7CGS
Crystal endo-deglycosylated hydroxynitrile lyase isozyme 5 mutant L343F from Prunus communis
Summary for 7CGS
| Entry DOI | 10.2210/pdb7cgs/pdb |
| Descriptor | (R)-mandelonitrile lyase, FLAVIN-ADENINE DINUCLEOTIDE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | hydroxynitrile lyase, flavin protein, lyase |
| Biological source | Prunus dulcis (Almond) |
| Total number of polymer chains | 1 |
| Total formula weight | 62061.11 |
| Authors | Zheng, Y.C.,Li, F.L. (deposition date: 2020-07-02, release date: 2021-04-21, Last modification date: 2024-11-20) |
| Primary citation | Zheng, Y.C.,Ding, L.Y.,Jia, Q.,Lin, Z.,Hong, R.,Yu, H.L.,Xu, J.H. A High-Throughput Screening Method for the Directed Evolution of Hydroxynitrile Lyase towards Cyanohydrin Synthesis. Chembiochem, 22:996-1000, 2021 Cited by PubMed Abstract: 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. PubMed: 33146944DOI: 10.1002/cbic.202000658 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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