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dc.contributor.author김순길-
dc.date.accessioned2018-04-19T09:25:19Z-
dc.date.available2018-04-19T09:25:19Z-
dc.date.issued2013-01-
dc.identifier.citationEnzyme and Microbial Technology, 10 January 2013, 52(1), P.54-59en_US
dc.identifier.issn0141-0229-
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S0141022912001743-
dc.identifier.urihttps://repository.hanyang.ac.kr/handle/20.500.11754/69595-
dc.description.abstractThe catabolic acetolactate synthase (cALS) of Enterococcus faecalis V583 was cloned, expressed in Escherichia colt, and purified to homogeneity. The purified protein had a molecular weight of 60 kDa. The cALS of E. faecalis is highly homologous with other cALSs, while sharing low homology with its anabolic counterparts. The cALS of E. faecalis exhibits optimum activity at a temperature of 37 degrees C and pH 6.8. Based on the enzyme characterization, the apparent K-m for pyruvate was calculated to be 1.37 mM, while the K-c for thiamin diphosphate (ThDP) and Mg2+ were found to be 0.031 mu M and 1.27 mM, respectively. Negligible absorbance at 450 nm and lack of activity enhancement upon addition of flavin adenine dinucleotide (FAD) to the assay buffer suggest that the cALS of E. faecalis is not FAD-dependent. The enzyme showed extreme stability against the organic solvent dimethyl sulfoxide (DMSO), whereas the activity decreased to less than 50% in the presence of acetone and ethanol. (C) 2012 Elsevier Inc. All rights reserved.en_US
dc.description.sponsorshipThis research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (2012R1A1A2008516) and by the “Cooperative Research Program grants for Agriculture Science & Technology Development (Project No. PJ907052)” funded by the Rural Development Administration, Republic of Korea.en_US
dc.language.isoenen_US
dc.publisherElsevier Science B.V., Amsterdam.en_US
dc.subjectEnterococcus faecalisen_US
dc.subjectCatabolicen_US
dc.subjectAcetolactate synthaseen_US
dc.subjectThDPen_US
dc.subjectFlavin adenine dinucleotideen_US
dc.subjectACETOHYDROXYACID SYNTHASEen_US
dc.subjectESCHERICHIA-COLIen_US
dc.subjectKLEBSIELLA-PNEUMONIAEen_US
dc.subjectSERRATIA-MARCESCENSen_US
dc.subjectFORMING ENZYMEen_US
dc.subjectAEROBACTER AEROGENESen_US
dc.subjectPOTENT INHIBITORSen_US
dc.subjectBACILLUS-SUBTILISen_US
dc.subjectPURIFICATIONen_US
dc.subjectPHen_US
dc.titleCharacterization of recombinant FAD-independent catabolic acetolactate synthase from Enterococcus faecalis V583en_US
dc.typeArticleen_US
dc.relation.no1-
dc.relation.volume52-
dc.identifier.doi10.1016/j.enzmictec.2012.10.006-
dc.relation.page54-59-
dc.relation.journalENZYME AND MICROBIAL TECHNOLOGY-
dc.contributor.googleauthorLee, S. C.-
dc.contributor.googleauthorKim, J.-
dc.contributor.googleauthorLa, I. J.-
dc.contributor.googleauthorKim, S. K.-
dc.contributor.googleauthorYoon, M. Y.-
dc.relation.code2013009811-
dc.sector.campusS-
dc.sector.daehakCOLLEGE OF MEDICINE[S]-
dc.sector.departmentDEPARTMENT OF MEDICINE-
dc.identifier.pidkimsg-
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COLLEGE OF MEDICINE[S](의과대학) > MEDICINE(의학과) > Articles
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