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Publication Abstract from PubMed

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, contains the same 8alpha-N3-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.

Discovery, biocatalytic exploration and structural analysis of a 4-ethylphenol oxidase from Gulosibacter chungangensis.,Laura A, Gran-Scheuch A, Guo Y, Trajkovic M, Saifuddin M, Fraaije MW, Mattevi A Chembiochem. 2021 Sep 15. doi: 10.1002/cbic.202100457. PMID:34523783^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.