Investigation of the Microbial Glyoxalase System
dc.contributor.author | Suttisansanee, Uthaiwan | |
dc.date.accessioned | 2011-05-19T18:58:43Z | |
dc.date.available | 2011-05-19T18:58:43Z | |
dc.date.issued | 2011-05-19T18:58:43Z | |
dc.date.submitted | 2011 | |
dc.description.abstract | The 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.identifier.uri | http://hdl.handle.net/10012/5946 | |
dc.language.iso | en | en |
dc.pending | false | en |
dc.publisher | University of Waterloo | en |
dc.subject | Glyoxalase | en |
dc.subject | Metalloenzyme | en |
dc.subject | Bacterial enzyme | en |
dc.subject | Superfamily | en |
dc.subject.program | Chemistry | en |
dc.title | Investigation of the Microbial Glyoxalase System | en |
dc.type | Doctoral Thesis | en |
uws-etd.degree | Doctor of Philosophy | en |
uws-etd.degree.department | Chemistry | en |
uws.peerReviewStatus | Unreviewed | en |
uws.scholarLevel | Graduate | en |
uws.typeOfResource | Text | en |