Biocatalysis is the chemical process through which enzymes or other biological catalysts perform reactions between organic components. Biocatalysis has been used widely in the pharmaceutical industry to make small molecule drugs.

Latest Research and Reviews

  • Research |

    The anthraquinone and enediyne halves of the antitumor antibiotic dynemicin A were previously thought to be assembled by two separate polyketide synthases (PKS). Now, a single polyketide synthase has been proposed to be responsible for their production, and a working model for their biosynthesis from a common octaketide intermediate has been suggested.

    • Douglas R. Cohen
    •  & Craig A. Townsend
  • Research |

    Biocatalysis, if selective, offers great potential for the well-controlled release of drugs and other payloads. Here, Minko and co-workers separate enzymes and substrates by loading them onto individual, polymer-coated nanoparticles, and show that a magnetic field switches on the catalytic activity by merging the polymer shells.

    • Andrey Zakharchenko
    • , Nataliia Guz
    • , Amine Mohamed Laradji
    • , Evgeny Katz
    •  & Sergiy Minko
  • Research |

    Peroxygenases can selectively functionalize organic compounds, but are sensitive to the co-substrate H2O2. Hollmann and co-workers show that water oxidation catalysts can provide a controlled supply of H2O2 to the enzyme in the presence of visible light, allowing efficient oxyfunctionalization without stoichiometric reductants.

    • Wuyuan Zhang
    • , Elena Fernández-Fueyo
    • , Yan Ni
    • , Morten van Schie
    • , Jenö Gacs
    • , Rokus Renirie
    • , Ron Wever
    • , Francesco G. Mutti
    • , Dörte Rother
    • , Miguel Alcalde
    •  & Frank Hollmann
  • Research | | open

    The biosynthetic pathway of fusidane-type antibiotics, such as helvolic acid, is largely undiscovered. Here, the authors investigate the biosynthesis of helvolic acid, thereby determining the sequence of the enzymatic reactions involved in the process and the intermediates formed.

    • Jian-Ming Lv
    • , Dan Hu
    • , Hao Gao
    • , Tetsuo Kushiro
    • , Takayoshi Awakawa
    • , Guo-Dong Chen
    • , Chuan-Xi Wang
    • , Ikuro Abe
    •  & Xin-Sheng Yao
  • Research |

    Within natural product biosynthetic pathways, nature has evolved highly selective catalysts capable of complexity generating reactions. Leveraging these tools, a suite of catalysts with complementary site- and stereoselectivity have been applied to the oxidative dearomatization of phenolic compounds, enabling one-pot transformations of phenols into various natural products.

    • Summer A. Baker Dockrey
    • , April L. Lukowski
    • , Marc R. Becker
    •  & Alison R. H. Narayan
  • Research | | open

    The eukaryotic release factor eRF1 is able to recognize the three stop codons UAA, UAG and UGA with high accuracy, while discriminating against near-cognate codons. Here the authors use molecular dynamic simulation to provide insight into the molecular basis behind the remarkable codon specificity of eRF1.

    • Christoffer Lind
    • , Ana Oliveira
    •  & Johan Åqvist

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