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The Catalytic Role of the W573 in the Mobile Loop of Recombinant Acetohydroxyacid Synthase from Tobacco

Title
The Catalytic Role of the W573 in the Mobile Loop of Recombinant Acetohydroxyacid Synthase from Tobacco
Author
김정림
Keywords
Acetohydroxyacid synthase; Kinetics; Fluorescence; Site-directed mutagenesis
Issue Date
2006-04
Publisher
대한화학회
Citation
BULLETIN OF THE KOREAN CHEMICAL SOCIETY, v. 27, No. 4, Page. 549-555
Abstract
Acetohydroxyacid synthase (AHAS, EC 2.2.1.6 also referred to as acetolactate synthase) catalyzes the first common step in the metabolic pathway leading to biosythesis of the branched-chain amino acids in plants and microorganisms. Due to its presence in plants, AHAS is a target for the herbicides (sulfonylurea and imidazolinone), which act as potent inhibitors of the enzyme. Recently, we have shown [J. Kim, D. G. Baek, Y. T. Kim, J. D. Choi, M. Y. Yoon, Biochem. J. (2004) 384, 59-68] that the residues in the "mobile loop" 567-582 on the C-termini are involved in the binding/stabilization of the active dimer and ThDP (thiamin diphosphate) binding. In this study, we have demonstrared the role of the W573 in the mobile loop of the C-termini of tobacco AHAS. The substitution of this W573 residue caused significant perturbations in the active process and in the binding site of ThDP. Position W573 plays a structurally important role in the binding of FAD, maintaining the enzyne active aite in the required geometry for catalysis to occur. In here we propose that the tryptophan at position 573 is important for the catalytic process.
URI
http://www.koreascience.or.kr/article/JAKO200602727044015.pagehttp://repository.hanyang.ac.kr/handle/20.500.11754/107865
ISSN
0253-2964; 1229-5949
DOI
10.5012/bkcs.2006.27.4.549
Appears in Collections:
COLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY[E](과학기술융합대학) > CHEMICAL AND MOLECULAR ENGINEERING(화학분자공학과) > Articles
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