6gio: Difference between revisions

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-'''Unreleased structure'''
-The entry 6gio is ON HOLD  until Paper Publication
+==Structure of Amino Acid Amide Racemase from Ochrobactrum anthropi==
+<StructureSection load='6gio' size='340' side='right'caption='[[6gio]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6gio]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GIO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GIO FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=6gio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gio OCA], [http://pdbe.org/6gio PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gio RCSB], [http://www.ebi.ac.uk/pdbsum/6gio PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gio ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The kinetic resolution of amino acid esters (AAEs) is a useful synthetic strategy for the preparation of single-enantiomer amino acids. The development of an enzymatic dynamic kinetic resolution (DKR) process for AAEs, which would give a theoretical yield of 100 % of the enantiopure product, would require an amino acid ester racemase (AAER); however, no such enzyme has been described. We have identified low AAER activity of 15 U mg(-1) in a homologue of a PLP-dependent alpha-amino -caprolactam racemase (ACLR) from Ochrobactrum anthropi. We have determined the structure of this enzyme, OaACLR, to a resolution of 1.87 A and, by using structure-guided saturation mutagenesis, in combination with a colorimetric screen for AAER activity, we have identified a mutant, L293C, in which the promiscuous AAER activity of this enzyme towards l-phenylalanine methyl ester is improved 3.7-fold.
-Authors: Frese, A., Grogan, G.
+An Aminocaprolactam Racemase from Ochrobactrum anthropi with Promiscuous Amino Acid Ester Racemase Activity.,Frese A, Barrass SV, Sutton PW, Adams JP, Grogan G Chembiochem. 2018 Jun 13. doi: 10.1002/cbic.201800265. PMID:29897155<ref>PMID:29897155</ref>
-Description: Structure of Amino Acid Amide Racemase from Ochrobactrum anthropi
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6gio" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Frese, A]]
 [[Category: Grogan, G]]
+[[Category: Amino acid]]
+[[Category: Amino acid amide]]
+[[Category: Amino acid ester]]
+[[Category: Isomerase]]
+[[Category: Plp]]
+[[Category: Racemase]]