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마수드카림,심미영,김정목,최경재,김정림,최정도,윤문영 대한화학회 2006 Bulletin of the Korean Chemical Society Vol.27 No.4
Acetohydroxyacid synthase (AHAS, EC 2.2.1.6 also referred to as acetolactate synthase) catalyzes the firstcommon step in the metabolic pathway leading to biosynthesis of the branched-chain amino acids in plantsand microorganisms. Due to its presence in plants, AHAS is a target for the herbicides (sulfonylurea andimidazolinone), 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 (thiamindiphosphate) binding. In this study, we have demonstrated the role of the W573 in the mobile loop of theC-termini of tobacco AHAS. The substitution of this W573 residue caused significant perturbations in theactivation process and in the binding site of ThDP. Position W573 plays a structurally important role in thebinding of FAD, maintaining the enzyme active site in the required geometry for catalysis to occur. In herewe propose that the tryptophan at position 573 is important for the catalytic process.