Stable and Functionally Diverse Versatile Peroxidases Designed Directly from Sequences.

ABSTRACT: White-rot fungi secrete a repertoire of high-redox potential oxidoreductases to efficiently decompose lignin. Of these enzymes, versatile peroxidases (VPs) are the most promiscuous biocatalysts. VPs are attractive enzymes for research and industrial use but their recombinant production is extremely challenging. To date, only a single VP has been structurally characterized and optimized for recombinant functional expression, stability, and activity. Computational enzyme optimization methods can be applied to many enzymes in parallel but they require accurate structures. Here, we demonstrate that model structures computed by deep-learning-based ab initio structure prediction methods are reliable starting points for one-shot PROSS stability-design calculations. Four designed VPs encodi

SUBMITTER: Barber-Zucker S 

PROVIDER: S-EPMC8895400 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature