7CGS
Crystal endo-deglycosylated hydroxynitrile lyase isozyme 5 mutant L343F from Prunus communis
7CGS の概要
| エントリーDOI | 10.2210/pdb7cgs/pdb |
| 分子名称 | (R)-mandelonitrile lyase, FLAVIN-ADENINE DINUCLEOTIDE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| 機能のキーワード | hydroxynitrile lyase, flavin protein, lyase |
| 由来する生物種 | Prunus dulcis (Almond) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 62061.11 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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