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An epoxide hydrolase from endophytic Streptomyces shows unique structural features and wide biocatalytic activity

Tormet-González, Gabriela D., Wilson, Carolina, de Oliveira, Gabriel Stephani, dos Santos, Jademilson Celestino, Gonzaga de Oliveira, Luciana and Dias, Marcio Vinicius Bertacine 2020. An epoxide hydrolase from endophytic Streptomyces shows unique structural features and wide biocatalytic activity. Acta Crystallographica Section D: Structural Biology 76 (9) , pp. 868-875. 10.1107/S2059798320010402

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The genus Streptomyces is characterized by the production of a wide variety of secondary metabolites with remarkable biological activities and broad antibiotic capabilities. The presence of an unprecedented number of genes encoding hydrolytic enzymes with industrial appeal such as epoxide hydrolases (EHs) reveals its resourceful microscopic machinery. The whole-genome sequence of Streptomyces sp. CBMAI 2042, an endophytic actinobacterium isolated from Citrus sinensis branches, was explored by genome mining, and a putative α/β-epoxide hydrolase named B1EPH2 and encoded by 344 amino acids was selected for functional and structural studies. The crystal structure of B1EPH2 was obtained at a resolution of 2.2 Å and it was found to have a similar fold to other EHs, despite its hexameric quaternary structure, which contrasts with previously solved dimeric and monomeric EH structures. While B1EPH2 has a high sequence similarity to EHB from Mycobacterium tuberculosis, its cavity is similar to that of human EH. A group of 12 aromatic and aliphatic racemic epoxides were assayed to determine the activity of B1EPH2; remarkably, this enzyme was able to hydrolyse all the epoxides to the respective 1,2-diols, indicating a wide-range substrate scope acceptance. Moreover, the (R)- and (S)-enantiomers of styrene oxide, epichlorohydrin and 1,2-epoxybutane were used to monitor enantiopreference. Taken together, the functional and structural analyses indicate that this enzyme is an attractive biocatalyst for future biotechnological applications.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Chemistry
Additional Information: Attribution 4.0 International (CC BY 4.0)
Publisher: International Union of Crystallography
ISSN: 2059-7983
Date of First Compliant Deposit: 4 November 2022
Date of Acceptance: 28 July 2020
Last Modified: 23 May 2023 14:28

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