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dc.contributor.authorSuttisansanee, Uthaiwan
dc.date.accessioned2011-05-19 18:58:43 (GMT)
dc.date.available2011-05-19 18:58:43 (GMT)
dc.date.issued2011-05-19T18:58:43Z
dc.date.submitted2011
dc.identifier.urihttp://hdl.handle.net/10012/5946
dc.description.abstractThe Glyoxalase system is composed of two metalloenzymes, Glyoxalase I and Glyoxalase II, that catalyze the conversion of toxic, metabolically produced alpha-ketoaldehydes, such as methyglyoxal, in the presence of a thiol cofactor, such as glutathione, into their corresponding nontoxic 2-hydroxycarboxylic acids, leading to detoxification of these cellular metabolites. Previous studies on the first enzyme in the Glyoxalase system, Glyoxalase I (GlxI), in yeast, protozoa, animals, human, plants and Gram-negative bacteria suggest two metal activation classes, zinc-activation or non-zinc-activation (but exhibiting selective nickel/cobalt-activation). This thesis provides the key discoveries of the Glyoxalase system from Gram-positive microorganisms using the major thiol cofactor/cosubstrate that produced within that particular organisms as well as the relatedness of the proteins in the same beta-alpha-beta-beta-beta protein superfamily.en
dc.language.isoenen
dc.publisherUniversity of Waterlooen
dc.subjectGlyoxalaseen
dc.subjectMetalloenzymeen
dc.subjectBacterial enzymeen
dc.subjectSuperfamilyen
dc.titleInvestigation of the Microbial Glyoxalase Systemen
dc.typeDoctoral Thesisen
dc.pendingfalseen
dc.subject.programChemistryen
uws-etd.degree.departmentChemistryen
uws-etd.degreeDoctor of Philosophyen
uws.typeOfResourceTexten
uws.peerReviewStatusUnrevieweden
uws.scholarLevelGraduateen


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