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| | <StructureSection load='4ofw' size='340' side='right'caption='[[4ofw]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='4ofw' size='340' side='right'caption='[[4ofw]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ofw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OFW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OFW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ofw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OFW FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ogf|4ogf]], [[4ogg|4ogg]]</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ofw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ofw OCA], [https://pdbe.org/4ofw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ofw RCSB], [https://www.ebi.ac.uk/pdbsum/4ofw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ofw ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DJ1D, At3g02720, F13E7.34 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-lactate_dehydratase D-lactate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.130 4.2.1.130] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ofw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ofw OCA], [http://pdbe.org/4ofw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ofw RCSB], [http://www.ebi.ac.uk/pdbsum/4ofw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ofw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DJ1D_ARATH DJ1D_ARATH]] Possesses glyoxalase I activity. Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. May be involved in oxidative stress response.<ref>PMID:23651081</ref> | + | [https://www.uniprot.org/uniprot/DJ1D_ARATH DJ1D_ARATH] Possesses glyoxalase I activity. Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. May be involved in oxidative stress response.<ref>PMID:23651081</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4ofw" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4ofw" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Protein DJ-1|Protein DJ-1]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: D-lactate dehydratase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Choi, D]] | + | [[Category: Choi D]] |
| - | [[Category: Kim, J]] | + | [[Category: Kim J]] |
| - | [[Category: Park, C]] | + | [[Category: Park C]] |
| - | [[Category: Ryu, K S]] | + | [[Category: Ryu K-S]] |
| - | [[Category: Glyoxalase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
DJ1D_ARATH Possesses glyoxalase I activity. Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. May be involved in oxidative stress response.[1]
Publication Abstract from PubMed
DJ-1 family proteins have recently been characterized as novel glyoxalases, although their cofactor-free catalytic mechanisms are not fully understood. In this work, we obtained crystals of Arabidopsis thaliana DJ-1d (atDJ-1d) and Homo sapiens DJ-1 (hDJ-1) covalently bound to glyoxylate, an analog of methylglyoxal, forming a hemithioacetal that presumably mimics an intermediate structure in the catalysis from methylglyoxal to lactate. The level of deuteration in lactate formation supported the proton transfer mechanism in the enzyme reaction. Differences in the enantiomeric specificity of D/L-lactacte formation observed in the DJ-1 superfamily proteins were explained by the presence of a His residue in the active site with essential Cys and Glu residues. The model for the stereospecificity was further evaluated by a molecular modeling simulation with methylglyoxal hemithioacetal superimposed on the glyoxylate hemithioacetal. The DJ-1 glyoxalase provides a unique mechanism in understanding the His residue-involved stereospecificity. This article is protected by copyright. All rights reserved.
Stereospecific mechanism of DJ-1 glyoxalases inferred from their hemithioacetal-containing crystal structures.,Choi D, Kim J, Ha S, Kwon K, Kim EH, Lee HY, Ryu KS, Park C FEBS J. 2014 Oct 4. doi: 10.1111/febs.13085. PMID:25283443[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kwon K, Choi D, Hyun JK, Jung HS, Baek K, Park C. Novel glyoxalases from Arabidopsis thaliana. FEBS J. 2013 Jul;280(14):3328-39. doi: 10.1111/febs.12321. Epub 2013 Jun 5. PMID:23651081 doi:http://dx.doi.org/10.1111/febs.12321
- ↑ Choi D, Kim J, Ha S, Kwon K, Kim EH, Lee HY, Ryu KS, Park C. Stereospecific mechanism of DJ-1 glyoxalases inferred from their hemithioacetal-containing crystal structures. FEBS J. 2014 Oct 4. doi: 10.1111/febs.13085. PMID:25283443 doi:http://dx.doi.org/10.1111/febs.13085
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