Journal
ACS CATALYSIS
Volume 11, Issue 15, Pages 9168-9203Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.1c00759
Keywords
flavin-dependent enzyme; monooxygenase; unspecific peroxygenase; P450; hydroxylation; biocatalysis; oxyfunctionalization
Categories
Funding
- Friedrich-Naumann-Stiftung fur die Freiheit
- Bundesministerium fur Bildung und Forschung (Biotechnologie 2020+ Strukturvorhaben: Leibniz Research Cluster) [031A360B]
- Landesgraduiertenforderung Sachsen-Anhalt
- National Key Research and Development Program of China [2019YFA0905100]
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The enzymatic hydroxylation of activated and nonactivated sp(3)-carbons is challenging in organic synthesis, but nature provides a variety of enzymes with catalytic versatility to tackle this task. Different enzymes have distinct specificity in substrate scope, selectivity, activity, stability, and catalytic cycle, and factors such as heterologous production, crystal structure availability, enzyme engineering potential, and substrate promiscuity play crucial roles in the applicability of these biocatalysts.
Enzymatic hydroxylation of activated and nonactivated sp(3)-carbons attracts keen interest from the chemistry community as it is one of the most challenging tasks in organic synthesis. Nature provides a vast number of enzymes with an enormous catalytic versatility to fulfill this task. Given that those very different enzymes have a distinct specificity in substrate scope, selectivity, activity, stability, and catalytic cycle, it is interesting to outline similarities and differences. In this Review, we intend to delineate which enzymes possess considerable advantages within specific issues. Heterologous production, crystal structure availability, enzyme engineering potential, and substrate promiscuity are essential factors for the applicability of these biocatalysts.
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