6gio: Difference between revisions
New page: '''Unreleased structure''' The entry 6gio is ON HOLD until Paper Publication Authors: Frese, A., Grogan, G. Description: Structure of Amino Acid Amide Racemase from Ochrobactrum anthro... |
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==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]] | |||
Latest revision as of 09:35, 27 March 2019
Structure of Amino Acid Amide Racemase from Ochrobactrum anthropiStructure of Amino Acid Amide Racemase from Ochrobactrum anthropi
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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