Glyoxalase

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== Relevance ==
== Relevance ==
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GLO1 is a target for drugs against bacteria, protozoans and cancer<ref>PMID:8277832</ref>.
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GLO1 is a target for drugs against bacteria, protozoans and cancer<ref>PMID:8277832</ref>. The GLO system is a focus of research on metabolic control and prevention of vascular complications in diabetes and obesity<ref>PMID:21335095</ref>.
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== Structural highlights ==
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Human GLO1 active site contains Zn+2 atom<ref>PMID:10521255</ref>.
==3D structures of glyoxalase==
==3D structures of glyoxalase==

Revision as of 11:12, 15 March 2016

Template:STRUCTURE 1qin

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]. The GLO system is a focus of research on metabolic control and prevention of vascular complications in diabetes and obesity[3].

Structural highlights

Human GLO1 active site contains Zn+2 atom[4].

3D structures of glyoxalase

Updated on 15-March-2016

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

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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