5E4D

Hydroxynitrile lyase from the fern Davallia tyermanii in complex with benzoic acid

5E4D の概要

• エントリーDOI: 10.2210/pdb5e4d/pdb
• 関連するPDBエントリー: 5E46
• 分子名称: Hydroxynitrile lyase, BENZOIC ACID (3 entities in total)
• 機能のキーワード: hydroxynitrile lyase, fern, benzoic acid, lyase
• 由来する生物種: Davallia tyermannii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47008.43

構造登録者

Pavkov-Keller, T.,Diepold, M.,Gruber, K. (登録日: 2015-10-05, 公開日: 2016-10-12, 最終更新日: 2024-01-10)

主引用文献

Lanfranchi, E.,Pavkov-Keller, T.,Koehler, E.M.,Diepold, M.,Steiner, K.,Darnhofer, B.,Hartler, J.,Van Den Bergh, T.,Joosten, H.J.,Gruber-Khadjawi, M.,Thallinger, G.G.,Birner-Gruenberger, R.,Gruber, K.,Winkler, M.,Glieder, A.
Enzyme discovery beyond homology: a unique hydroxynitrile lyase in the Bet v1 superfamily.
Sci Rep, 7:46738-46738, 2017

PubMed Abstract: Homology and similarity based approaches are most widely used for the identification of new enzymes for biocatalysis. However, they are not suitable to find truly novel scaffolds with a desired function and this averts options and diversity. Hydroxynitrile lyases (HNLs) are an example of non-homologous isofunctional enzymes for the synthesis of chiral cyanohydrins. Due to their convergent evolution, finding new representatives is challenging. Here we show the discovery of unique HNL enzymes from the fern Davallia tyermannii by coalescence of transcriptomics, proteomics and enzymatic screening. It is the first protein with a Bet v1-like protein fold exhibiting HNL activity, and has a new catalytic center, as shown by protein crystallography. Biochemical properties of D. tyermannii HNLs open perspectives for the development of a complementary class of biocatalysts for the stereoselective synthesis of cyanohydrins. This work shows that systematic integration of -omics data facilitates discovery of enzymes with unpredictable sequences and helps to extend our knowledge about enzyme diversity.

PubMed: 28466867
DOI: 10.1038/srep46738

実験手法

X-RAY DIFFRACTION (1.85 Å)