Escherichia coli.
@en
P2093
Rosenbusch JP
P304
P407
P577
1971-03-01T00:00:00Z