Article
Structural and functional evaluation of three well-conserved serine residues in tobacco acetohydroxyacid synthase.
Biochimie - 1 Jan 2010
Yoon Moon-Young, Gedi Vinayakumar, Kim Joungmok, Park Yoonkyung, Kim Dong-Eun, Park Eun-Hye, Choi Jung-Do
Abstract excerpt
The first step in the common pathway for the biosynthesis of branched-chain amino acids (BCAAs) is catalyzed by acetohydroxyacid synthase (AHAS). The roles of three well-conserved serine residues (S167, S506, and S539) in tobacco AHAS were determined using site-directed mutagenesis. The mutations S167F and S506F were found to be inactive and abolished the binding affinity for cofactor FAD. The Far-UV CD spectrum...
Topics
- Acetolactate Synthase
- Amino Acid Sequence
- Biocatalysis
- Coenzymes
- Conserved Sequence
- Crystallography, X-Ray
- Enzyme Activation
- Herbicides
- Kinetics
- Models, Molecular
- Molecular Sequence Data