Structure-Guided Immobilization of an Evolved Unspecific Peroxygenase.
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SUBMITTER: Molina-Espeja P
PROVIDER: S-EPMC6480235 | biostudies-literature | 2019 Apr
REPOSITORIES: biostudies-literature
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Structure-Guided Immobilization of an Evolved Unspecific Peroxygenase.
Molina-Espeja Patricia P Santos-Moriano Paloma P García-Ruiz Eva E Ballesteros Antonio A Plou Francisco J FJ Alcalde Miguel M
International journal of molecular sciences 20190402 7
Unspecific peroxygenases (UPOs) are highly promiscuous biocatalyst with self-sufficient mono(per)oxygenase activity. A laboratory-evolved UPO secreted by yeast was covalently immobilized in activated carriers through one-point attachment. In order to maintain the desired orientation without compromising the enzyme's activity, the S221C mutation was introduced at the surface of the enzyme, enabling a single disulfide bridge to be established between the support and the protein. Fluorescence confo ...[more]
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2023-11-18 | GSE246134 | GEO