Modifying the determinants of α-ketoacid substrate selectivity inmycobacterium tuberculosisα-isopropylmalate synthase
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2014.02.053/fullpdf
Reference23 articles.
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2. Kinetic and chemical mechanisms of homocitrate synthase from Thermus thermophilus;Kumar;J. Biol. Chem.,2011
3. Evidence for a catalytic dyad in the active site of homocitrate synthase from Saccharomyces cerevisiae;Qian;Biochemistry,2008
4. A synthetic iterative pathway for ketoacid elongation;Shen;Methods Enzymol.,2011
5. Kinetic evidence for inter-domain communication in the allosteric regulation of α-isopropylmalate synthase from Mycobacterium tuberculosis;de Carvalho;Biochemistry,2009
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