6rx8: Difference between revisions

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'''Unreleased structure'''


The entry 6rx8 is ON HOLD  until Paper Publication
==EDDS lyase variant D290M/Y320M with bound fumarate==
<StructureSection load='6rx8' size='340' side='right'caption='[[6rx8]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rx8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RX8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=6rx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rx8 OCA], [http://pdbe.org/6rx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rx8 RCSB], [http://www.ebi.ac.uk/pdbsum/6rx8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rx8 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aspartic acid derivatives with branched N -alkyl or N -arylalkyl substituents are valuable precursors to artificial dipeptide sweeteners such as neotame and advantame, which have wide-ranging applications in the food industry. Despite the potential applications of these amino acid precursors to aspartame-based sweeteners, the development of a biocatalyst to synthesize these compounds in a single asymmetric step is an as yet unmet challenge. Herein we report an enantioselective biocatalytic synthesis of various difficult N -substituted aspartic acids including N -(3,3-dimethylbutyl)-L-aspartic acid and N -[3-(3-hydroxy-4-methoxyphenyl)propyl]-L-aspartic acid, precursors to neotame and advantame respectively, using an engineered variant of ethylenediamine- N , N '-disuccinic acid (EDDS) lyase from Chelativorans sp. BNC1. This engineered C-N lyase (mutant D290M/Y320M) displayed a remarkable 1140-fold increase in activity for the selective hydroamination of fumarate compared to that of the wild-type enzyme, which could be rationalized from the analysis of crystal structures. These results open up new opportunities to develop practical multienzymatic processes for the more sustainable and step-economic synthesis of an important class of food additives.


Authors: Grandi, E., Poelarends, G.J., Thunnissen, A.M.W.H.
Enantioselective Synthesis of Chiral Synthons for Artificial Dipeptide Sweeteners Catalyzed by an Engineered C-N Lyase.,Zhang J, Grandi E, Fu H, Saravanan T, Bothof L, Tepper PG, Thunnissen AWH, Poelarends GJ Angew Chem Int Ed Engl. 2019 Oct 18. doi: 10.1002/anie.201910704. PMID:31625664<ref>PMID:31625664</ref>


Description: EDDS lyase variant D290M/Y320M with bound fumarate
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Poelarends, G.J]]
<div class="pdbe-citations 6rx8" style="background-color:#fffaf0;"></div>
[[Category: Thunnissen, A.M.W.H]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Grandi, E]]
[[Category: Grandi, E]]
[[Category: Poelarends, G J]]
[[Category: Thunnissen, A M.W H]]
[[Category: Aspartase/fumarase]]
[[Category: C-n lyase]]
[[Category: Edds lyase]]
[[Category: Lyase]]
[[Category: Protein engineering]]
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