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.pagehttps://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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