Discovery, Biocatalytic Exploration and Structural Analysis of a 4-Ethylphenol Oxidase from Gulosibacter chungangensis

Autor: Alejandro Gran-Scheuch, Mohammad Saifuddin, Milos Trajkovic, Alvigini Laura, Marco W. Fraaije, Andrea Mattevi, Yiming Guo
Přispěvatelé: Biotechnology
Rok vydání: 2021
Předmět:
Zdroj: ChemBioChem. WILEY-V C H VERLAG GMBH
ChemBioChem 2021, 22
'ChemBioChem ', vol: 22, pages: 3225-3233 (2021)
ISSN: 1439-7633
1439-4227
Popis: The vanillyl-alcohol oxidase (VAO) family is a rich source of biocatalysts for the oxidative bioconversion of phenolic compounds. Through genome mining and sequence comparisons, we found that several family members lack a generally conserved catalytic aspartate. This finding led us to study a VAO-homolog featuring a glutamate residue in place of the common aspartate. This 4-ethylphenol oxidase from Gulosibacter chungangensis (Gc4EO) shares 42 % sequence identity with VAO from Penicillium simplicissimum, contains the same 8 alpha-N-3-histidyl-bound FAD and uses oxygen as electron acceptor. However, Gc4EO features a distinct substrate scope and product specificity as it is primarily effective in the dehydrogenation of para-substituted phenols with little generation of hydroxylated products. The three-dimensional structure shows that the characteristic glutamate side chain creates a closely packed environment that may limit water accessibility and thereby protect from hydroxylation. With its high thermal stability, well defined structural properties and high expression yields, Gc4EO may become a catalyst of choice for the specific dehydrogenation of phenolic compounds bearing small substituents.
Databáze: OpenAIRE