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5NFQ

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

Summary for 5NFQ
Entry DOI10.2210/pdb5nfq/pdb
Descriptorepoxide hydrolase belonging to alpha/beta hydrolase superfamily metagenomic from Tomsk sample, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (6 entities in total)
Functional Keywordsepoxide hydrolases, metagenomics, industrial biocatalysis, stereoselectivity, protein structure, hydrolase
Biological sourcemetagenome
Total number of polymer chains1
Total formula weight35159.95
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 citationFerrandi, 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: 30386778
DOI: 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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