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| | <StructureSection load='6skx' size='340' side='right'caption='[[6skx]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='6skx' size='340' side='right'caption='[[6skx]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6skx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspfu Aspfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SKX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6skx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus_Af293 Aspergillus fumigatus Af293]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SKX FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AFUA_5G01250 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=330879 ASPFU])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-hydroxyisobutyrate_dehydrogenase 3-hydroxyisobutyrate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.31 1.1.1.31] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6skx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6skx OCA], [https://pdbe.org/6skx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6skx RCSB], [https://www.ebi.ac.uk/pdbsum/6skx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6skx ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6skx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6skx OCA], [https://pdbe.org/6skx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6skx RCSB], [https://www.ebi.ac.uk/pdbsum/6skx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6skx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q4WDZ8_ASPFU Q4WDZ8_ASPFU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 3-hydroxyisobutyrate dehydrogenase]] | + | [[Category: Aspergillus fumigatus Af293]] |
| - | [[Category: Aspfu]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Grogan, G]] | + | [[Category: Grogan G]] |
| - | [[Category: Mangas-Sanchez, J]] | + | [[Category: Mangas-Sanchez J]] |
| - | [[Category: Sharma, M]] | + | [[Category: Sharma M]] |
| - | [[Category: Turner, N J]] | + | [[Category: Turner NJ]] |
| - | [[Category: Amine]]
| + | |
| - | [[Category: Imine]]
| + | |
| - | [[Category: Nadph]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
Q4WDZ8_ASPFU
Publication Abstract from PubMed
Chiral primary amines are important intermediates in the synthesis of pharmaceutical compounds. Fungal reductive aminases (RedAms) are NADPH-dependent dehydrogenases that catalyse reductive amination of a range of ketones with short-chain primary amines supplied in an equimolar ratio to give corresponding secondary amines. Herein we describe structural and biochemical characterisation as well as synthetic applications of two RedAms from Neosartorya spp. (NfRedAm and NfisRedAm) that display a distinctive activity amongst fungal RedAms, namely a superior ability to use ammonia as the amine partner. Using these enzymes, we demonstrate the synthesis of a broad range of primary amines, with conversions up to >97% and excellent enantiomeric excess. Temperature dependent studies showed that these homologues also possess greater thermal stability compared to other enzymes within this family. Their synthetic applicability is further demonstrated by the production of several primary and secondary amines with turnover numbers (TN) up to 14 000 as well as continous flow reactions, obtaining chiral amines such as (R)-2-aminohexane in space time yields up to 8.1 g L(-1) h(-1). The remarkable features of NfRedAm and NfisRedAm highlight their potential for wider synthetic application as well as expanding the biocatalytic toolbox available for chiral amine synthesis.
Asymmetric synthesis of primary amines catalyzed by thermotolerant fungal reductive aminases.,Mangas-Sanchez J, Sharma M, Cosgrove SC, Ramsden JI, Marshall JR, Thorpe TW, Palmer RB, Grogan G, Turner NJ Chem Sci. 2020 May 5;11(19):5052-5057. doi: 10.1039/d0sc02253e. PMID:34122962[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mangas-Sanchez J, Sharma M, Cosgrove SC, Ramsden JI, Marshall JR, Thorpe TW, Palmer RB, Grogan G, Turner NJ. Asymmetric synthesis of primary amines catalyzed by thermotolerant fungal reductive aminases. Chem Sci. 2020 May 5;11(19):5052-5057. doi: 10.1039/d0sc02253e. PMID:34122962 doi:http://dx.doi.org/10.1039/d0sc02253e
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