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Two regions of the bifunctional protein aspartokinase I- homoserine dehydrogenase I are connected by a short hinge.

Authors
  • Sibilli, L
  • Le Bras, G
  • Le Bras, G
  • Cohen, G N
Type
Published Article
Journal
Journal of Biological Chemistry
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Publication Date
Oct 25, 1981
Volume
256
Issue
20
Pages
10228–10230
Identifiers
PMID: 7026556
Source
Medline
License
Unknown

Abstract

Four proteases differing in their specificity, i.e. subtilisin, trypsin, alpha-chymotrypsin and V8 staphylococcal protease, cleave the bifunctional protein Escherichia coli aspartokinase I-homoserine dehydrogenase I (composed of 820 residues) producing an active homoserine dehydrogenase fragment. This cleavage occurs within a short segment of the polypeptide chain extending from residue 293 to residue 300.

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