4uu3: Difference between revisions
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==Ferulic acid decarboxylase from Enterobacter sp.== | |||
<StructureSection load='4uu3' size='340' side='right'caption='[[4uu3]], [[Resolution|resolution]] 1.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4uu3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_sp. Enterobacter sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UU3 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]] 1.15Å</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=4uu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uu3 OCA], [https://pdbe.org/4uu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uu3 RCSB], [https://www.ebi.ac.uk/pdbsum/4uu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uu3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/C6F3U5_9ENTR C6F3U5_9ENTR] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We report on a 'green' method for the utilization of carbon dioxide as C1 unit for the regioselective synthesis of (E)-cinnamic acids via regioselective enzymatic carboxylation of para-hydroxystyrenes. Phenolic acid decarboxylases from bacterial sources catalyzed the beta-carboxylation of para-hydroxystyrene derivatives with excellent regio- and (E/Z)-stereoselectivity by exclusively acting at the beta-carbon atom of the C=C side chain to furnish the corresponding (E)-cinnamic acid derivatives in up to 40% conversion at the expense of bicarbonate as carbon dioxide source. Studies on the substrate scope of this strategy are presented and a catalytic mechanism is proposed based on molecular modelling studies supported by mutagenesis of amino acid residues in the active site. | |||
Regioselective Enzymatic beta-Carboxylation of -Hydroxy- styrene Derivatives Catalyzed by Phenolic Acid Decarboxylases.,Wuensch C, Pavkov-Keller T, Steinkellner G, Gross J, Fuchs M, Hromic A, Lyskowski A, Fauland K, Gruber K, Glueck SM, Faber K Adv Synth Catal. 2015 May 26;357(8):1909-1918. Epub 2015 Apr 2. PMID:26190963<ref>PMID:26190963</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4uu3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Enterobacter sp]] | |||
[[Category: Large Structures]] | |||
[[Category: Faber K]] | |||
[[Category: Fauland K]] | |||
[[Category: Fuchs M]] | |||
[[Category: Glueck SM]] | |||
[[Category: Gross J]] | |||
[[Category: Gruber K]] | |||
[[Category: Hromic A]] | |||
[[Category: Lyskowski A]] | |||
[[Category: Pavkov-Keller T]] | |||
[[Category: Steinkellner G]] | |||
[[Category: Wuensch C]] | |||
Latest revision as of 13:36, 10 January 2024
Ferulic acid decarboxylase from Enterobacter sp.Ferulic acid decarboxylase from Enterobacter sp.
Structural highlights
FunctionPublication Abstract from PubMedWe report on a 'green' method for the utilization of carbon dioxide as C1 unit for the regioselective synthesis of (E)-cinnamic acids via regioselective enzymatic carboxylation of para-hydroxystyrenes. Phenolic acid decarboxylases from bacterial sources catalyzed the beta-carboxylation of para-hydroxystyrene derivatives with excellent regio- and (E/Z)-stereoselectivity by exclusively acting at the beta-carbon atom of the C=C side chain to furnish the corresponding (E)-cinnamic acid derivatives in up to 40% conversion at the expense of bicarbonate as carbon dioxide source. Studies on the substrate scope of this strategy are presented and a catalytic mechanism is proposed based on molecular modelling studies supported by mutagenesis of amino acid residues in the active site. Regioselective Enzymatic beta-Carboxylation of -Hydroxy- styrene Derivatives Catalyzed by Phenolic Acid Decarboxylases.,Wuensch C, Pavkov-Keller T, Steinkellner G, Gross J, Fuchs M, Hromic A, Lyskowski A, Fauland K, Gruber K, Glueck SM, Faber K Adv Synth Catal. 2015 May 26;357(8):1909-1918. Epub 2015 Apr 2. PMID:26190963[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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