Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–11 of 11 results
Advanced filters: Author: Dominic J. Campopiano Clear advanced filters

  • Catalysis has been a standard topic taught in university chemistry courses over the past century yet biocatalysis — or enzyme catalysis — has only recently been integrated into standard chemistry curriculum despite its broad applicability in industry. In a fourth year undergraduate research project course, students can now choose to explore interesting chemical transformations in the lab using biocatalysis instead of traditional synthetic chemistry approaches.

    • Lisa Kennedy
    • Dominic J. Campopiano
    Comments & Opinion
    Nature Chemistry
    Volume: 18, P: 1-3

  • Structures of pimeloyl-CoA synthetase (BioW) provide insights into its catalytic mechanism and how it selects the correct length of dicarboxylic acid substrate, guiding engineering to make the enzyme capable of producing alternative CoA products.

    • Menglu Wang
    • Lucile Moynié
    • Dominic J Campopiano
    Research
    Nature Chemical Biology
    Volume: 13, P: 660-667

  • Elucidation of the bacterial ceramide biosynthetic pathway reveals that it likely evolved independently from the eukaryotic pathway, as bacteria lack homologs for many of the eukaryotic enzymes and the reactions occur in a different order.

    • Gabriele Stankeviciute
    • Peijun Tang
    • Eric A. Klein
    Research
    Nature Chemical Biology
    Volume: 18, P: 305-312

  • Converting simple building blocks into enantiopure amines is an important synthetic transformation. Now, a biocatalyst has been discovered that catalyses two reductive steps within a single active site, and can synthesize a range of amine targets from ene–one starting materials.

    • Michael A. Herrera
    • Dominic J. Campopiano
    News & Views
    Nature Synthesis
    Volume: 1, P: 420-421

  • The composition of a dynamic combinatorial library can be altered by adding a target molecule that either stabilizes (or destabilizes) one or more of its members. The range of reversible chemical reactions compatible with biological targets such as proteins is somewhat limited, but now it has been shown that aniline-catalysed acylhydrazone formation is effective in this context.

    • Venugopal T. Bhat
    • Anne M. Caniard
    • Michael F. Greaney
    Research
    Nature Chemistry
    Volume: 2, P: 490-497

  • The pathways responsible for inositol lipid production in human gut Bacteroides are characterized and these lipids are important for capsule expression and antimicrobial peptide resistance in vitro and colonization in vivo.

    • Stacey L. Heaver
    • Henry H. Le
    • Ruth E. Ley
    ResearchOpen Access
    Nature Microbiology
    Volume: 7, P: 986-1000

  • The α-oxoamine synthases (AOSes) are a class of pyridoxal 5’-phosphate-dependent enzymes that catalyse Claisen-like condensation of amino acids with an acyl-CoA thioester to generate α-aminoketones, however, their application in chemoenzymatic synthesis remains limited due to the substrate specificity. Here, the authors report the structure-guided engineering of thermostable AOS from Thermus thermophilus to expand the range of amino acids and simplify N-acetylcysteamine acyl-thioester substrates.

    • Ben Ashley
    • Sam Mathew
    • Dominic J. Campopiano
    ResearchOpen Access
    Communications Chemistry
    Volume: 8, P: 1-12