Many of the functional differences between acetohydroxyacid synthase (AHAS) isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-thiamin diphosphate adduct in AHAS I-Reference-Cited by-同舟云学术

Many of the functional differences between acetohydroxyacid synthase (AHAS) isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-thiamin diphosphate adduct in AHAS I

Published:2012-04-20 Issue:11 Volume:279 Page:1967-1979
ISSN:1742-464X
Container-title:FEBS Journal
language:en
Short-container-title:

Author:

Belenky Inna,Steinmetz Andrea,Vyazmensky Maria,Barak Ze’ev,Tittmann Kai,Chipman David M.

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2012.08577.x/fullpdf

Reference40 articles.

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2. Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria;Barak;J Bacteriol,1987

3. Branched-chain amino acid biosynthesis in Salmonella typhimurium: a quantitative analysis;Epelbaum;J Bacteriol,1998

4. Acetohydroxy acid synthase I is required for isoleucine and valine biosynthesis by Salmonella typhimurium LT2 during growth on acetate or long-chain fatty acids;Dailey;J Bacteriol,1987

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