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 |

    Thebaine, a naturally occurring opiate, is used to produce drugs that treat opiate addiction, but it must be processed using toxic reactants that produce harmful waste. In this study, the authors probed an opium-processing waste stream and identified a versatile enzyme that can be used instead.

    • M. M. Augustin
    • , J. M. Augustin
    • , J. R. Brock
    •  & T. M. Kutchan
  • Research | | open

    Respiratory complex I plays a central role in cellular energy metabolism coupling NADH oxidation to proton translocation. Here, the authors report the structure of the electron input part of Aquifex aeolicus complex I at up to 1.8 Å resolution with bound substrates in the reduced and oxidized states.

    • Marius Schulte
    • , Klaudia Frick
    • , Emmanuel Gnandt
    • , Sascha Jurkovic
    • , Sabrina Burschel
    • , Ramona Labatzke
    • , Karoline Aierstock
    • , Dennis Fiegen
    • , Daniel Wohlwend
    • , Stefan Gerhardt
    • , Oliver Einsle
    •  & Thorsten Friedrich
  • Research |

    Detailed knowledge about its catalytic process is important for exploiting [Fe]-hydrogenase—an enzyme that cleaves and produces H2—for technological purposes. This study presents an atomic-resolution crystal structure of a substrate-bound closed active form of the enzyme and a precise catalytic cycle.

    • Gangfeng Huang
    • , Tristan Wagner
    • , Matthew D. Wodrich
    • , Kenichi Ataka
    • , Eckhard Bill
    • , Ulrich Ermler
    • , Xile Hu
    •  & Seigo Shima
    Nature Catalysis 2, 537-543
  • Research |

    DNAzymes are attractive catalysts for biomedical and biotechnological applications, but their catalytic mechanism remained obscure. This work investigates the detailed reaction mechanism of RNA ligation catalysed by the 9DB1 DNAzyme, revealing that it resembles those of natural protein enzymes.

    • Juan Aranda
    • , Montserrat Terrazas
    • , Hansel Gómez
    • , Núria Villegas
    •  & Modesto Orozco
    Nature Catalysis 2, 544-552
  • Research | | open

    The UbiD-UbiX decarboxylase system is required for the biosynthesis of quinone cofactors. Here, the authors combine structural and biochemical analyses to elucidate the UbiX reaction mechanism, showing that it resembles the mode of action of class I terpene cyclases.

    • Stephen A. Marshall
    • , Karl A. P. Payne
    • , Karl Fisher
    • , Mark D. White
    • , Aisling Ní Cheallaigh
    • , Arune Balaikaite
    • , Stephen E. J. Rigby
    •  & David Leys

News and Comment

  • News and Views |

    A synthetic DNA enzyme catalyses the formation of a native phosphodiester bond between two RNA fragments, but the molecular details of the mechanism remained elusive. Research using computational and biochemical approaches now suggests that the DNA enzyme recruits two magnesium ions to assist in the catalysis of RNA ligation.

    • Claudia Höbartner
    Nature Catalysis 2, 483-484
  • News and Views |

    Hydrogenases are very powerful biocatalysts for dihydrogen cleavage. Now, X-ray crystallography shows how [Fe]-hydrogenase requires ligand exchanges at the metal centre and significant molecular motions to open and close its active site to effectively transfer a hydride to an electrophilic organic substrate.

    • Yvain Nicolet
    Nature Catalysis 2, 481-482
  • News and Views |

    The biological functions of glycan motifs such as the Lewis blood antigens are often defined by their precise multivalent presentation on complex glycoconjugates, making synthesis particularly challenging. Access to a number of positionally defined Lewis motifs on natural polysaccharide scaffolds has now been achieved using bacterial glycosyltransferases.

    • Kun Huang
    •  & Sabine L Flitsch
    Nature Catalysis 2, 479-480