5AIH

Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomic libraries. CH55-sample-Native

5AIH の概要

• エントリーDOI: 10.2210/pdb5aih/pdb
• 関連するPDBエントリー: 5AIF 5AIG 5AII
• 分子名称: LIMONENE-1,2-EPOXIDE HYDROLASE, DIMETHYL SULFOXIDE, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: UNIDENTIFIED
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28896.88

構造登録者

Ferrandi, E.,Sayer, C.,Isupov, M.N.,Annovazzi, C.,Marchesi, C.,Iacobone, G.,Peng, X.,Bonch-Osmolovskaya, E.,Wohlgemuth, R.,Littlechild, J.A.,Montia, D. (登録日: 2015-02-13, 公開日: 2015-06-17, 最終更新日: 2024-01-10)

主引用文献

Ferrandi, E.E.,Sayer, C.,Isupov, M.N.,Annovazzi, C.,Marchesi, C.,Iacobone, G.,Peng, X.,Bonch-Osmolovskaya, E.,Wohlgemuth, R.,Littlechild, J.A.,Montia, D.
Discovery and Characterization of Thermophilic Limonene-1,2-Epoxide Hydrolases from Hot Spring Metagenomic Libraries
FEBS J., 282:2879-, 2015

PubMed Abstract: The epoxide hydrolases (EHs) represent an attractive option for the synthesis of chiral epoxides and 1,2-diols which are valuable building blocks for the synthesis of several pharmaceutical compounds. A metagenomic approach has been used to identify two new members of the atypical EH limonene-1,2-epoxide hydrolase (LEH) family of enzymes. These two LEHs (Tomsk-LEH and CH55-LEH) show EH activities towards different epoxide substrates, differing in most cases from those previously identified for Rhodococcus erythropolis (Re-LEH) in terms of stereoselectivity. Tomsk-LEH and CH55-LEH, both from thermophilic sources, have higher optimal temperatures and apparent melting temperatures than Re-LEH. The new LEH enzymes have been crystallized and their structures solved to high resolution in the native form and in complex with the inhibitor valpromide for Tomsk-LEH and poly(ethylene glycol) for CH55-LEH. The structural analysis has provided insights into the LEH mechanism, substrate specificity and stereoselectivity of these new LEH enzymes, which has been supported by mutagenesis studies.

PubMed: 26032250
DOI: 10.1111/FEBS.13328

実験手法

X-RAY DIFFRACTION (1.42 Å)