Glyoxalase: Difference between revisions
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<StructureSection load='1qin' size='350' side='right' scene='' caption='Human glyoxalase I dimer complex with glutathione derivative and Zn+2 ion (grey) [[1qin]]'> | |||
== Function == | == Function == | ||
'''Glyoxalase''' (GLO) is part of glyoxalase system which detoxify the highly toxic methylglyoxal and other aldehydes produced by metabolism<ref>PMID:10066594</ref>. <br /> | '''Glyoxalase''' (GLO) is part of glyoxalase system which detoxify the highly toxic methylglyoxal and other aldehydes produced by metabolism<ref>PMID:10066594</ref>. <br /> | ||
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Human GLO1 active site contains Zn+2 atom<ref>PMID:10521255</ref>. | Human GLO1 active site contains Zn+2 atom<ref>PMID:10521255</ref>. | ||
</StructureSection> | |||
==3D structures of glyoxalase== | ==3D structures of glyoxalase== | ||
Revision as of 16:45, 16 March 2016
FunctionGlyoxalase (GLO) is part of glyoxalase system which detoxify the highly toxic methylglyoxal and other aldehydes produced by metabolism[1].
RelevanceGLO1 is a target for drugs against bacteria, protozoans and cancer[2]. The GLO system is a focus of research on metabolic control and prevention of vascular complications in diabetes and obesity[3]. Structural highlightsHuman GLO1 active site contains Zn+2 atom[4]. |
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3D structures of glyoxalase3D structures of glyoxalase
Updated on 16-March-2016
ReferencesReferences
- ↑ Dixon DP, Cummins L, Cole DJ, Edwards R. Glutathione-mediated detoxification systems in plants. Curr Opin Plant Biol. 1998 Jun;1(3):258-66. PMID:10066594
- ↑ Thornalley PJ. The glyoxalase system in health and disease. Mol Aspects Med. 1993;14(4):287-371. PMID:8277832
- ↑ Rabbani N, Thornalley PJ. Glyoxalase in diabetes, obesity and related disorders. Semin Cell Dev Biol. 2011 May;22(3):309-17. doi: 10.1016/j.semcdb.2011.02.015., Epub 2011 Feb 16. PMID:21335095 doi:http://dx.doi.org/10.1016/j.semcdb.2011.02.015
- ↑ Cameron AD, Ridderstrom M, Olin B, Kavarana MJ, Creighton DJ, Mannervik B. Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue. Biochemistry. 1999 Oct 12;38(41):13480-90. PMID:10521255