8S4P

Crystal structure of an Ene-reductase from Penicillium steckii

8S4P の概要

• エントリーDOI: 10.2210/pdb8s4p/pdb
• 分子名称: NADH:flavin oxidoreductase/NADH oxidase N-terminal domain-containing protein, FLAVIN MONONUCLEOTIDE, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: wild-type, twinning, oxidoreductase
• 由来する生物種: Penicillium steckii
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 366545.58

構造登録者

Rozeboom, H.J.,Fraaije, M.W. (登録日: 2024-02-22, 公開日: 2025-03-05, 最終更新日: 2025-04-30)

主引用文献

Damada, P.H.,Rozeboom, H.J.,Fraaije, M.W.
Recombinant Production and Characterization of Six Ene-reductases from Penicillium steckii.
Chembiochem, 26:e202401007-e202401007, 2025

PubMed Abstract: Fungi, known for their adaptability, are valuable sources of enzymes, making them promising for biocatalyst discovery. This study explored Penicillium steckii, primarily recognized for secondary meta-bolite production, as a source of ene-reductases (ERs), which reduce α,β-unsaturated compounds. Eleven ER-encoding genes were iden-tified, and plasmids for Escherichia coli expression were generated. Six ERs (PsOYE1-6) were successfully produced and purified as soluble FMN-containing proteins. Sequence analysis classified them into Class II (PsOYE1, PsOYE4, PsOYE6), Class III (PsOYE2, PsOYE3), and Class V (PsOYE5) OYEs. All were active on p-benzo-quinone and maleimide, with varying activity on other substrates. Their pH optima ranged from 6 to 7, and they exhibited moderate thermostability (35-50 °C). PsOYE2 was crystallized, and its 2.3 Å structure revealed a stable dimer with a unique active site. PsOYE3, PsOYE4, and PsOYE5 were tested for R-carvone conversion and stereoselectivity, all favouring one diastereomer. These fungal ERs expand the enzymatic toolbox for biocatalysis, emphasizing the need for tailored strategies based on specific applications.

PubMed: 40072226
DOI: 10.1002/cbic.202401007

実験手法

X-RAY DIFFRACTION (2.29 Å)