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- Publisher
- Springer Journals
- Copyright
- Copyright © 2010 by Springer Science+Business Media B.V.
- Subject
- Physics; Biochemistry, general; Polymer Sciences ; Biophysics and Biological Physics
- ISSN
- 1874-2718
- eISSN
- 1874-270X
- DOI
- 10.1007/s12104-010-9225-x
- pmid
- 20383786
- Publisher site
- See Article on Publisher Site
Abstract
Acetohydroxyacid synthase (AHAS) is an enzyme involved in the biosynthesis of the branched chain amino acids viz, valine, leucine and isoleucine. The activity of this enzyme is regulated through feedback inhibition by the end products of the pathway. Here we report the backbone and side-chain assignments of ilvN, the 22 kDa dimeric regulatory subunit of E. coli AHAS isoenzyme I, in the valine bound form. Detailed analysis of the structure of ilvN and its interactions with the catalytic subunit of E. coli AHAS I will help in understanding the mechanism of activation and regulation of the branched chain amino acid biosynthesis.
Journal
Biomolecular NMR Assignments – Springer Journals
Published: Apr 11, 2010