View source for 6rxa


==EDDS lyase variant D290M/Y320M with bound formate==
<StructureSection load='6rxa' size='340' side='right'caption='[[6rxa]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rxa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chelativorans_sp._BNC1 Chelativorans sp. BNC1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RXA 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]] 1.44&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[https://proteopedia.org/fgij/fg.htm?mol=6rxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rxa OCA], [https://pdbe.org/6rxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rxa RCSB], [https://www.ebi.ac.uk/pdbsum/6rxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rxa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q11KV9_CHESB Q11KV9_CHESB] 
<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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6rxa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chelativorans sp. BNC1]]
[[Category: Large Structures]]
[[Category: Grandi E]]
[[Category: Poelarends GJ]]
[[Category: Thunnissen AMWH]]