A Functional Analysis of the Allosteric Nucleotide Monophosphate Binding Site of Carbamoyl Phosphate Synthetase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference28 articles.
1. Control of Escherichia coli Carbamyl Phosphate Synthetase by Purine and Pyrimidine Nucleotides*
2. Carbamoyl phosphate synthetase: a crooked path from substrates to products
3. Bicarbonate-Dependent Cleavage of Adenosine Triphosphate and Other Reactions Catalyzed by Escherichia coli Carbamyl Phosphate Synthetase*
4. Control of the Activity of Escherichia coli Carbamoyl Phosphate Synthetase by Antagonistic Allosteric Effectors
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1. Mutations that improve efficiency of a weak-link enzyme are rare compared to adaptive mutations elsewhere in the genome;eLife;2019-12-09
2. Development of an engineered carbamoyl phosphate synthetase with released sensitivity to feedback inhibition by site-directed mutation and casting error-prone PCR;Enzyme and Microbial Technology;2019-10
3. Mutations that improve the efficiency of a weak-link enzyme are rare compared to adaptive mutations elsewhere in the genome;2019-04-30
4. Regulation of carbamoylphosphate synthesis in Escherichia coli: an amazing metabolite at the crossroad of arginine and pyrimidine biosynthesis;Amino Acids;2018-09-20
5. Metabolic engineering of Bacillus subtilis for the co-production of uridine and acetoin;Applied Microbiology and Biotechnology;2018-08-17
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