Two regions of the bifunctional protein aspartokinase I- homoserine dehydrogenase I are connected by a short hinge.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference13 articles.
1. Multifunctional Proteins;Cohen,1980
2. Nucleotide sequence of the thrA gene of Escherichia coli.
3. Revised Structure of Aspartokinase I-Homoserine Dehydrogenase I of Escherichia coli K12. Evidence for Four Identical Subunits
4. 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
5. The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Site of limited proteolytic cleavage by subtilisin.
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1. A novel bifunctional aspartate kinase-homoserine dehydrogenase from the hyperthermophilic bacterium, Thermotoga maritima;Bioscience, Biotechnology, and Biochemistry;2018-12-02
2. Threonine-insensitive Homoserine Dehydrogenase from Soybean;Journal of Biological Chemistry;2010-01
3. Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase;Journal of Biological Chemistry;1993-05
4. Cloning and nucleotide sequence of the gene coding for aspartokinase II from a thermophilic methylotrophic Bacillus sp;Applied and Environmental Microbiology;1992-09
5. Nucleotide sequence and fine structural analysis of theCorynebacterium glutamicum hom-thrBoperon;Molecular Microbiology;1988-01
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