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Molecular enzymology of the glyoxalase system.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Biochemistry and Organic Chemistry. (Biokemi I)
2008 (English)In: Drug metabolism and drug interactions, ISSN 0792-5077, Vol. 23, no 1-2, 13-27 p.Article in journal (Refereed) Published
Abstract [en]

The glyoxalase system catalyzes the conversion of 2-oxoaldehydes into the corresponding 2-hydroxyacids. This biotransformation involves two separate enzymes, glyoxalase I and glyoxalase II, which bring about two consecutive reactions involving the thiol-containing tripeptide glutathione as a cofactor. The physiologically most important substrate methylglyoxal is converted by glyoxalase I into S-D-lactoyl-glutathione in the first reaction. Subsequently, glyoxalase II catalyzes the hydrolysis of this thiolester into D-lactic acid and free glutathione. The structures of both enzymes have been obtained via molecular cloning, heterologous expression, and X-ray diffraction analysis. Glyoxalase I and glyoxalase II are metalloenzymes and zinc plays an essential role in their diverse catalytic mechanisms. Both enzymes appear linked to a variety of pathological conditions, but further investigations are required to clarify the different physiological aspects of the glyoxalase system.

Place, publisher, year, edition, pages
2008. Vol. 23, no 1-2, 13-27 p.
Identifiers
URN: urn:nbn:se:uu:diva-105757PubMedID: 18533362OAI: oai:DiVA.org:uu-105757DiVA: diva2:223290
Available from: 2009-06-11 Created: 2009-06-08 Last updated: 2009-07-06Bibliographically approved

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