5ny5: Difference between revisions
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The | ==The apo structure of 3,4-dihydroxybenzoic acid decarboxylases from Enterobacter cloacae== | ||
<StructureSection load='5ny5' size='340' side='right' caption='[[5ny5]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ny5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NY5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NY5 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5ny5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ny5 OCA], [http://pdbe.org/5ny5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ny5 RCSB], [http://www.ebi.ac.uk/pdbsum/5ny5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ny5 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The utilization of CO2 as carbon source for organic syntheses meets the urgent demand of more sustainability in chemical production. Here we report on the enzyme-catalyzed para-carboxylation of catechols, employing 3,4-dihydroxybenzoic acid decarboxylases (AroY) that belong to the UbiD enzyme family. Crystal structures and accompanying solution data confirm that AroY utilizes the recently discovered prenylated FMN (prFMN) cofactor, and requires oxidative maturation to form the catalytically competent prFMNiminium species. This study reports on the in vitro reconstitution and activation of a prFMN-dependent enzyme that is capable of directly carboxylating aromatic catechol substrates under ambient conditions. A reaction mechanism for the reversible decarboxylation involving a monocovalent quinoid-cofactor intermediate is proposed, which is distinct from the prFMN associated 1,3 dipolar cycloaddition mechanism in related enzymes. | |||
Regioselective para-Carboxylation of Catechols by a Prenylated Flavin Dependent Decarboxylase.,Payer S, Marshall SA, Barland N, Sheng X, Reiter T, Dordic A, Steinkellner G, Wuensch C, Kaltwasser S, Fisher K, Rigby SEJ, Macheroux P, Vonck J, Gruber K, Faber K, Himo F, Leys D, Pavkov-Keller T, Glueck SM Angew Chem Int Ed Engl. 2017 Aug 30. doi: 10.1002/anie.201708091. PMID:28857436<ref>PMID:28857436</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5ny5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Dordic, A]] | |||
[[Category: Glueck, S]] | |||
[[Category: Gruber, K]] | |||
[[Category: Leys, D]] | |||
[[Category: Marshall, S]] | |||
[[Category: Pavkov-Keller, T]] | |||
[[Category: Payer, S]] | |||
[[Category: Carboxylation]] | |||
[[Category: Catechol]] | |||
[[Category: Hydrolase]] | |||
[[Category: Prenylated fmn]] | |||
[[Category: Ubid-family]] | |||
Revision as of 13:40, 13 September 2017
The apo structure of 3,4-dihydroxybenzoic acid decarboxylases from Enterobacter cloacaeThe apo structure of 3,4-dihydroxybenzoic acid decarboxylases from Enterobacter cloacae
Structural highlights
Publication Abstract from PubMedThe utilization of CO2 as carbon source for organic syntheses meets the urgent demand of more sustainability in chemical production. Here we report on the enzyme-catalyzed para-carboxylation of catechols, employing 3,4-dihydroxybenzoic acid decarboxylases (AroY) that belong to the UbiD enzyme family. Crystal structures and accompanying solution data confirm that AroY utilizes the recently discovered prenylated FMN (prFMN) cofactor, and requires oxidative maturation to form the catalytically competent prFMNiminium species. This study reports on the in vitro reconstitution and activation of a prFMN-dependent enzyme that is capable of directly carboxylating aromatic catechol substrates under ambient conditions. A reaction mechanism for the reversible decarboxylation involving a monocovalent quinoid-cofactor intermediate is proposed, which is distinct from the prFMN associated 1,3 dipolar cycloaddition mechanism in related enzymes. Regioselective para-Carboxylation of Catechols by a Prenylated Flavin Dependent Decarboxylase.,Payer S, Marshall SA, Barland N, Sheng X, Reiter T, Dordic A, Steinkellner G, Wuensch C, Kaltwasser S, Fisher K, Rigby SEJ, Macheroux P, Vonck J, Gruber K, Faber K, Himo F, Leys D, Pavkov-Keller T, Glueck SM Angew Chem Int Ed Engl. 2017 Aug 30. doi: 10.1002/anie.201708091. PMID:28857436[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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