4a6g: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[ | ==N-acyl amino acid racemase from Amycalotopsis sp. Ts-1-60: G291D- F323Y mutant in complex with N-acetyl methionine== | ||
<StructureSection load='4a6g' size='340' side='right' caption='[[4a6g]], [[Resolution|resolution]] 2.71Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4a6g]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_sp. Amycolatopsis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A6G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A6G FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AME:N-ACETYLMETHIONINE'>AME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sjb|1sjb]], [[1sja|1sja]], [[1sjc|1sjc]], [[1sjd|1sjd]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/o-succinylbenzoate_synthase o-succinylbenzoate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.113 4.2.1.113] </span></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=4a6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a6g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a6g RCSB], [http://www.ebi.ac.uk/pdbsum/4a6g PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Using directed evolution, a variant N-acetyl amino acid racemase (NAAAR G291D/F323Y) has been developed with up to 6-fold higher activity than the wild-type on a range of N-acetylated amino acids. The variant has been coupled with an enantiospecific acylase to give a preparative scale dynamic kinetic resolution which allows 98% conversion of N-acetyl-dl-allylglycine into d-allylglycine in 18 h at high substrate concentrations (50 g L(-1)). This is the first example of NAAAR operating under conditions which would allow it to be successfully used on an industrial scale for the production of enantiomerically pure alpha-amino acids. X-ray crystal analysis of the improved NAAAR variant allowed a comparison with the wild-type enzyme. We postulate that a network of novel interactions that result from the introduction of the two side chains is the source of improved catalytic performance. | |||
An Improved Racemase/Acylase Biotransformation for the Preparation of Enantiomerically Pure Amino Acids.,Baxter S, Royer S, Grogan G, Brown F, Holt-Tiffin KE, Taylor IN, Fotheringham IG, Campopiano DJ J Am Chem Soc. 2012 Nov 15. PMID:23130969<ref>PMID:23130969</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Amycolatopsis sp | [[Category: Amycolatopsis sp]] | ||
[[Category: O-succinylbenzoate synthase]] | [[Category: O-succinylbenzoate synthase]] | ||
[[Category: Baxter, S | [[Category: Baxter, S]] | ||
[[Category: Campopiano, D J | [[Category: Campopiano, D J]] | ||
[[Category: Fotheringham, I G | [[Category: Fotheringham, I G]] | ||
[[Category: Grogan, G | [[Category: Grogan, G]] | ||
[[Category: Holt-Tiffin, K E | [[Category: Holt-Tiffin, K E]] | ||
[[Category: Royer, S | [[Category: Royer, S]] | ||
[[Category: Taylor, I N | [[Category: Taylor, I N]] | ||
[[Category: Biocatalysis]] | [[Category: Biocatalysis]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
