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.
| Identifer | oai:union.ndltd.org:WATERLOO/oai:uwspace.uwaterloo.ca:10012/5946 |
| Date | January 2011 |
| Creators | Suttisansanee, Uthaiwan |
| Source Sets | University of Waterloo Electronic Theses Repository |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
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