6gio
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Amino Acid Amide Racemase from Ochrobactrum anthropi== | |
| + | <StructureSection load='6gio' size='340' side='right'caption='[[6gio]], [[Resolution|resolution]] 1.87Å' 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6gio" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Frese, A]] | [[Category: Frese, A]] | ||
[[Category: Grogan, G]] | [[Category: Grogan, G]] | ||
| + | [[Category: Amino acid]] | ||
| + | [[Category: Amino acid amide]] | ||
| + | [[Category: Amino acid ester]] | ||
| + | [[Category: Isomerase]] | ||
| + | [[Category: Plp]] | ||
| + | [[Category: Racemase]] | ||
Current revision
Structure of Amino Acid Amide Racemase from Ochrobactrum anthropi
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