Glyoxalase: Difference between revisions

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{{STRUCTURE_1qin|  PDB=1qin  | SIZE=400| SCENE= |right|CAPTION=Human glyoxalase I complex with glutathione derivative, [[1qin]] }}
<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]]'>
'''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]].


===Glyoxalase 1===
== Function ==
'''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''' 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]].


[[1bh5]] – hGLO (mutant) – human<br />
== Relevance ==
[[1fa8]] – EcGLO – ''Escherichia coli''<br />
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>.
[[2c21]] – GLO – ''Leishmania major''<br />
[[1fro]] – hGLO + benzyl glutathione<br />
[[1qin]], [[1qip]] - hGLO + glutathione derivative<br />
[[1f9z]], [[1fa5]], [[1fa6]], [[1fa7]] – EcGLO + metal <br />
[[2za0]] – GLO + methyl gerfelin – mouse<br />
[[3hdp]] – GLO + Ni – ''Clostridium acetobutylicum''


===Glyoxalase 2===
== Structural highlights ==


[[1xm8]] – GLO – ''Arabidopsis thaliana''<br />
<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.
[[2p18]] - LiGLO – ''Leishmania infantum''<br />
[[1qh3]] – hGLO + actate + cacodylate<br />
[[1qh5]] – hGLO + glutathione derivative<br />
[[2p1e]] – LiGLO + lactate


==3D structures of glyoxalase==
[[Glyoxalase 3D structures]]
</StructureSection>
== References ==
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 11:56, 16 July 2019


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


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

Drag the structure with the mouse to rotate

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

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Michal Harel, Alexander Berchansky, Joel L. Sussman
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