Physical and kinetic properties of lysine-sensitive aspartate kinase purified from carrot cell suspension culture
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference35 articles.
1. The Threonine-Sensitive Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K 12. 4. Isolation, Molecular Weight, Amino Acid Analysis and Behaviour of the Sulfhydryl Groups of the Protein Catalyzing the Two Activities
2. The Methionine-Repressible Homoserine Dehydrogenase and Aspartokinase Activities of Escherichia coli K12. Preparation of the Homogeneous Protein Catalyzing the Two Activities. Molecular Weight of the Native Enzyme and of its Subunits
3. Regulation of the Lysine Biosynthetic Pathway of Escherichia coli K12. Isolation, Molecular Weight and Amino Acid Analysis of the Lysine Sensitive Aspartokinase
4. Use of monoclonal antibodies for the purification and characterization of the threonine-sensitive isozyme of maize homoserine dehydrogenase
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2. Lysine and threonine biosynthesis in sorghum seeds: characterisation of aspartate kinase and homoserine dehydrogenase isoenzymes;Annals of Applied Biology;2006-08
3. Isolation of enzymes involved in threonine biosynthesis from sorghum seeds;Brazilian Journal of Plant Physiology;2004-08
4. Analysis of the aspartic acid metabolic pathway using mutant genes;Amino Acids;2002-04
5. Overproduction, Purification, and Characterization of Recombinant Bifunctional Threonine-Sensitive Aspartate Kinase-Homoserine Dehydrogenase from Arabidopsis thaliana;Protein Expression and Purification;2002-02
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