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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Structure of a soluble epoxide hydrolase identified in Trichoderma reesei

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Autor(es):
Wilson, Carolina ; De Oliveira, Gabriel S. ; Adriani, Patricia P. ; Chambergo, Felipe S. ; Dias, Marcio V. B.
Número total de Autores: 5
Tipo de documento: Artigo Científico
Fonte: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS; v. 1865, n. 8, p. 1039-1045, AUG 2017.
Citações Web of Science: 3
Resumo

Epoxide hydrolases (EHs) are enzymes that have high biotechnological interest for the fine and transformation industry. Several of these enzymes have enantioselectivity, which allows their application in the separation of enantiomeric mixtures of epoxide substrates. Although two different families of EHs have been described, those that have the alpha/beta-hidrolase fold are the most explored for biotechnological purpose. These enzymes are functionally very well studied, but only few members have three-dimensional structures characterised. Recently, a new EH from the filamentous fungi Trichoderma reseei (TrEH) has been discovered and functionally studied. This enzyme does not have high homology to any other EH structure and have an enatiopreference for (S)-( - ) isomers. Herein we described the crystallographic structure of TrEH at 1.7 angstrom resolution, which reveals features of its tertiary structure and active site. TrEH has a similar fold to the other soluble epoxide hydrolases and has the two characteristic hydrolase and cap domains. The enzyme is predominantly monomeric in solution and has also been crystallised as a monomer in the asymmetric unit. Although the catalytic residues are conserved, several other residues of the catalytic groove are not, and might be involved in the specificity for substrates and in the enantioselectivy of this enzyme. In addition, the determination of the crystallographic structure of TrEH might contribute to the rational site direct mutagenesis to generate an even more stable enzyme with higher efficiency to be used in biotechnological purposes. (AU)

Processo FAPESP: 15/03329-9 - Clonagem e caracterização de enzimas epóxido hidrolases de Trichoderma reesei
Beneficiário:Gabriel Stephani de Oliveira
Linha de fomento: Bolsas no Brasil - Doutorado Direto
Processo FAPESP: 10/15971-3 - Caracterização estrutural de enzimas envolvidas em vias de biossíntese de antibióticos com interesse biotecnológico
Beneficiário:Marcio Vinicius Bertacine Dias
Linha de fomento: Auxílio à Pesquisa - Apoio a Jovens Pesquisadores
Processo FAPESP: 15/09188-8 - Biossíntese de antibióticos poliéteres e aminoglicosídeos: investigação estrutural de enzimas não usuais ou com aplicabilidade em biologia sintética
Beneficiário:Marcio Vinicius Bertacine Dias
Linha de fomento: Auxílio à Pesquisa - Regular
Processo FAPESP: 14/24107-1 - Estudo e caracterização de enzimas oxidases produzidas por fungos filamentosos
Beneficiário:Felipe Santiago Chambergo Alcalde
Linha de fomento: Auxílio à Pesquisa - Programa BIOEN - Regular