E.coli aspartokinase II-homoserine dehydrogenase II polypeptide chain has a triglobular structure
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference13 articles.
1. The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K12. The Two Catalytic Activities Are Carried by Two Independent Regions of the Polypeptide Chain
2. A triglobular model for the polypeptide chain of aspartokinase I-homoserine dehydrogenase I of Escherichia coli
3. Proteolysis of the bifunctional methionine-repressible aspartokinase II-homoserine dehydrogenase II of Escherichia coli K12. Production of an active homoserine dehydrogenase fragment.
4. Nucleotide sequence of the metL gene of Escherichia coli. Its product, the bifunctional aspartokinase ii-homoserine dehydrogenase II, and the bifunctional product of the thrA gene, aspartokinase I-homoserine dehydrogenase I, derive from a common ancestor.
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1. In silico strategy to rationally engineer metabolite production: A case study for threonine inEscherichia coli;Biotechnology and Bioengineering;2009-06-15
2. Characterization of the aspartate kinase from Saccharomyces cerevisiae and of its interaction with threonine;Biochemical and Biophysical Research Communications;2004-08
3. Conversion of feedback regulation in aspartate kinase by domain exchange;Biochemical and Biophysical Research Communications;2004-04
4. Molecular Genetics of the Maize (Zea mays L.) Aspartate Kinase-Homoserine Dehydrogenase Gene Family;Plant Physiology;1994-12-01
5. Evolutionary relationships between yeast and bacterial homoserine dehydrogenases;FEBS Letters;1993-06-01
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