5NFQ
Novel epoxide hydrolases belonging to the alpha/beta hydrolases superfamily in metagenomes from hot environments
Summary for 5NFQ
| Entry DOI | 10.2210/pdb5nfq/pdb |
| Descriptor | epoxide hydrolase belonging to alpha/beta hydrolase superfamily metagenomic from Tomsk sample, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (6 entities in total) |
| Functional Keywords | epoxide hydrolases, metagenomics, industrial biocatalysis, stereoselectivity, protein structure, hydrolase |
| Biological source | metagenome |
| Total number of polymer chains | 1 |
| Total formula weight | 35159.95 |
| Authors | Ferrandi, E.E.,De Rose, S.A.,Sayer, C.,Guazzelli, E.,Marchesi, C.,Saneei, V.,Isupov, M.N.,Littlechild, J.A.,Monti, D. (deposition date: 2017-03-15, release date: 2018-05-16, Last modification date: 2024-05-08) |
| Primary citation | 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 Cited by 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: 30386778DOI: 10.3389/fbioe.2018.00144 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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