Glyoxalase: Difference between revisions

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== 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 the glyoxalase system which detoxifies the highly toxic methylglyoxal and other aldehydes produced by metabolism<ref>PMID:10066594</ref>. <br />
* '''GLO1''' catalyzes the conversion of glutathione and methylglyoxal to lactoylglutathione.<br />
* '''GLO1''' or '''lactoylglutathione lyase''' catalyzes the conversion of glutathione and methylglyoxal to lactoylglutathione.<br />
* '''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]].
* '''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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{{#tree:id=OrganizedByTopic|openlevels=0|
{{#tree:id=OrganizedByTopic|openlevels=0|


*Glyoxalase 1
*Glyoxalase 1 or lactoylglutathione lyase


**[[1bh5]] – hGLO (mutant) – human<br />
**[[1bh5]] – hGLO (mutant) – human<br />
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**[[1fro]] – hGLO + benzyl glutathione<br />  
**[[1fro]] – hGLO + benzyl glutathione<br />  
**[[1qin]], [[1qip]] - hGLO + glutathione derivative<br />
**[[1qin]], [[1qip]] - hGLO + glutathione derivative<br />
**[[3w0u]], [[3w0t]], [[3vw9]] – hGLO + inhibitor<br />
**[[1f9z]], [[1fa5]], [[1fa6]], [[1fa7]] – EcGLO + metal <br />
**[[1f9z]], [[1fa5]], [[1fa6]], [[1fa7]] – EcGLO + metal <br />
**[[2za0]] – GLO + methyl gerfelin – mouse<br />
**[[2za0]] – mGLO + methyl gerfelin – mouse<br />
**[[3hdp]] – GLO + Ni – ''Clostridium acetobutylicum''
**[[4x2a]] – mGLO + baicalein<br />
**[[4pv5]] – mGLO + glycyrrhetinic acid<br />
**[[4opn]] – mGLO + MAH<br />
**[[4kyk]], [[4kyh]] – mGLO + drug<br />
**[[3hdp]] – GLO + Ni – ''Clostridium acetobutylicum''<br />
**[[5d7z]] – GLO – maize<br />


*Glyoxalase 2
*Glyoxalase 2

Revision as of 09:33, 5 June 2018


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 shown as red spheres.

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

Drag the structure with the mouse to rotate

3D structures of glyoxalase3D structures of glyoxalase

Updated on 05-June-2018

ReferencesReferences

  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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman