4e13: Difference between revisions
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==Substrate-directed dual catalysis of dicarbonyl compounds by diketoreductase== | |||
<StructureSection load='4e13' size='340' side='right'caption='[[4e13]], [[Resolution|resolution]] 2.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4e13]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baylyi Acinetobacter baylyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E13 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E13 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.08Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4e13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e13 OCA], [https://pdbe.org/4e13 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e13 RCSB], [https://www.ebi.ac.uk/pdbsum/4e13 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e13 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B1P3E1_ACIBI B1P3E1_ACIBI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Diketoreductase catalyzes a two-step bioreduction on a dicarbonyl substrate through a novel dual catalysis mode, in which random hydride attack simultaneously forms two mono-carbonyl intermediates, and subsequently distinct catalytic sites are responsible for the reductions of respective carbonyl group of the intermediates to yield the final dihydroxy product. | |||
Dual catalysis mode for the dicarbonyl reduction catalyzed by diketoreductase.,Lu M, Huang Y, White MA, Wu X, Liu N, Cheng X, Chen Y Chem Commun (Camb). 2012 Oct 24;48(92):11352-4. doi: 10.1039/c2cc36334h. PMID:23073461<ref>PMID:23073461</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
== | </div> | ||
<div class="pdbe-citations 4e13" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acinetobacter baylyi]] | [[Category: Acinetobacter baylyi]] | ||
[[Category: Chen | [[Category: Large Structures]] | ||
[[Category: Cheng | [[Category: Chen Y]] | ||
[[Category: Huang | [[Category: Cheng X]] | ||
[[Category: Liu | [[Category: Huang Y]] | ||
[[Category: Lu | [[Category: Liu N]] | ||
[[Category: White | [[Category: Lu M]] | ||
[[Category: Wu | [[Category: White MA]] | ||
[[Category: Wu X]] | |||
Latest revision as of 16:45, 8 November 2023
Substrate-directed dual catalysis of dicarbonyl compounds by diketoreductaseSubstrate-directed dual catalysis of dicarbonyl compounds by diketoreductase
Structural highlights
FunctionPublication Abstract from PubMedDiketoreductase catalyzes a two-step bioreduction on a dicarbonyl substrate through a novel dual catalysis mode, in which random hydride attack simultaneously forms two mono-carbonyl intermediates, and subsequently distinct catalytic sites are responsible for the reductions of respective carbonyl group of the intermediates to yield the final dihydroxy product. Dual catalysis mode for the dicarbonyl reduction catalyzed by diketoreductase.,Lu M, Huang Y, White MA, Wu X, Liu N, Cheng X, Chen Y Chem Commun (Camb). 2012 Oct 24;48(92):11352-4. doi: 10.1039/c2cc36334h. PMID:23073461[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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