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Glyoxalase

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{{STRUCTURE_1qin| PDB=1qin | SIZE=400| SCENE= |right|CAPTION=Human glyoxalase I dimer complex with glutathione derivative, [[1qin]] }}
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<StructureSection load='' size='350' side='right' scene='50/508460/Cv/1' caption='Human glyoxalase I dimer complex with glutathione derivative and Zn+2 ion (grey) [[1qin]]'>
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'''Glyoxalase''' (GLO) is part of glyoxalase system which detoxify the highly toxic methylglyoxal and other aldehydes produced by metabolism. 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]].
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==3D structures of glyoxalase==
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== Function ==
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'''Glyoxalase''' (GLO) is part of the glyoxalase system which detoxifies the highly toxic methylglyoxal and other aldehydes produced by metabolism<ref>PMID:10066594</ref>. <br />
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* '''GLO1''' or '''lactoylglutathione lyase''' catalyzes the conversion of glutathione and methylglyoxal to lactoylglutathione.<br />
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* '''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]].
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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== Relevance ==
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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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===Glyoxalase 1===
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== Structural highlights ==
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[[1bh5]] – hGLO (mutant) – human<br />
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<scene name='50/508460/Cv/5'>Human GLO1 active site contains Zn+2 atom</scene><ref>PMID:10521255</ref>. Water molecules are shown as red spheres.
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[[1fa8]] – EcGLO – ''Escherichia coli''<br />
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[[2c21]] – GLO – ''Leishmania major''<br />
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[[1fro]] – hGLO + benzyl glutathione<br />
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[[1qin]], [[1qip]] - hGLO + glutathione derivative<br />
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[[1f9z]], [[1fa5]], [[1fa6]], [[1fa7]] – EcGLO + metal <br />
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[[2za0]] – GLO + methyl gerfelin – mouse<br />
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[[3hdp]] – GLO + Ni – ''Clostridium acetobutylicum''
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===Glyoxalase 2===
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==3D structures of glyoxalase==
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[[Glyoxalase 3D structures]]
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[[1xm8]] – GLO – ''Arabidopsis thaliana''<br />
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[[2p18]] - LiGLO – ''Leishmania infantum''<br />
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[[1qh3]] – hGLO + actate + cacodylate<br />
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[[1qh5]] – hGLO + glutathione derivative<br />
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[[2p1e]] – LiGLO + lactate
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===Glyoxalase 3===
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[[4lru]] – GLO – ''Candida albicans''<br />
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</StructureSection>
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human glyoxalase I dimer complex with glutathione derivative and Zn+2 ion (grey) 1qin

Drag the structure with the mouse to rotate

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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