An epoxide hydrolase from endophytic Streptomycess hows unique structural features and wide biocatalytic activity

Author(s)

Tormet-Gonzalez, Gabriela D. ; Wilson, Carolina ; de Oliveira, Gabriel Stephani ; dos Santos, Jademilson Celestino ; de Oliveira, Luciana G. ; Dias, Marcio Vinicius Bertacine

• Document type: Journal article
• Source: ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY; v. 76, p. 8-pg., 2020-09-01.

Abstract

The genusStreptomycesis 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 ofStreptomycessp. CBMAI 2042, an endophytic actinobacterium isolated fromCitrus sinensisbranches, was explored by genome mining, and a putative alpha/beta-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 angstrom 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 fromMycobacterium 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. (AU)

• FAPESP's process: 19/10564-5 - Assessing the beneficial aspects of endophytic actinobacteria: expanding the Brazilian microorganisms genome codified natural products
• Grantee: Luciana Gonzaga de Oliveira
• Support Opportunities: Regular Research Grants
• FAPESP's process: 18/00351-1 - Applied structural biology involved in the biosynthesis of natural products: biotechnolgical aplications and study of unusual molecular reactions
• Grantee: Marcio Vinicius Bertacine Dias
• Support Opportunities: Regular Research Grants
• FAPESP's process: 15/09188-8 - Biosynthesis of polyether and aminoglycoside antibiotics: structural investigation of unusual enzymes or with synthetic biology applicability
• Grantee: Marcio Vinicius Bertacine Dias
• Support Opportunities: Regular Research Grants
• FAPESP's process: 11/06209-3 - Enzymes in asymmetric synthesis: directed evolution of Rhodotorula glutinis and Pichia stipitis epoxide hydrolases
• Grantee: Luciana Gonzaga de Oliveira
• Support Opportunities: Regular Research Grants
• FAPESP's process: 14/50249-8 - Green chemistry: sustainable synthetic methods employing benign solvents, safer reagents, and bio-renewable feedstock
• Grantee: Arlene Gonçalves Corrêa
• Support Opportunities: Research Grants - Research Centers in Engineering Program
• FAPESP's process: 10/15971-3 - Structural characterization of enzymes from antibiotic biosynthetic pathways with biotechnological interest
• Grantee: Marcio Vinicius Bertacine Dias
• Support Opportunities: Research Grants - Young Investigators Grants
• FAPESP's process: 13/26242-0 - Design of new antibiotics based in the fragment based drug discovery technique from the inhibition of vitamin biosynthesis in Mycobacterium tuberculosis
• Grantee: Jademilson Celestino dos Santos
• Support Opportunities: Scholarships in Brazil - Post-Doctoral
• FAPESP's process: 14/12727-5 - Genome mining in Streptomyces
• Grantee: Luciana Gonzaga de Oliveira
• Support Opportunities: Regular Research Grants