5NFQ

Novel epoxide hydrolases belonging to the alpha/beta hydrolases superfamily in metagenomes from hot environments

5NFQ の概要

• エントリーDOI: 10.2210/pdb5nfq/pdb
• 分子名称: epoxide hydrolase belonging to alpha/beta hydrolase superfamily metagenomic from Tomsk sample, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: epoxide hydrolases, metagenomics, industrial biocatalysis, stereoselectivity, protein structure, hydrolase
• 由来する生物種: metagenome
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35159.95

構造登録者

Ferrandi, E.E.,De Rose, S.A.,Sayer, C.,Guazzelli, E.,Marchesi, C.,Saneei, V.,Isupov, M.N.,Littlechild, J.A.,Monti, D. (登録日: 2017-03-15, 公開日: 2018-05-16, 最終更新日: 2024-05-08)

主引用文献

Ferrandi, E.E.,Sayer, C.,De Rose, S.A.,Guazzelli, E.,Marchesi, C.,Saneei, V.,Isupov, M.N.,Littlechild, J.A.,Monti, D.
New Thermophilic alpha / beta Class Epoxide Hydrolases Found in Metagenomes From Hot Environments.
Front Bioeng Biotechnol, 6:144-144, 2018

PubMed Abstract: Two novel epoxide hydrolases (EHs), Sibe-EH and CH65-EH, were identified in the metagenomes of samples collected in hot springs in Russia and China, respectively. The two α/β hydrolase superfamily fold enzymes were cloned, over-expressed in , purified and characterized. The new EHs were active toward a broad range of substrates, and in particular, Sibe-EH was excellent in the desymmetrization of -2,3-epoxybutane producing the (2,3)-diol product with exceeding 99%. Interestingly these enzymes also hydrolyse (4)-limonene-1,2-epoxide with Sibe-EH being specific for the isomer. The Sibe-EH is a monomer in solution whereas the CH65-EH is a dimer. Both enzymes showed high melting temperatures with the CH65-EH being the highest at 85°C retaining 80% of its initial activity after 3 h thermal treatment at 70°C making it the most thermal tolerant wild type epoxide hydrolase described. The Sibe-EH and CH65-EH have been crystallized and their structures determined to high resolution, 1.6 and 1.4 Å, respectively. The CH65-EH enzyme forms a dimer via its cap domains with different relative orientation of the monomers compared to previously described EHs. The entrance to the active site cavity is located in a different position in CH65-EH and Sibe-EH in relation to other known bacterial and mammalian EHs.

PubMed: 30386778
DOI: 10.3389/fbioe.2018.00144

実験手法

X-RAY DIFFRACTION (1.6 Å)