4.8 Review

Enzymatic Hydroxylations of sp3-Carbons

期刊

ACS CATALYSIS
卷 11, 期 15, 页码 9168-9203

出版社

AMER CHEMICAL SOC
DOI: 10.1021/acscatal.1c00759

关键词

flavin-dependent enzyme; monooxygenase; unspecific peroxygenase; P450; hydroxylation; biocatalysis; oxyfunctionalization

资金

  1. Friedrich-Naumann-Stiftung fur die Freiheit
  2. Bundesministerium fur Bildung und Forschung (Biotechnologie 2020+ Strukturvorhaben: Leibniz Research Cluster) [031A360B]
  3. Landesgraduiertenforderung Sachsen-Anhalt
  4. National Key Research and Development Program of China [2019YFA0905100]

向作者/读者索取更多资源

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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