4a6g

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(New page: '''Unreleased structure''' The entry 4a6g is ON HOLD Authors: Baxter, S., Royer, S., Grogan, G., Holt-Tiffin, K.E., Taylor, I.N., Fotheringham, I.G., Campopiano, D.J. Description: N-ac...)
Current revision (11:20, 20 December 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 4a6g is ON HOLD
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==N-acyl amino acid racemase from Amycalotopsis sp. Ts-1-60: G291D- F323Y mutant in complex with N-acetyl methionine==
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<StructureSection load='4a6g' size='340' side='right'caption='[[4a6g]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4a6g]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4A6G FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.71&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AME:N-ACETYLMETHIONINE'>AME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a6g OCA], [https://pdbe.org/4a6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a6g RCSB], [https://www.ebi.ac.uk/pdbsum/4a6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a6g ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NSAR_AMYSP NSAR_AMYSP] Acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of N-succinyl-phenylglycine and N-succinyl-methionine (PubMed:14705949, PubMed:24955846). Can catalyze the racemization of a broad range of N-acylamino acids, including N-acetyl-D/L-methionine, N-propionyl-D/L-methionine, N-butyryl-D/L-methionine and N-chloroacetyl-L-valine (PubMed:7766084, PubMed:10194342, PubMed:14705949, PubMed:23130969). Also converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:10194342, PubMed:14705949, PubMed:24955846). Catalyzes both N-succinylamino acid racemization and OSB synthesis at equivalent rates (PubMed:14705949, PubMed:24955846). NSAR is probably the biological function of this enzyme (Probable).<ref>PMID:10194342</ref> <ref>PMID:14705949</ref> <ref>PMID:23130969</ref> <ref>PMID:24955846</ref> <ref>PMID:7766084</ref> <ref>PMID:16740275</ref> <ref>PMID:24955846</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Baxter, S., Royer, S., Grogan, G., Holt-Tiffin, K.E., Taylor, I.N., Fotheringham, I.G., Campopiano, D.J.
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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>
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Description: N-acyl amino acid racemase from Amycalotopsis sp. Ts-1-60: G291D-F323Y mutant in complex with N-acetyl methionine
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4a6g" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Amycolatopsis sp]]
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[[Category: Large Structures]]
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[[Category: Baxter S]]
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[[Category: Campopiano DJ]]
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[[Category: Fotheringham IG]]
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[[Category: Grogan G]]
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[[Category: Holt-Tiffin KE]]
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[[Category: Royer S]]
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[[Category: Taylor IN]]

Current revision

N-acyl amino acid racemase from Amycalotopsis sp. Ts-1-60: G291D- F323Y mutant in complex with N-acetyl methionine

PDB ID 4a6g

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