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

ABSTRACT: 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 quaterna

SUBMITTER: Tormet-Gonzalez GD 

PROVIDER: S-EPMC7466753 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature