Catalytic-regulatory subunit interactions and allosteric effects in aspartate transcarbamylase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference55 articles.
1. L-Alanosine: a noncooperative substrate for Escherichia coli aspartate transcarbamylase
2. Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli.
3. Allosteric regulation of aspartate transcarbamoylase. Effect of active site ligands on the reactivity of sulfhydryl groups of the regulatory subunits
4. Equilibrium and kinetic studies of the association of catalytic and regulatory subunits of aspartate transcarbamoylase.
5. Spectrophotometric Study of the Reaction of Protein Sulfhydryl Groups with Organic Mercurials
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1. Aspartate Transcarbamylase from Escherichia Coli: Activity and Regulation;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
2. The conserved residues glutamate-37, aspartate-100, and arginine-269, are important for the structural stabilization of Escherichia coli aspartate transcarbamoylase;Biochemistry;1993-09-28
3. A putative zinc finger protein, Saccharomyces cerevisiae Vps18p, affects late Golgi functions required for vacuolar protein sorting and efficient alpha-factor prohormone maturation;Molecular and Cellular Biology;1991-12
4. Different amino acid substitutions at the same position in the nucleotide-binding site of aspartate transcarbamoylase have diverse effects on the allosteric properties of the enzyme.;Journal of Biological Chemistry;1991-11
5. Function of serine-52 and serine-80 in the catalytic mechanism of Escherichia coli aspartate transcarbamoylase;Biochemistry;1991-03
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