5AIH

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

Summary for 5AIH

• Entry DOI: 10.2210/pdb5aih/pdb
• Related: 5AIF 5AIG 5AII
• Descriptor: LIMONENE-1,2-EPOXIDE HYDROLASE, DIMETHYL SULFOXIDE, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: hydrolase
• Biological source: UNIDENTIFIED
• Total number of polymer chains: 2
• Total formula weight: 28896.88

Authors

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. (deposition date: 2015-02-13, release date: 2015-06-17, Last modification date: 2024-01-10)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.42 Å)