View source for 3zvh


==Methylaspartate ammonia lyase from Clostridium tetanomorphum mutant Q73A==
<StructureSection load='3zvh' size='340' side='right'caption='[[3zvh]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zvh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_tetanomorphum Clostridium tetanomorphum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZVH 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]] 1.99&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</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=3zvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zvh OCA], [https://pdbe.org/3zvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zvh RCSB], [https://www.ebi.ac.uk/pdbsum/3zvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zvh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MAAL_CLOTT MAAL_CLOTT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The redesign of enzymes to produce catalysts for a predefined transformation remains a major challenge in protein engineering. Here, we describe the structure-based engineering of methylaspartate ammonia lyase (which in nature catalyses the conversion of 3-methylaspartate to ammonia and 2-methylfumarate) to accept a variety of substituted amines and fumarates and catalyse the asymmetric synthesis of aspartic acid derivatives. We obtained two single-active-site mutants, one exhibiting a wide nucleophile scope including structurally diverse linear and cyclic alkylamines and one with broad electrophile scope including fumarate derivatives with alkyl, aryl, alkoxy, aryloxy, alkylthio and arylthio substituents at the C2 position. Both mutants have an enlarged active site that accommodates the new substrates while retaining the high stereo- and regioselectivity of the wild-type enzyme. As an example, we demonstrate a highly enantio- and diastereoselective synthesis of threo-3-benzyloxyaspartate (an important inhibitor of neuronal excitatory glutamate transporters in the brain).

Engineering methylaspartate ammonia lyase for the asymmetric synthesis of unnatural amino acids.,Raj H, Szymanski W, de Villiers J, Rozeboom HJ, Veetil VP, Reis CR, de Villiers M, Dekker FJ, de Wildeman S, Quax WJ, Thunnissen AM, Feringa BL, Janssen DB, Poelarends GJ Nat Chem. 2012 Apr 29;4(6):478-84. doi: 10.1038/nchem.1338. PMID:22614383<ref>PMID:22614383</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zvh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium tetanomorphum]]
[[Category: Large Structures]]
[[Category: Dekker FJ]]
[[Category: Feringa BL]]
[[Category: Janssen DB]]
[[Category: Poelarends GJ]]
[[Category: Quax WJ]]
[[Category: Raj H]]
[[Category: Reis CR]]
[[Category: Rozeboom HJ]]
[[Category: Szymanski W]]
[[Category: Thunnissen AMWH]]
[[Category: Veetil VP]]
[[Category: De Villiers J]]
[[Category: De Villiers M]]
[[Category: De Wildeman S]]