Proteolysis of the bifunctional methionine-repressible aspartokinase II-homoserine dehydrogenase II of Escherichia coli K12. Production of an active homoserine dehydrogenase fragment.-Reference-Cited by-同舟云学术

Proteolysis of the bifunctional methionine-repressible aspartokinase II-homoserine dehydrogenase II of Escherichia coli K12. Production of an active homoserine dehydrogenase fragment.

Published:1977-11 Issue:21 Volume:252 Page:7685-7689
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Dautry-Varsat A.,Cohen G.N.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference20 articles.

1. The hydrolysis of rabbit γ-globulin and antibodies with crystalline papain

2. Proteolytic Cleavage of Native DNA Polymerase into Two Different Catalytic Fragments. Influence of Assay Conditions on the Change of Exonuclease Activity and Polymerase Activity Accompanying Cleavage

3. Deoxyribonucleic Acid Polymerase: Two Distinct Enzymes in One Polypeptide

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. Lac Repressor

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1. Gene fusions and gene duplications: relevance to genomic annotation and functional analysis;BMC Genomics;2005-03-09

2. Production and Characterization of Bifunctional Enzymes. Domain Swapping To Produce New Bifunctional Enzymes in the Aspartate Pathway;Biochemistry;2002-02-16

3. Overproduction, Purification, and Characterization of Recombinant Bifunctional Threonine-Sensitive Aspartate Kinase-Homoserine Dehydrogenase from Arabidopsis thaliana;Protein Expression and Purification;2002-02

4. Specific proteolysis of native alanine racemases from Salmonella typhimurium: identification of the cleavage site and characterization of the clipped two-domain proteins;Biochemistry;1987-12

5. E.coli aspartokinase II-homoserine dehydrogenase II polypeptide chain has a triglobular structure;Biochemical and Biophysical Research Communications;1984-08