33 0

Full metadata record

DC FieldValueLanguage
dc.contributor.author김정림-
dc.date.accessioned2019-07-25T05:37:28Z-
dc.date.available2019-07-25T05:37:28Z-
dc.date.issued2006-04-
dc.identifier.citationBULLETIN OF THE KOREAN CHEMICAL SOCIETY, v. 27, No. 4, Page. 549-555en_US
dc.identifier.issn0253-2964-
dc.identifier.issn1229-5949-
dc.identifier.urihttp://www.koreascience.or.kr/article/JAKO200602727044015.page-
dc.identifier.urihttp://repository.hanyang.ac.kr/handle/20.500.11754/107865-
dc.description.abstractAcetohydroxyacid 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.en_US
dc.language.isoen_USen_US
dc.publisher대한화학회en_US
dc.subjectAcetohydroxyacid synthaseen_US
dc.subjectKineticsen_US
dc.subjectFluorescenceen_US
dc.subjectSite-directed mutagenesisen_US
dc.titleThe Catalytic Role of the W573 in the Mobile Loop of Recombinant Acetohydroxyacid Synthase from Tobaccoen_US
dc.typeArticleen_US
dc.identifier.doi10.5012/bkcs.2006.27.4.549-
dc.relation.journalBULLETIN OF THE KOREAN CHEMICAL SOCIETY-
dc.contributor.googleauthorKarim, M-
dc.contributor.googleauthorShim, MY-
dc.contributor.googleauthorKim, J-
dc.contributor.googleauthorChoi, KJ-
dc.contributor.googleauthorKim, JR-
dc.contributor.googleauthorChoi, JD-
dc.contributor.googleauthorYoon, MY-
dc.relation.code2009214307-
dc.sector.campusE-
dc.sector.daehakCOLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY[E]-
dc.sector.departmentDEPARTMENT OF CHEMICAL AND MOLECULAR ENGINEERING-
dc.identifier.pidjrkim-


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE