Glyoxalase
From Proteopedia
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| - | {{STRUCTURE_1qin| PDB=1qin | SIZE=400| SCENE= |right|CAPTION=Human glyoxalase I dimer complex with glutathione derivative and Zn+2 ion | + | {{STRUCTURE_1qin| PDB=1qin | SIZE=400| SCENE= |right|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 /> | ||
Revision as of 09:47, 15 March 2016
Contents |
Function
Glyoxalase (GLO) is part of glyoxalase system which detoxify the highly toxic methylglyoxal and other aldehydes produced by metabolism[1].
- GLO1 catalyzes the conversion of glutathione and methylglyoxal to lactoylglutathione.
- GLO2 is a metalloenzyme which catalyzes the hydrolysis of lactoylglutathione to glutathione and lactate. GLO2 exists as cytosolic and mitochondrial forms. For details on GLO2 see Leishmania infantum Glyoxalase II.
Relevance
GLO1 is a target for drugs against bacteria, protozoans and cancer[2].
3D structures of glyoxalase
Updated on 15-March-2016
References
- ↑ 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
