7cgs: Difference between revisions
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==Crystal endo-deglycosylated hydroxynitrile lyase isozyme 5 mutant L343F from Prunus communis== | ==Crystal endo-deglycosylated hydroxynitrile lyase isozyme 5 mutant L343F from Prunus communis== | ||
<StructureSection load='7cgs' size='340' side='right'caption='[[7cgs]]' scene=''> | <StructureSection load='7cgs' size='340' side='right'caption='[[7cgs]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CGS FirstGlance]. <br> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CGS FirstGlance]. <br> | ||
</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=7cgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cgs OCA], [https://pdbe.org/7cgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cgs RCSB], [https://www.ebi.ac.uk/pdbsum/7cgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cgs ProSAT]</span></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]] 1.6Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCN:BICINE'>BCN</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=7cgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cgs OCA], [https://pdbe.org/7cgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cgs RCSB], [https://www.ebi.ac.uk/pdbsum/7cgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cgs ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Chiral cyanohydrins are useful intermediates in the pharmaceutical and agricultural industries. In nature, hydroxynitrile lyases (HNLs) are a kind of elegant tool for enantioselective hydrocyanation of carbonyl compounds. However, currently available methods for demonstrating hydrocyanation are still stalled at precise, but low-throughput, GC or HPLC analyses. Herein, we report a chromogenic high-throughput screening (HTS) method that is feasible for the cyanohydrin synthesis reaction. This method was highly anti-interference and sensitive, and could be used to directly profile the substrate scope of HNLs either in cell-free extract or fermentation clear broth. This HTS method was also validated by generating new variants of PcHNL5 that presented higher catalytic efficiency and stronger acidic tolerance in variant libraries. | |||
A High-Throughput Screening Method for the Directed Evolution of Hydroxynitrile Lyase towards Cyanohydrin Synthesis.,Zheng YC, Ding LY, Jia Q, Lin Z, Hong R, Yu HL, Xu JH Chembiochem. 2021 Mar 16;22(6):996-1000. doi: 10.1002/cbic.202000658. Epub 2021, Jan 12. PMID:33146944<ref>PMID:33146944</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7cgs" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 06:10, 21 November 2024
Crystal endo-deglycosylated hydroxynitrile lyase isozyme 5 mutant L343F from Prunus communis
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