Glyoxalase

From Proteopedia

Revision as of 08:55, 16 July 2019

spinqualitylabelsall models Human glyoxalase I dimer complex with glutathione derivative and Zn+2 ion (grey) 1qin Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Structural highlights 4 3D structures of glyoxalase Function Glyoxalase (GLO) is part of the glyoxalase system which detoxifies the highly toxic methylglyoxal and other aldehydes produced by metabolism[1]. GLO1 or lactoylglutathione lyase 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]. The GLO system is a focus of research on metabolic control and prevention of vascular complications in diabetes and obesity[3]. Structural highlights [4]. Water molecules are shown as red spheres. 3D structures of glyoxalase Glyoxalase 3D structures

3D structures of glyoxalase

Updated on 16-July-2019

References

1. ↑ 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
2. ↑ Thornalley PJ. The glyoxalase system in health and disease. Mol Aspects Med. 1993;14(4):287-371. PMID:8277832
3. ↑ 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
4. ↑ 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